PubMed:20484118 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":424,"end":443},"obj":"https://glytoucan.org/Structures/Glycans/G64581RP"},{"id":"T2","span":{"begin":445,"end":453},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T3","span":{"begin":445,"end":453},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"},{"id":"T4","span":{"begin":1039,"end":1047},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T5","span":{"begin":1039,"end":1047},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":424,"end":443},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":445,"end":453},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":1039,"end":1047},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G64581RP"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G89565QL"},{"id":"A3","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G49108TO"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G89565QL"},{"id":"A5","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G49108TO"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

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{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":238,"end":241},"obj":"http://www.uniprot.org/uniprot/P26678"},{"id":"T2","span":{"begin":501,"end":504},"obj":"http://www.uniprot.org/uniprot/P26678"},{"id":"T3","span":{"begin":643,"end":646},"obj":"http://www.uniprot.org/uniprot/P26678"},{"id":"T4","span":{"begin":659,"end":662},"obj":"http://www.uniprot.org/uniprot/P26678"},{"id":"T5","span":{"begin":697,"end":700},"obj":"http://www.uniprot.org/uniprot/P26678"},{"id":"T6","span":{"begin":972,"end":975},"obj":"http://www.uniprot.org/uniprot/P26678"},{"id":"T7","span":{"begin":1026,"end":1029},"obj":"http://www.uniprot.org/uniprot/P26678"},{"id":"T8","span":{"begin":1118,"end":1121},"obj":"http://www.uniprot.org/uniprot/P26678"},{"id":"T9","span":{"begin":1275,"end":1278},"obj":"http://www.uniprot.org/uniprot/P26678"},{"id":"T10","span":{"begin":1609,"end":1612},"obj":"http://www.uniprot.org/uniprot/P26678"},{"id":"T11","span":{"begin":1784,"end":1787},"obj":"http://www.uniprot.org/uniprot/P26678"},{"id":"T12","span":{"begin":1048,"end":1059},"obj":"http://www.uniprot.org/uniprot/Q99484"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":1048,"end":1059},"obj":"http://www.uniprot.org/uniprot/P38649"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":580,"end":582},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/13893"},{"id":"T2","span":{"begin":910,"end":913},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/604139"},{"id":"T3","span":{"begin":922,"end":927},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T4","span":{"begin":1014,"end":1019},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T5","span":{"begin":1071,"end":1073},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/13893"},{"id":"T6","span":{"begin":1249,"end":1251},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/13893"},{"id":"T7","span":{"begin":1398,"end":1401},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/604139"},{"id":"T8","span":{"begin":1410,"end":1415},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T9","span":{"begin":1765,"end":1774},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/127244"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":28,"end":43},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T2","span":{"begin":293,"end":308},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T3","span":{"begin":953,"end":968},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T4","span":{"begin":1099,"end":1114},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T5","span":{"begin":1663,"end":1678},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T6","span":{"begin":148,"end":150},"obj":"http://purl.obolibrary.org/obo/GO_0033968"},{"id":"T7","span":{"begin":243,"end":252},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T8","span":{"begin":1788,"end":1798},"obj":"http://purl.obolibrary.org/obo/GO_0065007"},{"id":"T9","span":{"begin":1039,"end":1059},"obj":"http://purl.obolibrary.org/obo/GO_0097363"},{"id":"T10","span":{"begin":1410,"end":1429},"obj":"http://purl.obolibrary.org/obo/GO_0001775"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":285,"end":288},"obj":"http://purl.obolibrary.org/obo/GO_0005790"},{"id":"T2","span":{"begin":346,"end":349},"obj":"http://purl.obolibrary.org/obo/GO_0005790"},{"id":"T3","span":{"begin":686,"end":689},"obj":"http://purl.obolibrary.org/obo/GO_0005790"},{"id":"T4","span":{"begin":945,"end":948},"obj":"http://purl.obolibrary.org/obo/GO_0005790"},{"id":"T5","span":{"begin":1091,"end":1094},"obj":"http://purl.obolibrary.org/obo/GO_0005790"},{"id":"T6","span":{"begin":366,"end":377},"obj":"http://purl.obolibrary.org/obo/GO_0005737"},{"id":"T7","span":{"begin":922,"end":927},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T8","span":{"begin":1014,"end":1019},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T9","span":{"begin":1410,"end":1415},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T10","span":{"begin":1039,"end":1059},"obj":"http://purl.obolibrary.org/obo/GO_0017122"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":1206,"end":1211},"obj":"http://purl.obolibrary.org/obo/UBERON_0000948"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"Allie","denotations":[{"id":"SS1_20484118_1_0","span":{"begin":119,"end":160},"obj":"expanded"},{"id":"SS2_20484118_1_0","span":{"begin":162,"end":169},"obj":"abbr"},{"id":"SS1_20484118_2_0","span":{"begin":223,"end":236},"obj":"expanded"},{"id":"SS2_20484118_2_0","span":{"begin":238,"end":241},"obj":"abbr"},{"id":"SS1_20484118_3_0","span":{"begin":415,"end":443},"obj":"expanded"},{"id":"SS2_20484118_3_0","span":{"begin":445,"end":453},"obj":"abbr"}],"relations":[{"id":"AE1_20484118_1_0","pred":"abbreviatedTo","subj":"SS1_20484118_1_0","obj":"SS2_20484118_1_0"},{"id":"AE1_20484118_2_0","pred":"abbreviatedTo","subj":"SS1_20484118_2_0","obj":"SS2_20484118_2_0"},{"id":"AE1_20484118_3_0","pred":"abbreviatedTo","subj":"SS1_20484118_3_0","obj":"SS2_20484118_3_0"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":366,"end":377},"obj":"http://edamontology.org/topic_0616"},{"id":"T2","span":{"begin":390,"end":398},"obj":"http://edamontology.org/topic_0078"},{"id":"T3","span":{"begin":543,"end":550},"obj":"http://edamontology.org/topic_3678"},{"id":"T4","span":{"begin":580,"end":602},"obj":"http://edamontology.org/topic_3557"},{"id":"T5","span":{"begin":1030,"end":1034},"obj":"http://edamontology.org/topic_3512"},{"id":"T6","span":{"begin":1060,"end":1065},"obj":"http://edamontology.org/topic_0659"},{"id":"T7","span":{"begin":1249,"end":1271},"obj":"http://edamontology.org/topic_3557"},{"id":"T8","span":{"begin":1297,"end":1305},"obj":"http://edamontology.org/topic_3318"},{"id":"T9","span":{"begin":1306,"end":1317},"obj":"http://edamontology.org/topic_0602"},{"id":"T10","span":{"begin":1334,"end":1342},"obj":"http://edamontology.org/topic_0078"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":354,"end":362},"obj":"http://edamontology.org/data_1756"},{"id":"T2","span":{"begin":390,"end":398},"obj":"http://edamontology.org/format_1208"},{"id":"T3","span":{"begin":390,"end":398},"obj":"http://edamontology.org/data_1467"},{"id":"T4","span":{"begin":505,"end":516},"obj":"http://edamontology.org/operation_0004"},{"id":"T5","span":{"begin":1334,"end":1342},"obj":"http://edamontology.org/data_1467"},{"id":"T6","span":{"begin":1334,"end":1342},"obj":"http://edamontology.org/format_1208"},{"id":"T7","span":{"begin":1591,"end":1595},"obj":"http://edamontology.org/data_0006"},{"id":"T8","span":{"begin":1686,"end":1696},"obj":"http://edamontology.org/operation_3465"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":208,"end":221},"obj":"HP_0001371"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":424,"end":443},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":447,"end":453},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T3","span":{"begin":1041,"end":1047},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"DisGeNET5_gene_disease","denotations":[{"id":"20484118-0#14#27#gene5350","span":{"begin":14,"end":27},"obj":"gene5350"},{"id":"20484118-0#81#104#diseaseC0853897","span":{"begin":81,"end":104},"obj":"diseaseC0853897"},{"id":"20484118-12#45#48#gene5350","span":{"begin":1784,"end":1787},"obj":"gene5350"},{"id":"20484118-12#162#170#diseaseC0011847","span":{"begin":1901,"end":1909},"obj":"diseaseC0011847"},{"id":"20484118-12#162#170#diseaseC0011849","span":{"begin":1901,"end":1909},"obj":"diseaseC0011849"}],"relations":[{"id":"14#27#gene535081#104#diseaseC0853897","pred":"associated_with","subj":"20484118-0#14#27#gene5350","obj":"20484118-0#81#104#diseaseC0853897"},{"id":"45#48#gene5350162#170#diseaseC0011847","pred":"associated_with","subj":"20484118-12#45#48#gene5350","obj":"20484118-12#162#170#diseaseC0011847"},{"id":"45#48#gene5350162#170#diseaseC0011849","pred":"associated_with","subj":"20484118-12#45#48#gene5350","obj":"20484118-12#162#170#diseaseC0011849"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":193,"end":207},"obj":"http://purl.obolibrary.org/obo/MAT_0000453"},{"id":"T2","span":{"begin":201,"end":207},"obj":"http://purl.obolibrary.org/obo/MAT_0000025"},{"id":"T3","span":{"begin":1206,"end":1211},"obj":"http://purl.obolibrary.org/obo/MAT_0000036"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":148,"end":150},"obj":"https://acgg.asia/db/lfdb/LfDB0227"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":567,"end":575},"obj":"id"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":445,"end":453},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"PD-GlycoEpitope-B_T3","span":{"begin":1039,"end":1047},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G69371PB\""},{"id":"GlycanIUPAC_T2","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G04439TG\""},{"id":"GlycanIUPAC_T3","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G01418RR\""},{"id":"GlycanIUPAC_T4","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G98605AX\""},{"id":"GlycanIUPAC_T5","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G24282OK\""},{"id":"GlycanIUPAC_T6","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G55879EK\""},{"id":"GlycanIUPAC_T7","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G12116BQ\""},{"id":"GlycanIUPAC_T8","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G54590PA\""},{"id":"GlycanIUPAC_T9","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G31652HG\""},{"id":"GlycanIUPAC_T10","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G15155WL\""},{"id":"GlycanIUPAC_T11","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G52301ZX\""},{"id":"GlycanIUPAC_T12","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G04075BC\""},{"id":"GlycanIUPAC_T13","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G40829OF\""},{"id":"GlycanIUPAC_T14","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G29274DI\""},{"id":"GlycanIUPAC_T15","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G50601AY\""},{"id":"GlycanIUPAC_T16","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G52865ZM\""},{"id":"GlycanIUPAC_T17","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G73633QJ\""},{"id":"GlycanIUPAC_T18","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G33319MN\""},{"id":"GlycanIUPAC_T19","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G94717IQ\""},{"id":"GlycanIUPAC_T20","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G50452ZL\""},{"id":"GlycanIUPAC_T21","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G90753WM\""},{"id":"GlycanIUPAC_T22","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G27898GL\""},{"id":"GlycanIUPAC_T23","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G03827YH\""},{"id":"GlycanIUPAC_T24","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G64500BA\""},{"id":"GlycanIUPAC_T25","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G89743XV\""},{"id":"GlycanIUPAC_T26","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G62576QG\""},{"id":"GlycanIUPAC_T27","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G70212CQ\""},{"id":"GlycanIUPAC_T28","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G74708KP\""},{"id":"GlycanIUPAC_T29","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G02394PC\""},{"id":"GlycanIUPAC_T30","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G57814GP\""},{"id":"GlycanIUPAC_T31","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G81521LC\""},{"id":"GlycanIUPAC_T32","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G42918SL\""},{"id":"GlycanIUPAC_T33","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G95238FE\""},{"id":"GlycanIUPAC_T34","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G28403TD\""},{"id":"GlycanIUPAC_T35","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G30379UC\""},{"id":"GlycanIUPAC_T36","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G83583TH\""},{"id":"GlycanIUPAC_T37","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G59548EJ\""},{"id":"GlycanIUPAC_T38","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G47410OV\""},{"id":"GlycanIUPAC_T39","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G88663EK\""},{"id":"GlycanIUPAC_T40","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G90684PG\""},{"id":"GlycanIUPAC_T41","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G44881OW\""},{"id":"GlycanIUPAC_T42","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G54691YO\""},{"id":"GlycanIUPAC_T43","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G19289PT\""},{"id":"GlycanIUPAC_T44","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G23779KC\""},{"id":"GlycanIUPAC_T45","span":{"begin":350,"end":353},"obj":"\"http://rdf.glycoinfo.org/glycan/G94729UX\""},{"id":"GlycanIUPAC_T46","span":{"begin":350,"end":353},"obj"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":{"begin":447,"end":453},"obj":"\"http://rdf.glycoinfo.org/glycan/G40745NH\""},{"id":"GlycanIUPAC_T229","span":{"begin":1041,"end":1047},"obj":"\"http://rdf.glycoinfo.org/glycan/G40745NH\""},{"id":"GlycanIUPAC_T230","span":{"begin":447,"end":453},"obj":"\"http://rdf.glycoinfo.org/glycan/G54496YV\""},{"id":"GlycanIUPAC_T231","span":{"begin":1041,"end":1047},"obj":"\"http://rdf.glycoinfo.org/glycan/G54496YV\""},{"id":"GlycanIUPAC_T232","span":{"begin":447,"end":453},"obj":"\"http://rdf.glycoinfo.org/glycan/G62953SQ\""},{"id":"GlycanIUPAC_T233","span":{"begin":1041,"end":1047},"obj":"\"http://rdf.glycoinfo.org/glycan/G62953SQ\""},{"id":"GlycanIUPAC_T234","span":{"begin":447,"end":453},"obj":"\"http://rdf.glycoinfo.org/glycan/G70070AY\""},{"id":"GlycanIUPAC_T235","span":{"begin":1041,"end":1047},"obj":"\"http://rdf.glycoinfo.org/glycan/G70070AY\""},{"id":"GlycanIUPAC_T236","span":{"begin":447,"end":453},"obj":"\"http://rdf.glycoinfo.org/glycan/G78792WC\""},{"id":"GlycanIUPAC_T237","span":{"begin":1041,"end":1047},"obj":"\"http://rdf.glycoinfo.org/glycan/G78792WC\""},{"id":"GlycanIUPAC_T238","span":{"begin":447,"end":453},"obj":"\"http://rdf.glycoinfo.org/glycan/G25238AV\""},{"id":"GlycanIUPAC_T239","span":{"begin":1041,"end":1047},"obj":"\"http://rdf.glycoinfo.org/glycan/G25238AV\""},{"id":"GlycanIUPAC_T240","span":{"begin":447,"end":453},"obj":"\"http://rdf.glycoinfo.org/glycan/G40510DP\""},{"id":"GlycanIUPAC_T241","span":{"begin":1041,"end":1047},"obj":"\"http://rdf.glycoinfo.org/glycan/G40510DP\""},{"id":"GlycanIUPAC_T242","span":{"begin":447,"end":453},"obj":"\"http://rdf.glycoinfo.org/glycan/G61120TK\""},{"id":"GlycanIUPAC_T243","span":{"begin":1041,"end":1047},"obj":"\"http://rdf.glycoinfo.org/glycan/G61120TK\""},{"id":"GlycanIUPAC_T244","span":{"begin":447,"end":453},"obj":"\"http://rdf.glycoinfo.org/glycan/G41342KV\""},{"id":"GlycanIUPAC_T245","span":{"begin":1041,"end":1047},"obj":"\"http://rdf.glycoinfo.org/glycan/G41342KV\""},{"id":"GlycanIUPAC_T246","span":{"begin":447,"end":453},"obj":"\"http://rdf.glycoinfo.org/glycan/G90703NA\""},{"id":"GlycanIUPAC_T247","span":{"begin":1041,"end":1047},"obj":"\"http://rdf.glycoinfo.org/glycan/G90703NA\""},{"id":"GlycanIUPAC_T248","span":{"begin":447,"end":453},"obj":"\"http://rdf.glycoinfo.org/glycan/G01591HR\""},{"id":"GlycanIUPAC_T249","span":{"begin":1041,"end":1047},"obj":"\"http://rdf.glycoinfo.org/glycan/G01591HR\""},{"id":"GlycanIUPAC_T250","span":{"begin":447,"end":453},"obj":"\"http://rdf.glycoinfo.org/glycan/G56520XN\""},{"id":"GlycanIUPAC_T251","span":{"begin":1041,"end":1047},"obj":"\"http://rdf.glycoinfo.org/glycan/G56520XN\""},{"id":"GlycanIUPAC_T252","span":{"begin":447,"end":453},"obj":"\"http://rdf.glycoinfo.org/glycan/G81830JX\""},{"id":"GlycanIUPAC_T253","span":{"begin":1041,"end":1047},"obj":"\"http://rdf.glycoinfo.org/glycan/G81830JX\""},{"id":"GlycanIUPAC_T254","span":{"begin":910,"end":913},"obj":"\"http://rdf.glycoinfo.org/glycan/G02780QX\""},{"id":"GlycanIUPAC_T255","span":{"begin":1398,"end":1401},"obj":"\"http://rdf.glycoinfo.org/glycan/G02780QX\""},{"id":"GlycanIUPAC_T256","span":{"begin":910,"end":913},"obj":"\"http://rdf.glycoinfo.org/glycan/G18425DX\""},{"id":"GlycanIUPAC_T257","span":{"begin":1398,"end":1401},"obj":"\"http://rdf.glycoinfo.org/glycan/G18425DX\""},{"id":"GlycanIUPAC_T258","span":{"begin":910,"end":913},"obj":"\"http://rdf.glycoinfo.org/glycan/G18630JE\""},{"id":"GlycanIUPAC_T259","span":{"begin":1398,"end":1401},"obj":"\"http://rdf.glycoinfo.org/glycan/G18630JE\""},{"id":"GlycanIUPAC_T260","span":{"begin":910,"end":913},"obj":"\"http://rdf.glycoinfo.org/glycan/G01004IT\""},{"id":"GlycanIUPAC_T261","span":{"begin":1398,"end":1401},"obj":"\"http://rdf.glycoinfo.org/glycan/G01004IT\""},{"id":"GlycanIUPAC_T262","span":{"begin":910,"end":913},"obj":"\"http://rdf.glycoinfo.org/glycan/G87301QZ\""},{"id":"GlycanIUPAC_T263","span":{"begin":1398,"end":1401},"obj":"\"http://rdf.glycoinfo.org/glycan/G87301QZ\""},{"id":"GlycanIUPAC_T264","span":{"begin":910,"end":913},"obj":"\"http://rdf.glycoinfo.org/glycan/G39790GW\""},{"id":"GlycanIUPAC_T265","span":{"begin":1398,"end":1401},"obj":"\"http://rdf.glycoinfo.org/glycan/G39790GW\""},{"id":"GlycanIUPAC_T266","span":{"begin":910,"end":913},"obj":"\"http://rdf.glycoinfo.org/glycan/G42928BB\""},{"id":"GlycanIUPAC_T267","span":{"begin":1398,"end":1401},"obj":"\"http://rdf.glycoinfo.org/glycan/G42928BB\""},{"id":"GlycanIUPAC_T268","span":{"begin":910,"end":913},"obj":"\"http://rdf.glycoinfo.org/glycan/G51134HC\""},{"id":"GlycanIUPAC_T269","span":{"begin":1398,"end":1401},"obj":"\"http://rdf.glycoinfo.org/glycan/G51134HC\""},{"id":"GlycanIUPAC_T270","span":{"begin":910,"end":913},"obj":"\"http://rdf.glycoinfo.org/glycan/G68183GR\""},{"id":"GlycanIUPAC_T271","span":{"begin":1398,"end":1401},"obj":"\"http://rdf.glycoinfo.org/glycan/G68183GR\""},{"id":"GlycanIUPAC_T272","span":{"begin":910,"end":913},"obj":"\"http://rdf.glycoinfo.org/glycan/G46883FA\""},{"id":"GlycanIUPAC_T273","span":{"begin":1398,"end":1401},"obj":"\"http://rdf.glycoinfo.org/glycan/G46883FA\""},{"id":"GlycanIUPAC_T274","span":{"begin":910,"end":913},"obj":"\"http://rdf.glycoinfo.org/glycan/G54702VY\""},{"id":"GlycanIUPAC_T275","span":{"begin":1398,"end":1401},"obj":"\"http://rdf.glycoinfo.org/glycan/G54702VY\""}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":1206,"end":1211},"obj":"http://purl.obolibrary.org/obo/UBERON_0000948"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":193,"end":207},"obj":"Body_part"},{"id":"T2","span":{"begin":1206,"end":1211},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000453"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000036"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":90,"end":104},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0001638"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":90,"end":104},"obj":"Disease"},{"id":"T2","span":{"begin":1901,"end":1909},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0004994"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0005015"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":445,"end":453},"obj":"Glycan"},{"id":"T2","span":{"begin":1039,"end":1047},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GlyCosmos15-HP","denotations":[{"id":"T1","span":{"begin":90,"end":104},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0001638"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":90,"end":104},"obj":"Disease"},{"id":"T2","span":{"begin":1901,"end":1909},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0004994"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0005015"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":517,"end":520},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":992,"end":1007},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":1238,"end":1242},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10114"},{"id":"A2","pred":"db_id","subj":"T1","obj":"10116"},{"id":"A3","pred":"db_id","subj":"T3","obj":"10029"},{"id":"A4","pred":"db_id","subj":"T4","obj":"10114"},{"id":"A5","pred":"db_id","subj":"T4","obj":"10116"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":527,"end":541},"obj":"Cell"},{"id":"T2","span":{"begin":743,"end":757},"obj":"Cell"},{"id":"T3","span":{"begin":1375,"end":1389},"obj":"Cell"},{"id":"T4","span":{"begin":1498,"end":1512},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000746"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000746"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000746"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000746"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":138,"end":147},"obj":"Body_part"},{"id":"T2","span":{"begin":193,"end":207},"obj":"Body_part"},{"id":"T4","span":{"begin":366,"end":377},"obj":"Body_part"},{"id":"T5","span":{"begin":527,"end":541},"obj":"Body_part"},{"id":"T6","span":{"begin":743,"end":757},"obj":"Body_part"},{"id":"T7","span":{"begin":1008,"end":1013},"obj":"Body_part"},{"id":"T8","span":{"begin":1206,"end":1211},"obj":"Body_part"},{"id":"T12","span":{"begin":1375,"end":1389},"obj":"Body_part"},{"id":"T13","span":{"begin":1498,"end":1512},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0007361"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0001133"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002349"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0005737"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL_0000746"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL_0000746"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0000992"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0000948"},{"id":"A9","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0007100"},{"id":"A10","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0015228"},{"id":"A11","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0015230"},{"id":"A12","pred":"uberon_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/CL_0000746"},{"id":"A13","pred":"uberon_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/CL_0000746"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":193,"end":207},"obj":"Body_part"},{"id":"T2","span":{"begin":1206,"end":1211},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000453"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000036"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":105},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":106,"end":222},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":223,"end":309},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":310,"end":542},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":543,"end":739},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":740,"end":928},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":929,"end":988},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":989,"end":1171},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1172,"end":1243},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1244,"end":1390},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1391,"end":1584},"obj":"Sentence"},{"id":"TextSentencer_T12","span":{"begin":1585,"end":1738},"obj":"Sentence"},{"id":"TextSentencer_T13","span":{"begin":1739,"end":1910},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":105},"obj":"Sentence"},{"id":"T2","span":{"begin":106,"end":222},"obj":"Sentence"},{"id":"T3","span":{"begin":223,"end":309},"obj":"Sentence"},{"id":"T4","span":{"begin":310,"end":542},"obj":"Sentence"},{"id":"T5","span":{"begin":543,"end":739},"obj":"Sentence"},{"id":"T6","span":{"begin":740,"end":928},"obj":"Sentence"},{"id":"T7","span":{"begin":929,"end":988},"obj":"Sentence"},{"id":"T8","span":{"begin":989,"end":1171},"obj":"Sentence"},{"id":"T9","span":{"begin":1172,"end":1243},"obj":"Sentence"},{"id":"T10","span":{"begin":1244,"end":1390},"obj":"Sentence"},{"id":"T11","span":{"begin":1391,"end":1584},"obj":"Sentence"},{"id":"T12","span":{"begin":1585,"end":1738},"obj":"Sentence"},{"id":"T13","span":{"begin":1739,"end":1910},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":105},"obj":"Sentence"},{"id":"T2","span":{"begin":106,"end":222},"obj":"Sentence"},{"id":"T3","span":{"begin":223,"end":309},"obj":"Sentence"},{"id":"T4","span":{"begin":310,"end":542},"obj":"Sentence"},{"id":"T5","span":{"begin":543,"end":739},"obj":"Sentence"},{"id":"T6","span":{"begin":740,"end":928},"obj":"Sentence"},{"id":"T7","span":{"begin":929,"end":988},"obj":"Sentence"},{"id":"T8","span":{"begin":989,"end":1171},"obj":"Sentence"},{"id":"T9","span":{"begin":1172,"end":1243},"obj":"Sentence"},{"id":"T10","span":{"begin":1244,"end":1390},"obj":"Sentence"},{"id":"T11","span":{"begin":1391,"end":1584},"obj":"Sentence"},{"id":"T12","span":{"begin":1585,"end":1738},"obj":"Sentence"},{"id":"T13","span":{"begin":1739,"end":1910},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":105},"obj":"Sentence"},{"id":"T2","span":{"begin":106,"end":222},"obj":"Sentence"},{"id":"T3","span":{"begin":223,"end":309},"obj":"Sentence"},{"id":"T4","span":{"begin":310,"end":542},"obj":"Sentence"},{"id":"T5","span":{"begin":543,"end":739},"obj":"Sentence"},{"id":"T6","span":{"begin":740,"end":928},"obj":"Sentence"},{"id":"T7","span":{"begin":929,"end":988},"obj":"Sentence"},{"id":"T8","span":{"begin":989,"end":1171},"obj":"Sentence"},{"id":"T9","span":{"begin":1172,"end":1243},"obj":"Sentence"},{"id":"T10","span":{"begin":1244,"end":1390},"obj":"Sentence"},{"id":"T11","span":{"begin":1391,"end":1584},"obj":"Sentence"},{"id":"T12","span":{"begin":1585,"end":1738},"obj":"Sentence"},{"id":"T13","span":{"begin":1739,"end":1910},"obj":"Sentence"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":445,"end":453},"obj":"Glycan"},{"id":"T2","span":{"begin":1039,"end":1047},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":445,"end":453},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":1039,"end":1047},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0004"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":517,"end":520},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":992,"end":1007},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":1238,"end":1242},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10114"},{"id":"A2","pred":"db_id","subj":"T1","obj":"10116"},{"id":"A3","pred":"db_id","subj":"T3","obj":"10029"},{"id":"A4","pred":"db_id","subj":"T4","obj":"10114"},{"id":"A5","pred":"db_id","subj":"T4","obj":"10116"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":445,"end":453},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":1039,"end":1047},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0004"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":138,"end":147},"obj":"Body_part"},{"id":"T2","span":{"begin":193,"end":207},"obj":"Body_part"},{"id":"T4","span":{"begin":366,"end":377},"obj":"Body_part"},{"id":"T5","span":{"begin":527,"end":541},"obj":"Body_part"},{"id":"T6","span":{"begin":743,"end":757},"obj":"Body_part"},{"id":"T7","span":{"begin":1008,"end":1013},"obj":"Body_part"},{"id":"T8","span":{"begin":1206,"end":1211},"obj":"Body_part"},{"id":"T12","span":{"begin":1375,"end":1389},"obj":"Body_part"},{"id":"T13","span":{"begin":1498,"end":1512},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0007361"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0001133"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002349"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0005737"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL_0000746"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL_0000746"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0000992"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0000948"},{"id":"A9","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0007100"},{"id":"A10","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0015228"},{"id":"A11","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0015230"},{"id":"A12","pred":"uberon_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/CL_0000746"},{"id":"A13","pred":"uberon_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/CL_0000746"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":527,"end":541},"obj":"Cell"},{"id":"T2","span":{"begin":743,"end":757},"obj":"Cell"},{"id":"T3","span":{"begin":1375,"end":1389},"obj":"Cell"},{"id":"T4","span":{"begin":1498,"end":1512},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000746"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000746"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000746"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000746"}],"text":"Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy.\nCardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. Simultaneously, Ser(16)-phosphorylation of PLN was reduced. In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. The same results were observed in heart homogenates from diabetic rats. In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes."}