PubMed:24035784 JSONTXT

{"project":"GlyCosmos15-Species","denotations":[{"id":"40","span":{"begin":715,"end":718},"obj":"Species"},{"id":"42","span":{"begin":770,"end":773},"obj":"Species"},{"id":"44","span":{"begin":916,"end":921},"obj":"Species"}],"attributes":[{"id":"A40","pred":"db_id","subj":"40","obj":"10116"},{"id":"A42","pred":"db_id","subj":"42","obj":"10116"},{"id":"A44","pred":"db_id","subj":"44","obj":"9606"}],"text":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}

{"project":"PubMed_Structured_Abstracts","denotations":[{"id":"T1","span":{"begin":105,"end":906},"obj":"BACKGROUND"},{"id":"T2","span":{"begin":916,"end":1444},"obj":"METHODS"},{"id":"T3","span":{"begin":1454,"end":1870},"obj":"RESULTS"},{"id":"T4","span":{"begin":1893,"end":2018},"obj":"CONCLUSIONS"}],"text":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}

{"project":"Allie","denotations":[{"id":"SS1_24035784_2_0","span":{"begin":105,"end":135},"obj":"expanded"},{"id":"SS2_24035784_2_0","span":{"begin":137,"end":145},"obj":"abbr"},{"id":"SS1_24035784_3_0","span":{"begin":263,"end":296},"obj":"expanded"},{"id":"SS2_24035784_3_0","span":{"begin":298,"end":301},"obj":"abbr"},{"id":"SS1_24035784_3_1","span":{"begin":329,"end":372},"obj":"expanded"},{"id":"SS2_24035784_3_1","span":{"begin":374,"end":377},"obj":"abbr"},{"id":"SS1_24035784_8_0","span":{"begin":1076,"end":1087},"obj":"expanded"},{"id":"SS2_24035784_8_0","span":{"begin":1089,"end":1093},"obj":"abbr"},{"id":"SS1_24035784_9_0","span":{"begin":1166,"end":1177},"obj":"expanded"},{"id":"SS2_24035784_9_0","span":{"begin":1179,"end":1182},"obj":"abbr"},{"id":"SS1_24035784_11_0","span":{"begin":1402,"end":1436},"obj":"expanded"},{"id":"SS2_24035784_11_0","span":{"begin":1438,"end":1442},"obj":"abbr"}],"relations":[{"id":"AE1_24035784_2_0","pred":"abbreviatedTo","subj":"SS1_24035784_2_0","obj":"SS2_24035784_2_0"},{"id":"AE1_24035784_3_0","pred":"abbreviatedTo","subj":"SS1_24035784_3_0","obj":"SS2_24035784_3_0"},{"id":"AE1_24035784_3_1","pred":"abbreviatedTo","subj":"SS1_24035784_3_1","obj":"SS2_24035784_3_1"},{"id":"AE1_24035784_8_0","pred":"abbreviatedTo","subj":"SS1_24035784_8_0","obj":"SS2_24035784_8_0"},{"id":"AE1_24035784_9_0","pred":"abbreviatedTo","subj":"SS1_24035784_9_0","obj":"SS2_24035784_9_0"},{"id":"AE1_24035784_11_0","pred":"abbreviatedTo","subj":"SS1_24035784_11_0","obj":"SS2_24035784_11_0"}],"text":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":22,"end":28},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":116,"end":135},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T3","span":{"begin":139,"end":145},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T4","span":{"begin":265,"end":284},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T5","span":{"begin":331,"end":337},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T6","span":{"begin":866,"end":872},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T7","span":{"begin":1652,"end":1658},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T8","span":{"begin":1803,"end":1809},"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":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":20,"end":28},"obj":"Glycan"},{"id":"T2","span":{"begin":137,"end":145},"obj":"Glycan"},{"id":"T3","span":{"begin":329,"end":337},"obj":"Glycan"},{"id":"T4","span":{"begin":864,"end":872},"obj":"Glycan"},{"id":"T5","span":{"begin":1650,"end":1658},"obj":"Glycan"},{"id":"T6","span":{"begin":1801,"end":1809},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A7","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":"A8","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A9","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A10","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A11","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A12","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"}],"text":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":20,"end":28},"obj":"Glycan"},{"id":"T2","span":{"begin":137,"end":145},"obj":"Glycan"},{"id":"T3","span":{"begin":329,"end":337},"obj":"Glycan"},{"id":"T4","span":{"begin":864,"end":872},"obj":"Glycan"},{"id":"T5","span":{"begin":1650,"end":1658},"obj":"Glycan"},{"id":"T6","span":{"begin":1801,"end":1809},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A7","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":"A8","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A9","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A10","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A11","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A12","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G49108TO"}],"text":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":84,"end":91},"obj":"Cell"},{"id":"T2","span":{"begin":632,"end":639},"obj":"Cell"},{"id":"T3","span":{"begin":719,"end":739},"obj":"Cell"},{"id":"T4","span":{"begin":889,"end":895},"obj":"Cell"},{"id":"T5","span":{"begin":924,"end":937},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000968"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0002131"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0017005"}],"text":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":224,"end":241},"obj":"Body_part"},{"id":"T2","span":{"begin":506,"end":519},"obj":"Body_part"},{"id":"T3","span":{"begin":889,"end":895},"obj":"Body_part"},{"id":"T4","span":{"begin":1219,"end":1229},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0005622"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_2000098"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_2000098"}],"text":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":92},"obj":"Sentence"},{"id":"T2","span":{"begin":93,"end":251},"obj":"Sentence"},{"id":"T3","span":{"begin":252,"end":390},"obj":"Sentence"},{"id":"T4","span":{"begin":391,"end":577},"obj":"Sentence"},{"id":"T5","span":{"begin":578,"end":793},"obj":"Sentence"},{"id":"T6","span":{"begin":794,"end":906},"obj":"Sentence"},{"id":"T7","span":{"begin":907,"end":915},"obj":"Sentence"},{"id":"T8","span":{"begin":916,"end":1124},"obj":"Sentence"},{"id":"T9","span":{"begin":1125,"end":1184},"obj":"Sentence"},{"id":"T10","span":{"begin":1185,"end":1284},"obj":"Sentence"},{"id":"T11","span":{"begin":1285,"end":1444},"obj":"Sentence"},{"id":"T12","span":{"begin":1445,"end":1571},"obj":"Sentence"},{"id":"T13","span":{"begin":1572,"end":1668},"obj":"Sentence"},{"id":"T14","span":{"begin":1669,"end":1757},"obj":"Sentence"},{"id":"T15","span":{"begin":1758,"end":1870},"obj":"Sentence"},{"id":"T16","span":{"begin":1871,"end":1892},"obj":"Sentence"},{"id":"T17","span":{"begin":1893,"end":2018},"obj":"Sentence"}],"text":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":20,"end":28},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":137,"end":145},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":329,"end":337},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":864,"end":872},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":1650,"end":1658},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":1801,"end":1809},"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"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0004"}],"text":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":719,"end":739},"obj":"Body_part"},{"id":"T2","span":{"begin":922,"end":937},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:83109"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:83032"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":715,"end":718},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":770,"end":773},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":916,"end":921},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":1415,"end":1420},"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":"10114"},{"id":"A4","pred":"db_id","subj":"T3","obj":"10116"},{"id":"A5","pred":"db_id","subj":"T5","obj":"9606"},{"id":"A6","pred":"db_id","subj":"T6","obj":"4565"}],"text":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":20,"end":28},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":137,"end":145},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":329,"end":337},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":864,"end":872},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":1650,"end":1658},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":1801,"end":1809},"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"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0004"}],"text":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":224,"end":241},"obj":"Body_part"},{"id":"T2","span":{"begin":506,"end":519},"obj":"Body_part"},{"id":"T3","span":{"begin":889,"end":895},"obj":"Body_part"},{"id":"T4","span":{"begin":1219,"end":1229},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0005622"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_2000098"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_2000098"}],"text":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}

{"project":"GlyCosmos15-Lectin","denotations":[{"id":"T1","span":{"begin":1415,"end":1436},"obj":"GL_000042"}],"text":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}

{"project":"Lectin_test","denotations":[{"id":"T1","span":{"begin":1415,"end":1436},"obj":"GL_000042"}],"text":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":84,"end":91},"obj":"Cell"},{"id":"T2","span":{"begin":632,"end":639},"obj":"Cell"},{"id":"T3","span":{"begin":719,"end":739},"obj":"Cell"},{"id":"T4","span":{"begin":889,"end":895},"obj":"Cell"},{"id":"T5","span":{"begin":924,"end":937},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000968"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0002131"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000084"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0017005"}],"text":"Implications of the O-GlcNAc modification in the regulation of nuclear apoptosis in T cells.\nBACKGROUND: O-linked β-N-acetylglucosamine (O-GlcNAc) is a nutrient-/stress-sensitive post-translational modification that affects nucleocytoplasmic proteins. The enzyme O-N-acetylglucosamine transferase (OGT) catalyzes the addition of O-GlcNAc, whereas O-N-acetylglucosaminidase (OGA) removes it. O-GlcNAcylation plays a role in fundamental regulatory mechanisms through the modification of proteins involved in cell division, metabolism, transcription, cell signaling and apoptosis. The effects of O-GlcNAcylation on apoptosis appear to be cell-dependent, as elevated levels played a protective role in primary neonatal rat ventricular myocytes but had a cytotoxic effect in rat pancreatic β-cells. The aim of the current study was to determine the implications of the O-GlcNAc modification on T cell apoptosis.\nMETHODS: Human T lymphoblastic HPB-ALL cells were treated with the OGA inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), or with glucosamine (GlcN), to increase O-GlcNAcylation. Apoptosis was induced in the presence of tributyltin (TBT). DNA fragmentation was observed by cell cycle analysis and corresponded to the sub G0/G1 population. O-GlcNAcylated proteins were detected by immunoblot using a specific antibody (ctd110.6) and were precipitated using succinylated wheat germ agglutinin (sWGA).\nRESULTS: HPB-ALL cells treated with PUGNAc displayed a significant reduction in DNA fragmentation after TBT-induced apoptosis. DFF45, the protein that inhibits the endonuclease DFF40, was identified to be O-GlcNAc modified. O-GlcNAcylated DFF45 appeared to be more resistant to caspase cleavage during apoptosis. Our results suggest that a decrease in the O-GlcNAc modification on DFF45 occurs before its cleavage by caspase.\nGENERAL SIGNIFICANCE: Our results indicate that the O-GlcNAcylation of DFF45 may represent a mechanism to control the accidental activation of DFF."}