PubMed:15525818 JSONTXT

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":824,"end":838},"obj":"Cell"},{"id":"T2","span":{"begin":926,"end":936},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000010"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000235"},{"id":"A3","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000394"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":1004,"end":1011},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":1004,"end":1011},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G15021LG"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":1004,"end":1011},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":62,"end":69},"obj":"http://purl.obolibrary.org/obo/MAT_0000393"},{"id":"T2","span":{"begin":1081,"end":1087},"obj":"http://purl.obolibrary.org/obo/MAT_0000393"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":94},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":95,"end":156},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":157,"end":305},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":306,"end":539},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":540,"end":718},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":719,"end":870},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":871,"end":1023},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1024,"end":1114},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1115,"end":1272},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1273,"end":1506},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":94},"obj":"Sentence"},{"id":"T2","span":{"begin":95,"end":156},"obj":"Sentence"},{"id":"T3","span":{"begin":157,"end":305},"obj":"Sentence"},{"id":"T4","span":{"begin":306,"end":539},"obj":"Sentence"},{"id":"T5","span":{"begin":540,"end":718},"obj":"Sentence"},{"id":"T6","span":{"begin":719,"end":870},"obj":"Sentence"},{"id":"T7","span":{"begin":871,"end":1023},"obj":"Sentence"},{"id":"T8","span":{"begin":1024,"end":1114},"obj":"Sentence"},{"id":"T9","span":{"begin":1115,"end":1272},"obj":"Sentence"},{"id":"T10","span":{"begin":1273,"end":1506},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":94},"obj":"Sentence"},{"id":"T2","span":{"begin":95,"end":156},"obj":"Sentence"},{"id":"T3","span":{"begin":157,"end":305},"obj":"Sentence"},{"id":"T4","span":{"begin":306,"end":539},"obj":"Sentence"},{"id":"T5","span":{"begin":540,"end":718},"obj":"Sentence"},{"id":"T6","span":{"begin":719,"end":870},"obj":"Sentence"},{"id":"T7","span":{"begin":871,"end":1023},"obj":"Sentence"},{"id":"T8","span":{"begin":1024,"end":1114},"obj":"Sentence"},{"id":"T9","span":{"begin":1115,"end":1272},"obj":"Sentence"},{"id":"T10","span":{"begin":1273,"end":1506},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":1115,"end":1131},"obj":"http://www.uniprot.org/uniprot/P07996"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":224,"end":227},"obj":"http://www.uniprot.org/uniprot/P62340"},{"id":"T2","span":{"begin":232,"end":235},"obj":"http://www.uniprot.org/uniprot/P62340"},{"id":"T3","span":{"begin":265,"end":268},"obj":"http://www.uniprot.org/uniprot/P62340"},{"id":"T4","span":{"begin":295,"end":298},"obj":"http://www.uniprot.org/uniprot/P62340"},{"id":"T5","span":{"begin":340,"end":343},"obj":"http://www.uniprot.org/uniprot/P62340"},{"id":"T6","span":{"begin":348,"end":351},"obj":"http://www.uniprot.org/uniprot/P62340"},{"id":"T7","span":{"begin":1115,"end":1131},"obj":"http://www.uniprot.org/uniprot/P35441"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":434,"end":443},"obj":"http://purl.bioontology.org/ontology/STY/T192"},{"id":"T2","span":{"begin":833,"end":838},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T3","span":{"begin":951,"end":956},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T4","span":{"begin":1243,"end":1250},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T5","span":{"begin":1342,"end":1349},"obj":"http://purl.bioontology.org/ontology/STY/T024"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":34,"end":47},"obj":"http://purl.obolibrary.org/obo/GO_0097502"},{"id":"T2","span":{"begin":317,"end":330},"obj":"http://purl.obolibrary.org/obo/GO_0097502"},{"id":"T3","span":{"begin":494,"end":507},"obj":"http://purl.obolibrary.org/obo/GO_0097502"},{"id":"T4","span":{"begin":573,"end":586},"obj":"http://purl.obolibrary.org/obo/GO_0097502"},{"id":"T5","span":{"begin":807,"end":820},"obj":"http://purl.obolibrary.org/obo/GO_0097502"},{"id":"T6","span":{"begin":895,"end":908},"obj":"http://purl.obolibrary.org/obo/GO_0097502"},{"id":"T7","span":{"begin":1039,"end":1052},"obj":"http://purl.obolibrary.org/obo/GO_0097502"},{"id":"T8","span":{"begin":1176,"end":1189},"obj":"http://purl.obolibrary.org/obo/GO_0097502"},{"id":"T9","span":{"begin":1303,"end":1316},"obj":"http://purl.obolibrary.org/obo/GO_0097502"},{"id":"T10","span":{"begin":97,"end":110},"obj":"http://purl.obolibrary.org/obo/GO_0097502"},{"id":"T11","span":{"begin":239,"end":251},"obj":"http://purl.obolibrary.org/obo/GO_0097502"},{"id":"T12","span":{"begin":282,"end":294},"obj":"http://purl.obolibrary.org/obo/GO_0097502"},{"id":"T13","span":{"begin":130,"end":143},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T14","span":{"begin":130,"end":155},"obj":"http://purl.obolibrary.org/obo/GO_0006486"},{"id":"T15","span":{"begin":1468,"end":1479},"obj":"http://purl.obolibrary.org/obo/GO_0032502"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":643,"end":653},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T2","span":{"begin":729,"end":737},"obj":"http://purl.obolibrary.org/obo/GO_0003823"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":515,"end":519},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":833,"end":838},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":951,"end":956},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":62,"end":69},"obj":"http://purl.obolibrary.org/obo/UBERON_0000055"},{"id":"T2","span":{"begin":1081,"end":1087},"obj":"http://purl.obolibrary.org/obo/UBERON_0000055"},{"id":"T3","span":{"begin":1243,"end":1250},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"T4","span":{"begin":1342,"end":1349},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":62,"end":69},"obj":"http://purl.obolibrary.org/obo/MAT_0000393"},{"id":"T2","span":{"begin":1081,"end":1087},"obj":"http://purl.obolibrary.org/obo/MAT_0000393"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":62,"end":69},"obj":"http://purl.obolibrary.org/obo/UBERON_0000055"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":1081,"end":1087},"obj":"http://purl.obolibrary.org/obo/UBERON_0000055"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":1243,"end":1250},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":1342,"end":1349},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":62,"end":69},"obj":"Body_part"},{"id":"T2","span":{"begin":1081,"end":1087},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000393"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000393"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":89,"end":93},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":865,"end":869},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":1109,"end":1113},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":1267,"end":1271},"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":"10114"},{"id":"A6","pred":"db_id","subj":"T5","obj":"10116"},{"id":"A7","pred":"db_id","subj":"T7","obj":"10114"},{"id":"A8","pred":"db_id","subj":"T7","obj":"10116"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":926,"end":936},"obj":"Body_part"},{"id":"T2","span":{"begin":1081,"end":1087},"obj":"Body_part"},{"id":"T3","span":{"begin":1088,"end":1092},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000235"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000055"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000060"}],"text":"Increased expression of protein C-mannosylation in the aortic vessels of diabetic Zucker rats.\nC-Mannosylation is a novel type of glycosylation in proteins. There are several examples of proteins in which the specific motif Trp-X-X-Trp is mannosylated at the first Trp to produce C-mannosylated Trp (CMW). Although C-mannosylation modifies Trp-X-X-Trp, predicted to be a functional motif of various integral proteins such as cytokine receptors, the physiological or pathological relevance of C-mannosylation in the cell is still not known. In this study, to characterize C-mannosylation in biological samples, we generated specific polyclonal antibodies against CMW by using a chemically synthesized CMW as an antigen. Using the antibody, we investigated the effect of hyperglycemic conditions on protein C-mannosylation in cultured cells and diabetic Zucker fatty rats. We found that protein C-mannosylation was increased in macrophage-like RAW264.7 cells under hyperglycemic conditions compared to low-glucose conditions. Furthermore, C-mannosylation was increased in the aortic vessel wall of Zucker fatty rats. Thrombospondin-1 was identified as a protein modified with C-mannosylation, and its expression was also increased in the aortic tissues of Zucker fatty rats. These results indicate that C-mannosylation is increased in specific tissues or cell types under hyperglycemic conditions, suggesting a pathological role for the increased C-mannosylation in the development of diabetic complications."}