Lack of O-G1cNAcylation enhances exercise-dependent glucose utilization potentially through AMP -activated protein kinase activation in skeletal muscle
DC Field | Value | Language |
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dc.contributor.author | Murata, Koichiro | - |
dc.contributor.author | Morino, Katsutaro | - |
dc.contributor.author | Ida, Shogo | - |
dc.contributor.author | Ohashi, Natsuko | - |
dc.contributor.author | Lemecha, Mengistu | - |
dc.contributor.author | Park, Shi-Young | - |
dc.contributor.author | Ishikado, Atsushi | - |
dc.contributor.author | Kume, Shinji | - |
dc.contributor.author | Choi, Cheol Soo | - |
dc.contributor.author | Sekine, Osamu | - |
dc.contributor.author | Ugi, Satoshi | - |
dc.contributor.author | Maegawa, Hiroshi | - |
dc.date.available | 2020-02-27T12:41:02Z | - |
dc.date.created | 2020-02-06 | - |
dc.date.issued | 2018-01-08 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/4140 | - |
dc.description.abstract | O-G1cNAcylation is a post-translational modification that is characterized by the addition of N-acetylglucosamine (GIcNAc) to proteins by O-G1cNAc transferase (Ogt). The degree of O-GIcNAcylation is thought to be associated with glucotoxicity and diabetic complications, because GlcNAc is produced by a branch of the glycolytic pathway. However, its role in skeletal muscle has not been fully elucidated. In this study, we created skeletal muscle-specific Ogt knockout (Ogt-MKO) mice and analyzed their glucose metabolism. During an intraperitoneal glucose tolerance test, blood glucose was slightly lower in OgtMKO mice than in control Ogt-fiox mice. High fat diet-induced obesity and insulin resistance were reversed in Ogt-MKO mice. In addition, 12-month-old Ogt-MKO mice had lower adipose and body mass. A single bout of exercise significantly reduced blood glucose in Ogt-MKO mice, probably because of higher AMP-activated protein kinase cc (AMPKa) protein expression. Furthermore, intraperitoneal injection of 5-aminoimidazole-4-carboxamide ribonucleotide, an AMPK activator, resulted in a more marked decrease in blood glucose levels in Ogt-MKO mice than in controls. Finally, Ogt knockdown by siRNA in C2C12 myotubes significantly increased protein expression of AMPKa, glucose uptake and oxidation. In conclusion, loss of O-G1cNAcylation facilitates glucose utilization in skeletal muscle, potentially through AMPK activation. The inhibition of O-G1cNAcylation in skeletal muscle may have an anti-diabetic effect, through an enhancement of glucose utilization during exercise. (C) 2017 Elsevier Inc. All rights reserved. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.subject | O-LINKED GLYCOSYLATION | - |
dc.subject | INSULIN-RESISTANCE | - |
dc.subject | MITOCHONDRIAL BIOGENESIS | - |
dc.subject | GLCNAC | - |
dc.subject | MICE | - |
dc.subject | EXPRESSION | - |
dc.subject | GLCNACYLATION | - |
dc.subject | HOMEOSTASIS | - |
dc.subject | NUTRIENT | - |
dc.subject | SUBUNIT | - |
dc.title | Lack of O-G1cNAcylation enhances exercise-dependent glucose utilization potentially through AMP -activated protein kinase activation in skeletal muscle | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000424732700079 | - |
dc.identifier.doi | 10.1016/j.bbrc.2017.12.081 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.495, no.2, pp.2098 - 2104 | - |
dc.identifier.scopusid | 2-s2.0-85039423040 | - |
dc.citation.endPage | 2104 | - |
dc.citation.startPage | 2098 | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 495 | - |
dc.citation.number | 2 | - |
dc.contributor.affiliatedAuthor | Park, Shi-Young | - |
dc.contributor.affiliatedAuthor | Choi, Cheol Soo | - |
dc.type.docType | Article | - |
dc.subject.keywordAuthor | O-GlcNAcylation | - |
dc.subject.keywordAuthor | AMP-activated protein kinase | - |
dc.subject.keywordAuthor | Skeletal muscle | - |
dc.subject.keywordPlus | O-LINKED GLYCOSYLATION | - |
dc.subject.keywordPlus | INSULIN-RESISTANCE | - |
dc.subject.keywordPlus | MITOCHONDRIAL BIOGENESIS | - |
dc.subject.keywordPlus | GLCNAC | - |
dc.subject.keywordPlus | MICE | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | GLCNACYLATION | - |
dc.subject.keywordPlus | HOMEOSTASIS | - |
dc.subject.keywordPlus | NUTRIENT | - |
dc.subject.keywordPlus | SUBUNIT | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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