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Suh, Pann-Ghill
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dc.citation.endPage 5742 -
dc.citation.number 8 -
dc.citation.startPage 5732 -
dc.citation.title JOURNAL OF BIOLOGICAL CHEMISTRY -
dc.citation.volume 288 -
dc.contributor.author Song, Parkyong -
dc.contributor.author Kim, Jong Hyun -
dc.contributor.author Ghim, Jaewang -
dc.contributor.author Yoon, Jong Hyuk -
dc.contributor.author Lee, Areum -
dc.contributor.author Kwon, Yonghoon -
dc.contributor.author Hyun, Hyunjung -
dc.contributor.author Moon, Hyo-Youl -
dc.contributor.author Choi, Hueng-Sik -
dc.contributor.author Berggren, Per-Olof -
dc.contributor.author Suh, Pann-Ghill -
dc.contributor.author Ryu, Sung Ho -
dc.date.accessioned 2023-12-22T04:13:12Z -
dc.date.available 2023-12-22T04:13:12Z -
dc.date.created 2013-06-28 -
dc.date.issued 2013-02 -
dc.description.abstract AMP-activated protein kinase has been described as a key signaling protein that can regulate energy homeostasis. Here, we aimed to characterize novel AMP-activated kinase (AMPK)-activating compounds that have a much lower effective concentration than metformin. As a result, emodin, a natural anthraquinone derivative, was shown to stimulate AMPK activity in skeletal muscle and liver cells. Emodin enhanced GLUT4 translocation and [C-14]glucose uptake into the myotube in an AMPK-dependent manner. Also, emodin inhibited glucose production by suppressing the expression of key gluconeogenic genes, such as phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, in hepatocytes. Furthermore, we found that emodin can activate AMPK by inhibiting mitochondrial respiratory complex I activity, leading to increased reactive oxygen species and Ca2+/calmodulin-dependent protein kinase kinase activity. Finally, we confirmed that a single dose administration of emodin significantly decreased the fasting plasma glucose levels and improved glucose tolerance in C57Bl/6J mice. Increased insulin sensitivity was also confirmed after daily injection of emodin for 8 days using an insulin tolerance test and insulin-stimulated PI3K phosphorylation in wild type and high fat diet-induced diabetic mouse models. Our study suggests that emodin regulates glucose homeostasis in vivo by AMPK activation and that this may represent a novel therapeutic principle in the treatment of type 2 diabetic models. -
dc.identifier.bibliographicCitation JOURNAL OF BIOLOGICAL CHEMISTRY, v.288, no.8, pp.5732 - 5742 -
dc.identifier.doi 10.1074/jbc.M112.441477 -
dc.identifier.issn 0021-9258 -
dc.identifier.scopusid 2-s2.0-84874314479 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/3395 -
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84874314479 -
dc.identifier.wosid 000315342500045 -
dc.language 영어 -
dc.publisher AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC -
dc.title Emodin Regulates Glucose Utilization by Activating AMP-activated Protein Kinase -
dc.type Article -
dc.relation.journalWebOfScienceCategory Biochemistry & Molecular Biology -
dc.relation.journalResearchArea Biochemistry & Molecular Biology -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordPlus 11-BETA-HYDROXYSTEROID DEHYDROGENASE TYPE-1 -
dc.subject.keywordPlus DEPENDENT DIABETES-MELLITUS -
dc.subject.keywordPlus RAT SKELETAL-MUSCLE -
dc.subject.keywordPlus COMPLEX-I -
dc.subject.keywordPlus SIGNALING PATHWAY -
dc.subject.keywordPlus ADIPOSE-TISSUE -
dc.subject.keywordPlus INSULIN -
dc.subject.keywordPlus METFORMIN -
dc.subject.keywordPlus CELLS -
dc.subject.keywordPlus TRANSPORT -

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