Cyanidin-3-O-β-glucoside regulates fatty acid metabolism via an AMP-activated protein kinase-dependent signaling pathway in human HepG2 cells
العنوان: | Cyanidin-3-O-β-glucoside regulates fatty acid metabolism via an AMP-activated protein kinase-dependent signaling pathway in human HepG2 cells |
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المؤلفون: | Honghui Guo, Duan Wang, Yun Wang, Min Xia, Guoling Liu, Ruimin Zhong |
المصدر: | Lipids in Health and Disease Lipids in Health and Disease, Vol 11, Iss 1, p 10 (2012) |
بيانات النشر: | BioMed Central, 2012. |
سنة النشر: | 2012 |
مصطلحات موضوعية: | Endocrinology, Diabetes and Metabolism, Clinical Biochemistry, Enzyme Activators, Gene Expression, Calcium-Calmodulin-Dependent Protein Kinase Kinase, carnitine palmitoyl transferase 1, acetyl CoA carboxylase, anthocyanin, Anthocyanins, chemistry.chemical_compound, Endocrinology, AMP-activated protein kinase, Glucosides, Ca2+/calmodulin-dependent protein kinase, Humans, Calcium Signaling, Phosphorylation, Protein kinase A, lcsh:RC620-627, Beta oxidation, Biochemistry, medical, Fatty acid metabolism, biology, Carnitine O-Palmitoyltransferase, Research, Lipogenesis, Biochemistry (medical), Adenylate Kinase, Fatty Acids, Lipid Mobilization, Acetyl-CoA carboxylase, AMPK, Hep G2 Cells, Enzyme Activation, Malonyl Coenzyme A, lcsh:Nutritional diseases. Deficiency diseases, Malonyl-CoA, chemistry, Biochemistry, fatty acid metabolism, biology.protein, Fatty Acid Synthases, Oxidation-Reduction, Acetyl-CoA Carboxylase |
الوصف: | Background Hepatic metabolic derangements are key components in the development of fatty liver disease. AMP-activated protein kinase (AMPK) plays a central role in controlling hepatic lipid metabolism through modulating the downstream acetyl CoA carboxylase (ACC) and carnitine palmitoyl transferase 1 (CPT-1) pathway. In this study, cyanidin-3-O-β-glucoside (Cy-3-g), a typical anthocyanin pigment was used to examine its effects on AMPK activation and fatty acid metabolism in human HepG2 hepatocytes. Results Anthocyanin Cy-3-g increased cellular AMPK activity in a calmodulin kinase kinase dependent manner. Furthermore, Cy-3-g substantially induced AMPK downstream target ACC phosphorylation and inactivation, and then decreased malonyl CoA contents, leading to stimulation of CPT-1 expression and significant increase of fatty acid oxidation in HepG2 cells. These effects of Cy-3-g are largely abolished by pharmacological and genetic inhibition of AMPK. Conclusion This study demonstrates that Cy-3-g regulates hepatic lipid homeostasis via an AMPK-dependent signaling pathway. Targeting AMPK activation by anthocyanin may represent a promising approach for the prevention and treatment of obesity-related nonalcoholic fatty liver disease. |
اللغة: | English |
تدمد: | 1476-511X |
الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6859ded60850412042454cc062b8f7dTest http://europepmc.org/articles/PMC3398342Test |
حقوق: | OPEN |
رقم الانضمام: | edsair.doi.dedup.....b6859ded60850412042454cc062b8f7d |
قاعدة البيانات: | OpenAIRE |
تدمد: | 1476511X |
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