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- 검색키워드
- 저자 : Horng-Mo Lee (검색결과 2 건)
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Mei-Chen Lo,Jia-Yin Chen,Yung-Ting Kuo,Wei-Lu Chen,Horng-Mo Lee,Shyang-Guang Wang 대한약학회 2019 Archives of Pharmacal Research Vol.42 No.8
Caloric restriction activates sirtuin 1 (SIRT1)and induces a variety of metabolic effects that are beneficialfor preventing age-related disease. The present studyscreened a commercially available used drug library todevelop small molecule activators of SIRT1 as therapeuticsfor treatment of metabolic disorders. Using an in vitrofluorescence assay, the cancer therapeutic camptothecinincreased SIRT1 enzymatic activity by 5.5-fold, indicatingit to be a potent SIRT1 activator. Camptothecin also elevatedthe nicotinamide adenine dinucleotide (NAD)?/NADH ratio and increased SIRT1 protein levels in differentiatedC2C12 myogenic cells. Treatment of C2C12 myotubeswith camptothecin increased phosphorylation ofAMP-dependent kinase (AMPK) and acetyl-coenzyme Acarboxylase, caused nuclear translocation and deacetylationof forkhead box O1 (FoxO1), increased transcriptionand protein expression of adipose triglyceride lipase(ATGL), decreased the amount of intracellular oil droplets,and significantly increased b-oxidation of fatty acids. These in vitro data were confirmed in vivo as camptothecintreatment of C57BL/6J mice reduced fat and plasmatriglyceride levels. All of the above camptothecin-inducedalterations were attenuated by the SIRT1-specific inhibitornicotinamide and/or 6-[4-(2-piperidin-1-ylethoxy) phenyl]-3-pyridin-4-ylpyrazolo [1,5-a]pyrimidin (compound C). Thus, camptothecin activation of SIRT1 promotes lipidcatabolism through AMPK/FoxO1/ATGL signaling.
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Monacolin K affects lipid metabolism through SIRT1/AMPK pathway in HepG2 cells
Chia-Hsin Huang,Shin-Mau Shiu,Min-Tze Wu,Wei-Lu Chen,Shyang-Guang Wang,Horng-Mo Lee 대한약학회 2013 Archives of Pharmacal Research Vol.36 No.12
Monacolin K is the secondary metabolite isolatedfrom Monascus spp. It is the natural form of lovastatin,which is clinically used to reduce the synthesis of cholesterolby inhibiting 3-hydroxy-3-methylglutaryl coenzyme Areductase. In the present study, monacolin K increased proteinexpression of SIRT1 and phosphorylation level of AMPactivatedprotein kinase (AMPK) in HepG2 cells. Throughactivation of SIRT1/AMPK pathway, monacolin Kincreased phosphorylation of acetyl CoA carboxylase andcaused nuclear translocation of forkhead box O1. The westernblotting results showed that monacolin K increasedexpression of adipose triglyceride lipase but decreasedabundances of fatty acid synthase (FAS) and sterol regulatory element-binding protein 1 (SREBP1). MonacolinK also decreased the intracellular accumulation of lipids asdemonstrated by Oil Red O staining. In addition, theimmunostaining showed that monacolin K prevented thenuclear translocation of SREBP1, indicating the associationwith down-regulation of FAS. All the demonstrated effectsof monacolin K were counteracted by nicotinamide orcompound C, the inhibitors of SIRT1 orAMPK. In summary,monacolin K reduces the lipid content through SIRT1/AMPK pathway in HepG2 cells, which promotes catabolismand inhibits anabolism of lipid.
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