期刊
AMERICAN JOURNAL OF PHYSIOLOGY-GASTROINTESTINAL AND LIVER PHYSIOLOGY
卷 292, 期 5, 页码 G1195-G1199出版社
AMER PHYSIOLOGICAL SOC
DOI: 10.1152/ajpgi.00553.2006
关键词
insulin resistance; diacylglycerol; lysophosphatidate; sterol regulatory element binding protein; hepatic steatosis
资金
- FIC NIH HHS [R03 TW006034, R03-TW06034] Funding Source: Medline
- NIDDK NIH HHS [R01 DK056598-15, P30 DK056350, DK-56598, DK-59935, R01 DK056598, R01 DK059935, P30 DK-56350] Funding Source: Medline
GPAT1, one of four known glycerol-3-phosphate acyltransferase isoforms, is located on the mitochondrial outer membrane, allowing reciprocal regulation with carnitine palmitoyltransferase1. GPAT1 is upregulated transcriptionally by insulin and SREBP-1c and downregulated acutely by AMP-activated protein kinase, consistent with a role in triacylglycerol synthesis. Knockout and overexpression studies suggest that GPAT1 is critical for the development of hepatic steatosis and that steatosis initiated by overexpression of GPAT1 causes hepatic, and perhaps also peripheral, insulin resistance. Future questions include the function of GPAT1 in relation to the other GPAT isoforms and whether the lipid intermediates synthesized by GPAT and downstream enzymes in the pathway of glycerolipid biosynthesis participate in intracellular signaling pathways.
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