Regulation of Hepatic Triacylglycerol Metabolism by CGI-58 Does Not Require ATGL Co-activation

Cell Rep. 2016 Jul 26;16(4):939-949. doi: 10.1016/j.celrep.2016.06.049. Epub 2016 Jul 7.

Abstract

Adipose triglyceride lipase (ATGL) and comparative gene identification 58 (CGI-58) are critical regulators of triacylglycerol (TAG) turnover. CGI-58 is thought to regulate TAG mobilization by stimulating the enzymatic activity of ATGL. However, it is not known whether this coactivation function of CGI-58 occurs in vivo. Moreover, the phenotype of human CGI-58 mutations suggests ATGL-independent functions. Through direct comparison of mice with single or double deficiency of CGI-58 and ATGL, we show here that CGI-58 knockdown causes hepatic steatosis in both the presence and absence of ATGL. CGI-58 also regulates hepatic diacylglycerol (DAG) and inflammation in an ATGL-independent manner. Interestingly, ATGL deficiency, but not CGI-58 deficiency, results in suppression of the hepatic and adipose de novo lipogenic program. Collectively, these findings show that CGI-58 regulates hepatic neutral lipid storage and inflammation in the genetic absence of ATGL, demonstrating that mechanisms driving TAG lipolysis in hepatocytes differ significantly from those in adipocytes.

Keywords: lipase; neutral lipid storage disease; triacylglycerol.

MeSH terms

  • 1-Acylglycerol-3-Phosphate O-Acyltransferase / metabolism*
  • Adipocytes / metabolism
  • Animals
  • Diglycerides / metabolism
  • Fatty Liver / metabolism
  • Hepatocytes / metabolism
  • Humans
  • Inflammation / metabolism
  • Lipase / metabolism*
  • Lipid Metabolism / physiology
  • Lipogenesis / physiology
  • Lipolysis / physiology
  • Liver / metabolism*
  • Male
  • Mice
  • Mice, Knockout
  • Triglycerides / metabolism*

Substances

  • Diglycerides
  • Triglycerides
  • 1-Acylglycerol-3-Phosphate O-Acyltransferase
  • Abhd5 protein, mouse
  • Lipase
  • PNPLA2 protein, mouse