Regulation of lipoprotein lipase by Angptl4

Trends Endocrinol Metab. 2014 Mar;25(3):146-55. doi: 10.1016/j.tem.2013.12.005. Epub 2014 Jan 4.

Abstract

Triglyceride (TG)-rich chylomicrons and very low density lipoproteins (VLDL) distribute fatty acids (FA) to various tissues by interacting with the enzyme lipoprotein lipase (LPL). The protein angiopoietin-like 4 (Angptl4) is under sensitive transcriptional control by FA and the FA-activated peroxisome proliferator activated receptors (PPARs), and its tissue expression largely overlaps with that of LPL. Growing evidence indicates that Angptl4 mediates the physiological fluctuations in LPL activity, including the decrease in adipose tissue LPL activity during fasting. This review focuses on the major ambiguities concerning the mechanism of LPL inhibition by Angptl4, as well as on the physiological role of Angptl4 in lipid metabolism, highlighting its function in a variety of tissues, and uses this information to make suggestions for further research.

Keywords: angiopoietin-like 4; glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein; hypertriglyceridemia; lipoprotein lipase; proprotein convertases.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adipose Tissue / metabolism
  • Angiopoietin-like 4 Protein
  • Angiopoietins / genetics
  • Angiopoietins / metabolism*
  • Fatty Acids / metabolism
  • Humans
  • Lipoprotein Lipase / genetics
  • Lipoprotein Lipase / metabolism*
  • Peroxisome Proliferator-Activated Receptors / metabolism
  • Proprotein Convertases / genetics
  • Proprotein Convertases / metabolism

Substances

  • ANGPTL4 protein, human
  • Angiopoietin-like 4 Protein
  • Angiopoietins
  • Fatty Acids
  • Peroxisome Proliferator-Activated Receptors
  • Lipoprotein Lipase
  • Proprotein Convertases