Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8

Am J Physiol Endocrinol Metab. 2021 Oct 1;321(4):E493-E508. doi: 10.1152/ajpendo.00195.2021. Epub 2021 Aug 2.

Abstract

Triglyceride-rich lipoproteins deliver fatty acids to tissues for oxidation and for storage. Release of fatty acids from circulating lipoprotein triglycerides is carried out by lipoprotein lipase (LPL), thus LPL serves as a critical gatekeeper of fatty acid uptake into tissues. LPL activity is regulated by a number of extracellular proteins including three members of the angiopoietin-like family of proteins. In this review, we discuss our current understanding of how, where, and when ANGPTL3, ANGPTL4, and ANGPTL8 regulate lipoprotein lipase activity, with a particular emphasis on how these proteins interact with each other to coordinate triglyceride metabolism and fat partitioning.

Keywords: ANGPTL proteins; cardiovascular disease; dyslipidemia; lipoprotein lipase; lipoproteins.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Angiopoietin-Like Protein 3
  • Angiopoietin-Like Protein 4 / metabolism*
  • Angiopoietin-Like Protein 8
  • Angiopoietin-like Proteins / metabolism*
  • Humans
  • Lipid Metabolism*
  • Lipoproteins / metabolism*
  • Peptide Hormones / metabolism*
  • Triglycerides / metabolism*

Substances

  • ANGPTL3 protein, human
  • ANGPTL4 protein, human
  • ANGPTL8 protein, human
  • Angiopoietin-Like Protein 3
  • Angiopoietin-Like Protein 4
  • Angiopoietin-Like Protein 8
  • Angiopoietin-like Proteins
  • Lipoproteins
  • Peptide Hormones
  • Triglycerides