Angptl4 serves as an endogenous inhibitor of intestinal lipid digestion

Frits Mattijssen, Sheril Alex, Hans J. Swarts, Albert K. Groen, Evert M. van Schothorst, Sander Kersten*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

62 Citations (Scopus)
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Dietary triglycerides are hydrolyzed in the small intestine principally by pancreatic lipase. Following uptake by enterocytes and secretion as chylomicrons, dietary lipids are cleared from the bloodstream via lipoprotein lipase. Whereas lipoprotein lipase is inhibited by several proteins including Angiopoietin-like 4 (Angptl4), no endogenous regulator of pancreatic lipase has yet been identified. Here we present evidence that Angptl4-/- is an endogenous inhibitor of dietary lipid digestion. Angptl4-/- mice were heavier compared to their wild -type counterparts without any difference in food intake, energy expenditure or locomotor activity. However, Angptl4 / mice showed decreased lipid content in the stools and increased accumulation of dietary triglycerides in the small intestine, which coincided with elevated lumina! lipase activity in Angptl4 l mice. Furthermore, recombinant Angptl4-/- reduced the activity of pancreatic lipase as well as the lipase activity in human ileostomy output. In conclusion, our data suggest that Angptl4-/- is an endogenous inhibitor of intestinal lipase activity. 2013 The Authors. Published by Elsevier

Original languageEnglish
Pages (from-to)135-144
Number of pages10
JournalMolecular metabolism
Issue number2
Publication statusPublished - Apr-2014


  • Angptl4
  • Pancreatic lipase
  • Intestine
  • Obesity

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