TY - JOUR
T1 - Angptl4 serves as an endogenous inhibitor of intestinal lipid digestion
AU - Mattijssen, Frits
AU - Alex, Sheril
AU - Swarts, Hans J.
AU - Groen, Albert K.
AU - van Schothorst, Evert M.
AU - Kersten, Sander
PY - 2014
Y1 - 2014
N2 - 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
AB - 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
U2 - https://doi.org/10.1016/j.molmet.2013.11.004
DO - https://doi.org/10.1016/j.molmet.2013.11.004
M3 - Article
C2 - 24634819
SN - 2212-8778
VL - 3
SP - 135
EP - 144
JO - Molecular metabolism
JF - Molecular metabolism
IS - 2
ER -