ANGPTL4 inactivates lipoprotein lipase by catalyzing the irreversible unfolding of LPL's hydrolase domain
KK Kristensen, KZ Leth-Espensen, SG Young… - Journal of Lipid …, 2020 - ASBMB
The ANGPTL proteins regulate the catalytic activity of lipoprotein lipase (LPL) by catalyzing
the unfolding of LPL's N-terminal hydrolase domain. Intravascular processing of triglyceride-
rich lipoproteins depends on LPL and GPIHBP1 (an endothelial cell protein that binds LPL
and transports it to the capillary lumen). A deficiency of either protein severely impairs
triglyceride hydrolysis, resulting in markedly elevated plasma triglyceride levels and a
substantial risk of acute pancreatitis. Angiopoietin-like proteins (ANGPTL) 3, 4, and 8 …
the unfolding of LPL's N-terminal hydrolase domain. Intravascular processing of triglyceride-
rich lipoproteins depends on LPL and GPIHBP1 (an endothelial cell protein that binds LPL
and transports it to the capillary lumen). A deficiency of either protein severely impairs
triglyceride hydrolysis, resulting in markedly elevated plasma triglyceride levels and a
substantial risk of acute pancreatitis. Angiopoietin-like proteins (ANGPTL) 3, 4, and 8 …