Work

ANGPTL4 inactivates lipoprotein lipase by catalyzing the irreversible unfolding of LPL's hydrolase domain

Year: 2020

Type: editorial

Abstract: 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 regulate LPL activity.

Source: Journal of Lipid Research

DOI: 10.1194/jlr.ilr120000780

Authors: Kristian Kølby Kristensen, Katrine Zinck Leth-Espensen, Stephen G. Young, Michael Ploug

Institutions: University of Copenhagen, Rigshospitalet, University of California, Los Angeles

Language: English

Topic: Lipid metabolism and disorders

Subfield: Cardiology and Cardiovascular Medicine

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $3,430