Work

ANGPTL4 sensitizes lipoprotein lipase to PCSK3 cleavage by catalyzing its unfolding

Year: 2021
Type: article
Abstract: The lipolytic processing of triglyceride-rich lipoproteins within capillaries is mediated by LPL complexed to GPIHBP1, a protein of capillary endothelial cells (1). Angiopoietin-like protein 4 (ANGPTL4) plays an important role in regulating LPL activity, particularly in adipose tissue. Hydrogen-deuterium exchange experiments show that ANGPTL4 binds to sequences adjacent to the catalytic pocket of LPLs. This binding triggers progressive and irreversible unfolding of LPLs catalytic domain (2, 3). Importantly, ANGPTL4 catalyzes this unfolding.
Language: English
Field: Medicine
Open Access status: gold
Estimated APC paid: $2,500
OpenAlex ID: W3137965592
FWCI: 1.842
Cites: 5
Cited by: 15
Related to: 10