Exchangeable APOA1 on HDL inhibits LDL binding to proteoglycans.

ABSTRACT: The entrapment of LDLs by proteoglycans (PGs) in the extracellular matrix of the arterial intima is a key initial step in the development of atherosclerosis. HDLs can interfere with this process, but the underlying mechanism is not fully understood. The aim of this study was to investigate the mechanisms by which HDL inhibits LDL binding to PG. An In-Cell ELISA was used to measure the binding of LDL to PGs in the extracellular matrix synthesized by mouse vascular smooth muscle cells. Fast-protein liquid chromatography, immunoprecipitation, SDS-PAGE, and immunoblotting analysis were performed to characterize how HDL and its apolipoproteins inhibit LDL binding to PGs. HDL and APOA1 inhibited LDL binding to PGs in a dose-dependent manner. Competition experiments showed that HDL did not compet

SUBMITTER: Geh EN 

PROVIDER: S-EPMC12512155 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature