ANGPTL3 accelerates atherosclerotic progression via direct regulation of M1 macrophage activation in plaque.

ABSTRACT:

Introduction

The N-terminal domain of angiopoietin-like protein 3 (ANGPTL3) inhibits lipoprotein lipase activity. Its C-terminal fibrinogen-like (FBN) domain is a ligand of macrophage integrin αvβ3.

Objectives

ANGPTL3 might home to plaque where it directly regulates macrophage function via integrin αvβ3 for atherosclerosis progression.

Methods

Ldlr^-/- mice on a high-fat diet and ApoE^-/- mice on a chow diet were received adeno-associated virus (AAV)-mediated Angptl3 gene transfer and followed up for 12 weeks. ApoE^-/- mice were injected AAV containing FLAG-tagged Angptl3 cDNA for tracing. Atherosclerotic features were compared between Angptl3^-/-ApoE^-/- mice and ApoE^-/- littermates. THP-1 cells were expose

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC11976407 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature