OxLDL triggers retrograde translocation of arginase2 in aortic endothelial cells via ROCK and mitochondrial processing peptidase.

ABSTRACT:

Rationale

Increased arginase activity contributes to endothelial dysfunction by competition for l-arginine substrate and reciprocal regulation of nitric oxide synthase (NOS). The rapid increase in arginase activity in human aortic endothelial cells exposed to oxidized low-density lipoprotein (OxLDL) is consistent with post-translational modification or subcellular trafficking.

Objective

To test the hypotheses that OxLDL triggers reverse translocation of mitochondrial arginase 2 (Arg2) to cytosol and Arg2 activation, and that this process is dependent on mitochondrial processing peptidase, lectin-like OxLDL receptor-1 receptor, and rho kinase.

Methods and results

OxLDL-triggered translocation of Arg2 from mitochondria to cytosol in human aortic endothelial cells and in

SUBMITTER: Pandey D 

PROVIDER: S-EPMC8760889 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature