Open AccessOxLDL Triggers Retrograde Translocation of Arginase2 in Aortic Endothelial Cells via ROCK and Mitochondrial Processing Peptidase
Author(s) -
Deepesh Pandey,
Anil K. Bhunia,
Young Jun Oh,
Fumin Chang,
Yehudit Bergman,
Jae Hyung Kim,
Janna Serbo,
Tatiana Boronina,
Robert N. Cole,
Jennifer E. Van Eyk,
Alan T. Remaley,
Dan E. Berkowitz,
Lewis H. Romer
Publication year - 2014
Publication title -
circulation research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.899
H-Index - 336
eISSN - 1524-4571
pISSN - 0009-7330
DOI - 10.1161/circresaha.115.304262
Subject(s) - arginase , mitochondrion , microbiology and biotechnology , cytosol , biology , chemistry , biochemistry , arginine , enzyme , amino acid
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.
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