Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10759148 | Biochemical and Biophysical Research Communications | 2013 | 6 Pages |
Abstract
Lectin-like oxidized low-density lipoprotein (LDL) receptor-1 (LOX-1) is an endothelial scavenger receptor that is important for oxidized low-density lipoprotein uptake. LOX-1 functions as an oligomer; however, little is known about the oligomeric complex and ligand processing after recognition by LOX-1. Here, we found that LOX-1 recognized and internalized ligands through the caveolae/raft-dependent endocytosis pathway in human coronary artery endothelial cells. Furthermore, we demonstrated that LOX-1 was palmitoylated and that both cysteine 36 and cysteine 46 were necessary for the recruitment of LOX-1 into raft microdomains and for its ligand uptake ability.
Keywords
AcLDLCT-BCAV1LOX-1oxLDLBiotin-HPDPDRMSPalmitoylationHCAECN-ethylmaleimide2BP2-BromopalmitateCaveolaehuman coronary artery endothelial cellsDetergent-resistant membranesacetylated low-density lipoproteinOxidized low-density lipoproteinLow-density lipoproteinLDLNEMHydroxylaminecaveolin-1cholera toxin subunit BLectin-like oxidized low-density lipoprotein receptor-1
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Authors
Miyuki Kumano-Kuramochi, Qiuhong Xie, Shoko Kajiwara, Shiro Komba, Takashi Minowa, Sachiko Machida,