Abstract:
:Lectin-like oxidized low-density lipoprotein receptor (LOX-1) is a scavenger receptor that binds oxidized low-density lipoprotein (OxLDL) and has a role in atherosclerosis development. The N-terminus intracellular region (cytoplasmic domain) of LOX-1 mediates receptor internalization and trafficking, potentially through intracellular protein interactions. Using affinity isolation, we identified 6 of the 8 components of the chaperonin-containing TCP-1 (CCT) complex bound to LOX-1 cytoplasmic domain, which we verified by coimmunoprecipitation and immunostaining in human umbilical vein endothelial cells. We found that the interaction between CCT and LOX-1 is direct and ATP-dependent and that OxLDL suppressed this interaction. Understanding the association between LOX-1 and the CCT complex may facilitate the design of novel therapies for cardiovascular disease.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Bakthavatsalam D,Soung RH,Tweardy DJ,Chiu W,Dixon RA,Woodside DGdoi
10.1016/j.febslet.2014.04.049subject
Has Abstractpub_date
2014-06-13 00:00:00pages
2133-40issue
13eissn
0014-5793issn
1873-3468pii
S0014-5793(14)00372-Xjournal_volume
588pub_type
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