Lectin-like oxidized LDL receptor-1 (LOX-1) was initially identified as an
oxidized LDL receptor in aortic endothelial cells. Here we identified LOX-1
mRNA and protein in human platelets in addition to recent findings on the
expression in macrophages and smooth muscle cells. The presence of LOX-1 wa
s further confirmed in the megakaryocytic cell lines. Flow cytometric analy
ses revealed that LOX-1 was exposed on the surface of platelets in an activ
ation-dependent manner. Consistently, the activation-dependent binding of O
xLDL to platelets was mostly inhibited by anti-LOX-1 antibody. Immunohistoc
hemistry of the atherosclerotic plaque from a patient with unstable angina
pectoris (UAP) revealed accumulation of LOX-1 protein at the site of thromb
us, As LOX-1 recognizes and binds activated platelets, exposure of LOX-1 on
activated platelets surface might assist thrombosis formation. (C) 2001 Ac
ademic Press.