Diabetes enhances lectin-like oxidized LDL receptor-1 (LOX-1) expression in the vascular endothelium: possible role of LOX-1 ligand and AGE

M Chen, M Nagase, T Fujita, S Narumiya… - Biochemical and …, 2001 - Elsevier
M Chen, M Nagase, T Fujita, S Narumiya, T Masaki, T Sawamura
Biochemical and biophysical research communications, 2001Elsevier
Diabetes mellitus accelerating atherosclerosis was associated with the enhanced
glycoxidative modification of lipoproteins. LOX-1, the endothelial oxidized LDL receptor
might be involved in the pathogenesis of diabetic atherosclerosis. In this study, we examined
the vascular expression of LOX-1 in streptozotocin-induced diabetic rats. We found that LOX-
1 was significantly increased in diabetic rat aorta compared with nondiabetic control.
Immunohistochemistry revealed that the most distinctive staining of LOX-1 was in the …
Diabetes mellitus accelerating atherosclerosis was associated with the enhanced glycoxidative modification of lipoproteins. LOX-1, the endothelial oxidized LDL receptor might be involved in the pathogenesis of diabetic atherosclerosis. In this study, we examined the vascular expression of LOX-1 in streptozotocin-induced diabetic rats. We found that LOX-1 was significantly increased in diabetic rat aorta compared with nondiabetic control. Immunohistochemistry revealed that the most distinctive staining of LOX-1 was in the endothelial cells, especially in the bifurcations of artery branches from aorta. In cultured aortic endothelial cells, diabetic rat serum and advanced glycation endproducts–BSA induced LOX-1 expression, while control rat serum along with high glucose did not. Applying a competitive inhibition assay, we found that LOX-1 ligand activity was accumulated in the diabetic rat serum, mainly in VLDL/LDL fractions. In addition, VLDL/LDL prominently increased LOX-1 among all the lipoprotein fractions of diabetic rat serum. In conclusion, diabetes markedly upregulated LOX-1 expression in the aortic endothelial cells. The enhanced glycoxidative modification of lipoproteins may contribute to the underlying mechanisms.
Elsevier