Interference of Advanced Glycation End-products signaling with collagen cross-linking in human endothelium
Kandaraki, Eleni A.
Spyropoulou, Anastasia
Gargalionis, Antonios N.
Papavassiliou, Athanasios. G.
Adamopoulos, Christos
Piperi, Christina
Korkolopoulou, Penelope
Dalagiorgou, Georgia
Maintenance of extracellular matrix (ECM) stability is critical for vascular remodeling associated with cardiovascular diseases. Covalent cross-linking of collagen and elastin initiated by the copper-dependent lysyl oxidase (LOX) is a central event assuring ECM stability and vascular homeostasis. LOX downregulation leads to endothelial dysfunction characteristic of early atherosclerotic stages, whereas its upregulation in vascular cells can induce neointimal thickening in atherosclerosis and restenosis. Advanced Glycation End-products (AGEs), the highly reactive products of non-enzymatic glycation of proteins, lipids and nucleic acids, contribute to endothelial dysfunction, atherosclerosis and vascular injury under both normal and diabetic conditions.
The aim of the present study was to investigate the effect of AGEs in regulation of LOX gene/protein expression in human endothelial cells and to explore the potential functional impact of this interaction in an animal model.
