Angiogenic potency of Amadori-glycated phosphatidylethanolamine.
Glycation has been thought to participate in diabetic vascular diseases. However, there are no reports about the effects of lipid glycation on endothelial dysfunction. In this study, we have evaluated whether Amadori-glycated phosphatidylethanolamine (Amadori-PE), a lipid-linked glycation compound, affected proliferation, migration, and tube formation of cultured human umbilical vein endothelial cells. These three factors involved in angiogenesis were significantly stimulated by Amadori-PE at a low concentration of less than 5 microM. Furthermore, Amadori-PE also stimulated the secretion of matrix metalloproteinase-2 (MMP-2), a pivotal enzyme in the initial step of angiogenesis. Our results indicated for the first time that Amadori-PE would elicit vascular disease through angiogenic potency on endothelial cells, thereby playing an active part in the development and progression of diabetic microangiopathy.
Nakagawa
Kiyotaka
K
Food and Biodynamic Chemistry Laboratory, Graduate School of Agricultural Science, Tohoku University, Sendai 981-8555, Japan.
Oak
Jeong-Ho
JH
Miyazawa
Teruo
T
D002455:Cell Division / Q000187:drug effects; D002465:Cell Movement / Q000187:drug effects; D002478:Cells, Cultured; D004730:Endothelium, Vascular / Q000166:cytology* / Q000187:drug effects / Q000502:physiology*; D017127:Glycation End Products, Advanced; D006031:Glycosylation; D006801:Humans; D020778:Matrix Metalloproteinase 2 / Q000378:metabolism; D009389:Neovascularization, Pathologic / Q000473:pathology / Q000503:physiopathology; D010714:Phosphatidylethanolamines / Q000494:pharmacology*; D014471:Umbilical Veins
D017127:Glycation End Products, Advanced; D010714:Phosphatidylethanolamines; D020778:Matrix Metalloproteinase 2