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Amadori‐glycated phosphatidylethanolamine induces angiogenic differentiations in cultured human umbilical vein endothelial cells
Author(s) -
Oak Jeong-Ho,
Nakagawa Kiyotaka,
Oikawa Shinichi,
Miyazawa Teruo
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01237-7
Subject(s) - umbilical vein , phosphatidylethanolamine , amadori rearrangement , chemistry , microbiology and biotechnology , glycation , biochemistry , biology , receptor , in vitro , phosphatidylcholine , phospholipid , membrane
Glycation has been implicated in the endothelial dysfunction that contributes to both diabetes‐ and aging‐associated vascular complications. The aim of the present study was to determine whether Amadori‐glycated phosphatidylethanolamine (Amadori‐PE), a lipid‐linked glycation compound that is formed at an increased rate in hyperglycemic states, affected proliferation, migration and tube formation of cultured human umbilical vein endothelial cells (HUVEC). Amadori‐PE at a low concentration of less than 5 μM significantly enhanced these three factors involved in angiogenesis. Furthermore, stimulation of HUVEC with Amadori‐PE resulted in secretion of matrix metalloproteinase 2 (MMP‐2), a pivotal enzyme in the initial step of angiogenesis. Our results demonstrated for the first time that Amadori‐PE may be an important compound that promotes vascular disease as a result of its angiogenic activity on endothelial cells. We also demonstrated that MMP‐2 is a primary mediator of Amadori‐PE‐driven angiogenesis.