English to Russian Medical

2) Effects of advanced glicosilation end products on endothelial cell proliferation and metabolism
Advanced glicosilation end products (AGE) are generated from non enzymatic glicosilation of different proteins when they are exposed to high concentration of glucose. Their plasmatic concentration is particularly elevated in elderly subjects or diabetic patients. AGE proteins are able to induce a dose-dependent proliferation of endothelial cells in vitro and, in vivo, in the rabbit cornea assay. AGE proteins exert their effect through specific cellular receptors. These have been characterized in collaboration with Molecular Biology Laboratories of Merck & Co: three proteins with MW of 40, 60, and 80 kDa have been isolated. The 40 kDa protein, which appears to play a critical role in signal transduction, has been cloned (RAGE). Neutralizing antibodies anti-RAGE inhibit the endothelial cell proliferation induced by AGE proteins. The soluble form of the receptor, obtained in recombinant form, inhibit the binding of radiolabeled AGE proteins on endothelial cells and their biologic effects. AGE proteins induce endothelial cell proliferation by interfering in the FGF/FGF receptor system. The proliferative effect was reduced more than 70 % when neutralizing monoclonal anti-bFGF antibodies were added in the culture medium. Since AGE proteins did not modulate FGF receptor expression or FGF synthesis by endothelial cells it is believed that they act through an increase in the availability of FGF bound to the extracellular matrix.