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Binding of mannose-binding lectin to fructosamines: a potential link between hyperglycaemia and complement activation in diabetes 0comments
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  • published in 2010-04-23 03:09:00 
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  • Complement activation via the MBL pathway has been proposed to play a role in the pathogenesis of diabetic complications. As protein glycation is increased in diabetes we tested the possibility t ...
  • Complement activation via the MBL pathway has been proposed to play a role in the pathogenesis of diabetic complications. As protein glycation is increased in diabetes we tested the possibility that the glycation production fructoselysine is a ligand for MBL and that its interaction with this protein may inaugurate complement activation.We investigated the binding of MBL to fructoselysine by chromatography of human serum on fructoselysine-Sepharose followed by Western blot and mass spectrometry analysis. We also performed enzyme-linked immunosorbent assays using purified MBL and fructoselysine-derivatized (binding assay) or mannan-coated plates (inhibition assay). Complement activation was determined by the fixation of C3d following incubation of fructoselysine-derivatized plates with serum from subjects with different levels of MBL.MBL and its associated proteases were selectively purified from serum by chromatography on fructoselysine-Sepharose. Competition experiments indicated that MBL had a comparable affinity for mannose fructose and fructoselysine. MBL bound in a highly cooperative manner to fructoselysine-derivatized plates. This binding was associated with complement activation and was much lower with serum from subjects with low-MBL genotypes.MBL binding to fructoselysine and the ensuing complement activation may supply a physiopathological link between enhanced glycation and complement activation in diabetes. The cooperative character of this binding may interpre the high sensitivity of diabetic complications to hyperglycaemia. Copyright 漏 2010 John Wiley & Sons Ltd.
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