Mixed dimers formed by crosslinking of native and glycated proteins in the absence of free sugar.
After a hyperglycaemic episode, glycated proteins remain in the body until removed by protein turnover. We have shown that in the absence of free sugar, such proteins can crosslink to native proteins, forming mixed dimers. They can also induce native proteins to crosslink into homodimers, presumably by release of a soluble crosslinking agent. Similar reactions in vivo could be responsible for the deposition of serum proteins in diabetic kidney, nerve and other tissues. Exposure to glycating sugar for brief periods, or a low concentration, still produced glycated protein capable of crosslinking to other proteins under sugar-free conditions. These crosslinks are nonfluorescent, unlike the advanced glycation endproducts usually observed.
Liggins
J
J
Open University, Oxford Research Unit, England.
Furth
A J
AJ
D003432:Cross-Linking Reagents; D003920:Diabetes Mellitus / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005632:Fructose; D017127:Glycation End Products, Advanced / Q000032:analysis*; D006031:Glycosylation; D006801:Humans; D006943:Hyperglycemia; D007782:Lactoglobulins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D046911:Macromolecular Substances; D009113:Muramidase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D013050:Spectrometry, Fluorescence
D003432:Cross-Linking Reagents; D017127:Glycation End Products, Advanced; D007782:Lactoglobulins; D046911:Macromolecular Substances; D005632:Fructose; D009113:Muramidase