Protein glycation: its role in the changes induced by diabetes in the properties of the serum insulin-like growth factor-I binding proteins.

摘要: The purpose of this work was to study the effect diabetes on 125I-labelled insulin-like growth factor (IGF) binding specific serum proteins (IGFBPs) and possible role protein glycation in such an effect. Accordingly, ligand blotting fructosamine assays were performed samples from diabetic non-diabetic eSS rats as well normal rat previously incubated with different concentrations glucose. IGFBPs molecular weights 24, 30 40 kDa identified rats. 125I-Labelled IGF-I each these fractions increased significantly IGFBP-40 a function degree proteins. Conversely, IGFBP-24 IGFBP-30 related only glucose concentration attained at 120 min during oral tolerance test. Glycation labelled incubation media. In in-vitro glycated sera, significantly; increase closely amount glycation. No clear reproducible changes occurred fractions. These results confirm capacity reported animals. They also show that IGFBP fraction is regulated by mechanism; whereas induces IGFBP-40, mechanism does not affect properties other two IGFBPs. might availability free IGF-I, consequent alterations IGF-I-dependent metabolic processes could explain pathogenesis chronic complications diabetes.