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Antibodies in NIDDM serum binding to advanced glycation modified proteins (CROSBI ID 472284)

Prilog sa skupa u časopisu | sažetak izlaganja sa skupa | međunarodna recenzija

Turk, Zdenka ; Ljubić, Spomenka ; Benko, Bojan ; Granić, Mate Antibodies in NIDDM serum binding to advanced glycation modified proteins // Diabetologia (Berlin) / Ferannini, E. (ur.). 1999. str. A57-A57

Podaci o odgovornosti

Turk, Zdenka ; Ljubić, Spomenka ; Benko, Bojan ; Granić, Mate

engleski

Antibodies in NIDDM serum binding to advanced glycation modified proteins

The evidence that advanced glycation endproducts (AGEs) have antigenic properties have led to a hypothesis that AGE as an antigen being continuously formed in a diabetic body may arouse an autoimmune response. The aim of this study was to investigate the AGE level and anti-AGE response in NIDDM patients (35 without microangiopathy and 15 with nephropathy and/or retinopathy), and in 20 nondiabetic controls. Competitive ELISA was developed to measure AGEs in serum, and inhibition assay was used to detect anti-AGE response. A purified immunoglobulin fraction from human plasma (4500 healthy donors) of normal subclass distribution was used as a standard. AGE- modified IgG was used as antigen to detect anti- IgG-AGE positive samples. The binding inhibition assay showed a significant difference between diabetic subjects and nondiabetic controls (36.2ą3.9% vs 26.4ą3.6%, p<0.0004) (meanąSE). There also was a significant difference in AGE levels between diabetic patients and control subjects (51.6ą4.2 vs 19.8ą1.7 AU/mg, p<0.001). The binding inhibition percentage differed between the diabetics with nephropathy and/or retinopathy (42.0ą7.2%), and those free from complications (33.5ą4.6%), but the difference was not statistically significant. Spearman correlation showed an inverse relationship between the binding inhibition percentage and parameters of nonenzymatic glycation, HbA1c (r= -0.4, p<0.002) and AGE level (r= -0.35, p<0.004). Anti-IgG-AGE positive individuals were detected in both NIDDM groups. These data indicate a stronger immune response to proteins modified by advanced glycation in diabetic subjects than in healthy age-matched controls. Long-term presence of both antigens and antigen-specific antibodies might be the cause of a series of undesired phenomena. There is a possibility that antiAGEab form immune complexes which are believed to have a role in atherogenesis. Therefore, additional studies are needed to establish the role and significance of autoantibodies against AGEs in atherogenic processes in diabetes.

diabetes; advanced glycation; autoantibodies

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Podaci o prilogu

A57-A57.

1999.

nije evidentirano

objavljeno

Podaci o matičnoj publikaciji

Diabetologia (Berlin)

Ferannini, E.

Heidelberg: Springer

0012-186X

Podaci o skupu

Aannual Meeting of the European Association for the Study of Diabetes

pozvano predavanje

28.09.1999-03.10.1999

Bruxelles, Belgija

Povezanost rada

Kliničke medicinske znanosti

Indeksiranost