Determination of anti-AGE antibodies in human serum

Baydanoff, S; Konova, E; Иванова, Н. Е.

doi:10.1007/bf00731464

Cited by 22 publications

(22 citation statements)

References 13 publications

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“…As a consequence, new AGE epitopes are formed in and between the chains. In our previous investigation [38] , anti-AGE autoantibodies, common for glycated proteins, were studied. Our future aims are to investigate and compare the antigenic characteristics of glycated and unmodified fibrillins.…”

Section: Discussionmentioning

confidence: 99%

Non-Enzymatic Glycation of Human Fibrillin-1

Atanasova¹,

Konova²,

Betova

et al. 2008

Gerontology

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Non-enzymatic glycation of proteins is one of the key mechanisms in the pathogenesis of diabetic complications and may be significant in the age-related changes of tissues. We isolated and investigated the in vitro glycation of human aortic fibrillin-1. Fibrillin-1 was prepared from thoracic aortas of 9 accident victims distributed in three age groups. The purity of isolated fibrillin-1 was proved. It was glycated by incubating with different glucose concentrations in 0.2 M phosphate buffer, pH 7.4, for 30 days, at 37°C. The degree of early products of glycation was measured by two colorimetric methods, i.e. nitroblue tetrazolium and 2-thiobarbituric acid. Advanced glycation end products (AGEs) were determined by fluorescence measurement. The highest level of early products of glycation was found on day 2 after the beginning of incubation for the fibrillin-1 isolated from the youngest group. Fluorescence in the age groups, as an index of advanced glycation, consistently increased between days 6 and 24. The fibrillin-1 isolated from the youngest group had the highest capacity to form fructosamine and AGEs under glycation in vitro. The capacity of glycation of the ‘oldest’ fibrillin did not increase significantly during the incubation. Investigation of the properties of glycated fibrillin-1 will help to understand the importance of this long-lived protein to age-related changes in tissues and for diabetic complications.

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Section: Discussionmentioning

confidence: 99%

Non-Enzymatic Glycation of Human Fibrillin-1

Atanasova¹,

Konova²,

Betova

et al. 2008

Gerontology

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“…In order to elicit an immune response, a molecule must be recognized as non-self by the biological system. Proteins containing AGE are highly immunogenic and anti-AGE antibodies have been found in the sera of patients with diabetes (Reddy et al, 1995;Shibayama et al, 1999;Baydanoff et al, 1996). Several AGE structures have been identified including pyrraline, pentosidine (Sell & Monnier 1989), (carboxymethyl)lysine (Ahmed et al, 1986), and crosslines (Nakamura et al, 1992).…”

Section: Autoantibodies In Diabetes Complicationsmentioning

confidence: 99%

“…These increased serum levels of AGE can predict changes in microvascular morphology in patients with diabetic retinopathy. Proteins containing AGE are highly immunogenic (Reddy et al, 1995) and anti-AGE antibodies were found in the sera of patients with diabetes (Shibayama et al, 1999;Baydanoff et al, 1996). Our research team has hypothesized that increase in the titre of anti-AGE antibodies has a direct role in the pathogenesis of diabetes microvascular complications especially diabetic retinopathy.…”

Section: Introductionmentioning

confidence: 99%

Gluco-Oxidation of Proteins in Etiology of Diabetic Retinopathy

Khan¹,

Banga²,

Khan³

2012

Diabetic Retinopathy

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“…These antibodies recognize and react with AGE-epitopes regardless of the proteins they have been formed on. Assessment of the levels of these antibodies shows that they are present at low titres even in sera of healthy subjects, perhaps as a part of homeostatic mechanism which clears glycated structures via in situ destruction or via opsonization of the gflycated proteins and products of their degradation (Baydanoff et al, 1996). However, in the conditions of increased nonenzymatic glycation the homeostatic control is inefficient and the generation of these antibodies increases (Baydanoff et al, 1996).…”

Section: Introductionmentioning

confidence: 99%