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  • 1
    ISSN: 1432-5233
    Keywords: Ascorbate ; Collagen ; Diabetic complications ; Glycation ; Pentosidine ; Retinopathy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Recent work has led to the structural elucidation of three compounds of the advanced Maillard reaction-pyrraline, pentosidine and carboxymethyllysine-which can serve as markers for in vivo studies. Pyrraline is a glucose-derived compound, the presence of which was detected with a monoclonal antibody in elevated amounts in the plasma of diabetic individuals and rodents and in histological sections of renal tissue, especially in sclerosed glomerular and arteriolar regions. The immediate precursor of pyrraline is 3-deoxyglucosone (3-DG), a product formed through degradation of glycated proteins. 3-DG is present in elevated levels in plasma and urine from diabetic humans. Pentosidine is a pentose-derived protein crosslink, which forms from glycated proteins in the presence of oxygen. Pentosidine increases ubiquitously in aging tissues, and at an accelerated rate in diabetes and especially in uraemia. Skin pentosidine levels correlate with the severity of diabetic complications in type I (insulin-dependent) diabetes. Its levels, like those of carboxymethyllysine, an Amadori fragmentation and oxidation product, are not reversible upon tight control of diabetes over a 4-month period. Assuming these advanced products reflect cumulative glycaemia over several years, it would appear that there is a correlation between the severity of complications and total exposure to glucose.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0263-6484
    Keywords: glycation ; oxidation ; irradiation ; fluorescence ; albumin ; free radicals ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Oxidation and glycation are non-enzymatic protein modifications involved in the pathogenesis of aging. We evaluated their possible influences in an in vitro system: albumin was oxidized by gamma-irradiation and then exposed to glycation in vitro. Fluorescence modifications were analysed as signals of protein alterations. Both radiolytic oxidation and in vitro glycation provoked a sharp decrease of tryptophan fluorescence (278 nm ex./340 nm em.); their effects tended to be additive, unless a saturation limit was reached. Both individually and in combination, these two non-enzymatic processes induced the appearance of a new fluorescence (335 nm ex./415 nm em.); in this case as well there was an additive effect, with a trend toward saturation. Radiolytic oxidation and in vitro glycation seem to provoke similar damage to the exposed proteins: the observed fluorescence alterations may be due to similar conformational changes, breaks or the development of fluorophores.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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