Accumulation of Maillard reaction products in skin collagen in diabetes and aging

To investigate the contribution of glycation and oxidation reactions to the modification of insoluble collagen in aging and diabetes, Maillard reaction products were measured in skin collagen from 39 type 1 diabetic patients and 52 nondiabetic control subjects. Compounds studied included fructoselys...

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Bibliographic Details
Published in:The Journal of clinical investigation 1993-06, Vol.91 (6), p.2463-2469
Main Authors: DYER, D. G, DUNN, J. A, THORPE, S. R, BAILIE, K. E, LYONS, T. J, MCCANCE, D. R, BAYNES, J. W
Format: Article
Language:English
Subjects:
Adolescent
Adult
Aged
Aged, 80 and over
Aging
Arginine - analogs & derivatives
Arginine - analysis
Associated diseases and complications
Biological and medical sciences
Collagen - chemistry
Diabetes Mellitus, Type 1 - metabolism
Diabetes. Impaired glucose tolerance
Endocrine pancreas. Apud cells (diseases)
Endocrinopathies
Female
Glycosylation
Humans
Lysine - analogs & derivatives
Lysine - analysis
Maillard Reaction
Male
Medical sciences
Middle Aged
Oxidation-Reduction
Skin - chemistry
Spectrometry, Fluorescence
Spectrophotometry, Ultraviolet
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Summary:To investigate the contribution of glycation and oxidation reactions to the modification of insoluble collagen in aging and diabetes, Maillard reaction products were measured in skin collagen from 39 type 1 diabetic patients and 52 nondiabetic control subjects. Compounds studied included fructoselysine (FL), the initial glycation product, and the glycoxidation products, N epsilon-(carboxymethyl) lysine (CML) and pentosidine, formed during later Maillard reactions. Collagen-linked fluorescence was also studied. In nondiabetic subjects, glycation of collagen (FL content) increased only 33% between 20 and 85 yr of age. In contrast, CML, pentosidine and fluorescence increased five-fold, correlating strongly with age. In diabetic patients, collagen FL was increased threefold compared with nondiabetic subjects, correlating strongly with glycated hemoglobin but not with age. Collagen CML, pentosidine and fluorescence were increased up to twofold in diabetic compared with control patients: this could be explained by the increase in glycation alone, without invoking increased oxidative stress. There were strong correlations among CML, pentosidine and fluorescence in both groups, providing evidence for age-dependent chemical modification of collagen via the Maillard reaction, and acceleration of this process in diabetes. These results support the description of diabetes as a disease characterized by accelerated chemical aging of long-lived tissue proteins.
ISSN:0021-9738
1558-8238
DOI:10.1172/jci116481