1984
DOI: 10.1073/pnas.81.2.583
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Accelerated age-related browning of human collagen in diabetes mellitus.

Abstract: The nonenzymatic glycosylation reaction that is accelerated in diabetes is the first step of the Maillard or nonenzymatic browning reaction that occurs in stored food. The glucose-protein adduct rearranges and dehydrates to form brown and fluorescent pigments, which can act as crosslinks, resulting in decreased protein solubility and altered mechanical properties. Evidence suggesting that this process occurs in vivo has been found in lens crystallins. The observation that nonenzymatic glycosylation and insolub… Show more

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Cited by 624 publications
(380 citation statements)
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“…Further, inhibitors of lysyl oxidase can prevent the insolubilization of collagens in diabetes [69], also suggesting that the increase in cross-linking may be due to induction of enzymatic pathways. Non-enzymatic glycosylation may also be involved, however, since some recent studies have shown that solubilized dermal collagen from juvenile-onset diabetic patients is browner and more fluorescent than collagen from agematched control subjects [70]. The absorbance and fluorescence spectra of the diabetic collagens were different from those of normal collagen, and strikingly similar to those produced by melanoidins formed in browning reactions between protein and glucose in vitro.…”
Section: Extracellular Matrix Proteinsmentioning
confidence: 98%
See 1 more Smart Citation
“…Further, inhibitors of lysyl oxidase can prevent the insolubilization of collagens in diabetes [69], also suggesting that the increase in cross-linking may be due to induction of enzymatic pathways. Non-enzymatic glycosylation may also be involved, however, since some recent studies have shown that solubilized dermal collagen from juvenile-onset diabetic patients is browner and more fluorescent than collagen from agematched control subjects [70]. The absorbance and fluorescence spectra of the diabetic collagens were different from those of normal collagen, and strikingly similar to those produced by melanoidins formed in browning reactions between protein and glucose in vitro.…”
Section: Extracellular Matrix Proteinsmentioning
confidence: 98%
“…A strong case exists for glycosylation as a potential source of collagen abnormalities in diabetes, based on the recent observation of non-enzymatic type browning and fluorescence of diabetic collagen [70]; but evidence for the occurrence of the browning reaction in vivo is still circumstantial. One of the serious problems with research in this area is that browning, fluorescence, insolubility and indigestibility of collagen are relatively imprecise terms.…”
Section: Significance Of Protein Glycosylationmentioning
confidence: 99%
“…In addition, general measures of glycation-derived cross-links, i.e. browning and Maillard-type fluorescence [12], were determined. Modification of arginine, lysine and hydroxylysine residues in cartilage collagen was also determined as a possible measure of overall glycation and AGE formation.…”
Section: Introductionmentioning
confidence: 99%
“…In subsequent Maillard or browning reactions, products known as advanced glycation end products (AGEs) are formed from FL [3,4], and accumulate with age in long-lived proteins [1,2,[5][6][7][8]. These AGEs include structurally characterized adducts, such as N ε -(carboxymethyl)lysine (CML) [1][2][3] and N ε -(carboxyethyl)-lysine (CEL) [9], fluorescent cross-links, such as pentosidine formed between lysine and arginine residues [5,10], as well as chemically unidentified compounds which result in proteinbound browning or fluorescence, and cross-linking [11][12][13][14].In comparison with other collagen-rich tissues such as skin, cartilage contains relatively large amounts of pentosidine [5,15]. Pentosidine levels in articular cartilage increase linearly with age [6-8], as was previously described for skin collagen [16] and lens proteins [10].…”
mentioning
confidence: 99%
“…Pentosidine, a fluorescent AGE formed by lysine and arginine residues, is often used for this purpose (16). AGEs are formed in all proteins, and since they can only be removed from the body when the protein is removed, AGEs accumulate in long-lived proteins such as collagens (17,18). In human articular cartilage, a tissue with extremely slow turnover (half-life of type II collagen Ͼ100 years), pentosidine levels increase 50-fold from age 20 years to age 80 years (18)(19)(20)(21)(22).…”
mentioning
confidence: 99%