Linked Life Data

8168645

Source:http://linkedlifedata.com/resource/pubmed/id/8168645

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1994-6-2
pubmed:abstractText
The Maillard or browning reaction between sugar and protein contributes to the increased chemical modification and cross-linking of long-lived tissue proteins in diabetes. To evaluate the role of glycation and oxidation in these reactions, we have studied the effects of oxidative and antioxidative conditions and various types of inhibitors on the reaction of glucose with rat tail tendon collagen in phosphate buffer at physiological pH and temperature. The chemical modifications of collagen that were measured included fructoselysine, the glycoxidation products N epsilon-(carboxymethyl)lysine and pentosidine and fluorescence. Collagen cross-linking was evaluated by analysis of cyanogen bromide peptides using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and by changes in collagen solubilization on treatment with pepsin or sodium dodecylsulfate. Although glycation was unaffected, formation of glycoxidation products and cross-linking of collagen were inhibited by antioxidative conditions. The kinetics of formation of glycoxidation products proceeded with a short lag phase and were independent of the amount of Amadori adduct on the protein, suggesting that autoxidative degradation of glucose was a major contributor to glycoxidation and cross-linking reactions. Chelators, sulfhydryl compounds, antioxidants, and aminoguanidine also inhibited formation of glycoxidation products, generation of fluorescence, and cross-linking of collagen without significant effect on the extent of glycation of the protein. We conclude that autoxidation of glucose or Amadori compounds on protein plays a major role in the formation of glycoxidation products and cross-liking of collagen by glucose in vitro and that chelators, sulfhydryl compounds, antioxidants, and aminoguanidine act as uncouplers of glycation from subsequent glycoxidation and cross-linking reactions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0012-1797
pubmed:author
pubmed:issnType
Print
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
676-83
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8168645-Animals, pubmed-meshheading:8168645-Antioxidants, pubmed-meshheading:8168645-Arginine, pubmed-meshheading:8168645-Chelating Agents, pubmed-meshheading:8168645-Chromatography, High Pressure Liquid, pubmed-meshheading:8168645-Collagen, pubmed-meshheading:8168645-Cross-Linking Reagents, pubmed-meshheading:8168645-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:8168645-Female, pubmed-meshheading:8168645-Glucose, pubmed-meshheading:8168645-Glycosylation, pubmed-meshheading:8168645-Kinetics, pubmed-meshheading:8168645-Lysine, pubmed-meshheading:8168645-Maillard Reaction, pubmed-meshheading:8168645-Oxidation-Reduction, pubmed-meshheading:8168645-Pentetic Acid, pubmed-meshheading:8168645-Rats, pubmed-meshheading:8168645-Rats, Sprague-Dawley, pubmed-meshheading:8168645-Spectrometry, Fluorescence, pubmed-meshheading:8168645-Tendons
pubmed:year
1994
pubmed:articleTitle
Glycation, glycoxidation, and cross-linking of collagen by glucose. Kinetics, mechanisms, and inhibition of late stages of the Maillard reaction.
pubmed:affiliation
Department of Chemistry and Biochemistry, University of South Carolina, Columbia 29208.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.