Document Detail


Oxidative glycation and free radical production: a causal mechanism of diabetic complications.
MedLine Citation:
PMID:  1649079     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Glucose may oxidise under physiological conditions and lead to the production of protein reactive ketoaldehydes, hydrogen peroxide and highly reactive oxidants. Glucose is thus able to modify proteins by the attachment of its oxidation derived aldehydes, leading to the development of novel protein fluorophores, as well as fragment protein via free radical mechanisms. The fragmentation of protein by glucose is inhibitable by metal chelators such as diethylenetriamine pentaacetic acid (DETAPAC) and free radical scavengers such as benzoic acid, and sorbitol. The enzymic antioxidant, catalase, also inhibits protein fragmentation. Protein glycation and protein oxidation are inextricably linked. Indeed, using boronate affinity chromatography to separate glycated from non-glycated material, we demonstrate that proteins which are glycated exhibit an enhanced tryptophan oxidation. Our observation that both glycation and oxidation occur simultaneously further supports the hypothesis that tissue damage associated with diabetes and ageing has an oxidative origin.
Authors:
J V Hunt; S P Wolff
Related Documents :
10101259 - In vivo modulation of rodent glutathione and its role in peroxynitrite-induced neocorti...
9033259 - Immunohistochemical detection of 4-hydroxy-2-nonenal adducts in alzheimer's disease is ...
14706859 - Copper-induced oxidative stress in saccharomyces cerevisiae targets enzymes of the glyc...
16690189 - Esr and nmr spectroscopy studies on protein oxidation and formation of dityrosine in em...
19354299 - Mapping protein-protein interactions by localized oxidation: consequences of the reach ...
12014829 - Hormetic action of mild heat stress decreases the inducibility of protein oxidation and...
23157399 - Chemically-modified tandem repeats in proteins - natural combinatorial peptide libraries.
8707049 - Targeting aequorin and green fluorescent protein to intracellular organelles.
22226179 - Expression of cytoskeleton and energetic metabolism-related proteins at human abdominal...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Free radical research communications     Volume:  12-13 Pt 1     ISSN:  8755-0199     ISO Abbreviation:  Free Radic. Res. Commun.     Publication Date:  1991  
Date Detail:
Created Date:  1991-08-22     Completed Date:  1991-08-22     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8709453     Medline TA:  Free Radic Res Commun     Country:  SWITZERLAND    
Other Details:
Languages:  eng     Pagination:  115-23     Citation Subset:  IM    
Affiliation:
Department of Clinical Pharmacology, University College London.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Aging / metabolism
Aldehydes / metabolism
Animals
Benzoates / pharmacology
Benzoic Acid
Cattle
Chelating Agents / pharmacology
Chromatography, Affinity
Diabetes Complications*
Diabetes Mellitus / metabolism
Free Radical Scavengers
Free Radicals*
Glucose / metabolism*
Humans
Hydrogen Peroxide / metabolism
Hydroxides / metabolism
Hydroxyl Radical
Oxidation-Reduction
Pentetic Acid / pharmacology
Proteins / metabolism
Sorbitol / pharmacology
Chemical
Reg. No./Substance:
0/Aldehydes; 0/Benzoates; 0/Chelating Agents; 0/Free Radical Scavengers; 0/Free Radicals; 0/Hydroxides; 0/Proteins; 3352-57-6/Hydroxyl Radical; 50-70-4/Sorbitol; 50-99-7/Glucose; 65-85-0/Benzoic Acid; 67-43-6/Pentetic Acid; 7722-84-1/Hydrogen Peroxide

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Ferritin, lipid peroxidation and redox-cycling xenobiotics.
Next Document:  Tetravalent vanadium releases ferritin iron which stimulates vanadium-dependent lipid peroxidation.