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The dicarbonyl proteome - proteins susceptible to dicarbonyl glycation at functional sites in health, aging, and disease

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Rabbani, Naila and Thornalley, Paul J. (2008) The dicarbonyl proteome - proteins susceptible to dicarbonyl glycation at functional sites in health, aging, and disease. In: 9th International Symposium on the Maillard Reaction, Munich, Germany, Sep, 2007. Published in: Annals of the New York Academy of Sciences, Vol.1126 pp. 124-127.

Full text not available from this repository.
Official URL: http://dx.doi.org/10.1196/annals.1433.043

Abstract

Reactive, physiological, dicarbonyl, glycating agents, glyoxal and methylglyoxal, are arginine-directed glycating agents forming mainly hydroimidazolone residues. Arginine residues have high-frequency occurrence in sites of protein-protein, enzyme substrate and protein-nucleotide binding sites. There is emerging evidence that functionally important arginine residues in proteins are often activated toward dicarbonyl glycation-leading to functional impairment. When uncontrolled, this is associated with aging, degenerative diseases, and metabolic disorders where dicarbonyl glycation may be viewed as damage to the proteome. The glyoxalase system, particularly glyoxalase 1, is the vanguard against dicarbonyl glycation in physiological systems. Functional regulation of glyoxalase I suggests a role for dicarbonyl glycation in cell signaling. Although extents of modification are usually low, the dicarbonyl proteome is a critical feature of the impact of glycation on physiological function-particularly in mitochondrial dysfunction, vascular disease, and potentially in disorders of lipoprotein metabolism.

Item Type: Conference Item (Paper)
Subjects: Q Science
Divisions: Faculty of Science > Computer Science
Faculty of Medicine > Warwick Medical School > Metabolic and Vascular Health
Faculty of Medicine > Warwick Medical School
Series Name: ANNALS OF THE NEW YORK ACADEMY OF SCIENCES
Journal or Publication Title: Annals of the New York Academy of Sciences
Publisher: Wiley-Blackwell Publishing, Inc.
ISBN: 978-1-57331-719-1
ISSN: 0077-8923
Editor: Schleicher, E and Somoza, V and Shieberle, P
Date: April 2008
Volume: Vol.1126
Number of Pages: 4
Page Range: pp. 124-127
Identification Number: 10.1196/annals.1433.043
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
Conference Paper Type: Paper
Title of Event: 9th International Symposium on the Maillard Reaction
Type of Event: Conference
Location of Event: Munich, Germany
Date(s) of Event: Sep, 2007
URI: http://wrap.warwick.ac.uk/id/eprint/30065

Data sourced from Thomson Reuters' Web of Knowledge

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