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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, Volume 1126 pp. 124-127. ISBN 978-1-57331-719-1. doi:10.1196/annals.1433.043 ISSN 0077-8923.
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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) | ||||
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| Subjects: | Q Science > QH Natural history > QH301 Biology Q Science > QP Physiology |
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| Divisions: | Faculty of Science, Engineering and Medicine > Science > Computer Science Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences > Translational & Experimental Medicine > Metabolic and Vascular Health (- until July 2016) Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School |
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| Library of Congress Subject Headings (LCSH): | Glycosylation, Glyoxalase -- Physiological effect, Proteomics, Glyoxal, Arginine, Bioinformatics | ||||
| 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 | ||||
| Official Date: | April 2008 | ||||
| Dates: |
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| Volume: | Volume 1126 | ||||
| Number of Pages: | 4 | ||||
| Page Range: | pp. 124-127 | ||||
| DOI: | 10.1196/annals.1433.043 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access | ||||
| Funder: | Wellcome Trust (London, England), British Heart Foundation, Cancer Research UK (CRUK), Diabetes UK | ||||
| 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 |
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