| Literature DB >> 18533367 |
Abstract
Glycation of proteins, nucleotides and basic phospholipids by glyoxal and methylglyoxal--physiological substrates of glyoxalase 1--is potentially damaging to the proteome, genome and lipidome. Glyoxalase 1 suppresses glycation by these alpha-oxoaldehyde metabolites and thereby represents part of the enzymatic defence against glycation. Albert Szent-Györgyi pioneered and struggled to understand the physiological function of methylglyoxal and the glyoxalase system. We now appreciate that glyoxalase 1 protects against dicarbonyl modifications of the proteome, genome and lipome. Latest research suggests there are functional modifications of this process--implying a role in cell signalling, ageing and disease.Entities:
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Year: 2008 PMID: 18533367 PMCID: PMC2649415 DOI: 10.1515/dmdi.2008.23.1-2.125
Source DB: PubMed Journal: Drug Metabol Drug Interact ISSN: 0792-5077