Deleterious effects of reactive aldehydes and glycated proteins on macrophage proteosomal function: Possible links between diabetes and atherosclerosis

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dc.contributor.author Moheimani, Fatemeh en_US
dc.contributor.author Morgan, Philip en_US
dc.contributor.author Van Reyk, David en_US
dc.contributor.author Davies, Michael en_US
dc.contributor.editor en_US
dc.date.accessioned 2011-02-07T06:20:47Z
dc.date.available 2011-02-07T06:20:47Z
dc.date.issued 2010 en_US
dc.identifier 2009004783 en_US
dc.identifier.citation Moheimani Fatemeh et al. 2010, 'Deleterious effects of reactive aldehydes and glycated proteins on macrophage proteosomal function: Possible links between diabetes and atherosclerosis', Elsevier, vol. 1802, no. 6, pp. 561-571. en_US
dc.identifier.issn 0925-4439 en_US
dc.identifier.other C1 en_US
dc.identifier.uri http://hdl.handle.net/10453/13331
dc.description.abstract People with diabetes experience chronic hyperglycemia and are at a high risk of developing atherosclerosis and microvascular disease. Reactions of glucose, or aldehydes derived from glucose (e.g. methylglyoxal, glyoxal, or glycolaldehyde), with proteins result in glycation that ultimately yield advanced glycation end products (AGE). AGE are present at elevated levels in plasma and atherosclerotic lesions from people with diabetes, and previous in vitro studies have postulated that the presence of these materials is deleterious to cell function. This accumulation of AGE and glycated proteins within cells may arise from either increased formation and/or ineffective removal by cellular proteolytic systems, such as the proteasomes, the major multi-enzyme complex that removes proteins within cells. In this study it is shown that whilst high glucose concentrations fail to modify proteasome enzyme activities in J774A.1 macrophage-like cell extracts, reactive aldehydes enhanced proteasomal enzyme activities. In contrast BSA, pre-treated with high glucose for 8 weeks, inhibited both the chymotrypsin-like and caspase-like activities. BSA glycated using methylglyoxal or glycolaldehyde, also inhibited proteasomal activity though to differing extents. This suppression of proteasome activity by glycated proteins may result in further intracellular accumulation of glycated proteins with subsequent deleterious effects on cellular function. en_US
dc.language en_US
dc.publisher Elsevier en_US
dc.relation.hasversion Accepted manuscript version en_US
dc.rights NOTICE: this is the author’s version of a work that was accepted for publication in Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, [Volume 1802, Issue 6, June 2010, Pages 561–571] DOI# http://dx.doi.org/10.1016/j.bbadis.2010.02.007 en_US
dc.title Deleterious effects of reactive aldehydes and glycated proteins on macrophage proteosomal function: Possible links between diabetes and atherosclerosis en_US
dc.parent Biochimica et Biophysica acta en_US
dc.journal.volume 1802 en_US
dc.journal.number 6 en_US
dc.publocation Netherlands en_US
dc.identifier.startpage 561 en_US
dc.identifier.endpage 571 en_US
dc.cauo.name SCI.Medical and Molecular Biosciences en_US
dc.conference Verified OK en_US
dc.for 110100 en_US
dc.personcode 999181 en_US
dc.personcode 0000061715 en_US
dc.personcode 000788 en_US
dc.personcode 0000045917 en_US
dc.percentage 100 en_US
dc.classification.name Medical Biochemistry and Metabolomics en_US
dc.classification.type FOR-08 en_US
dc.edition May 2 en_US
dc.custom en_US
dc.date.activity en_US
dc.location.activity en_US
dc.description.keywords diabetes-associated atherosclerosis proteosome glycated proteins advanced glycation end products reactive aldehydes protein turnover en_US
dc.staffid en_US


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