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

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dc.contributor.author Moheimani, F
dc.contributor.author Morgan, PE
dc.contributor.author van Reyk, DM
dc.contributor.author Davies, MJ
dc.date.accessioned 2011-02-07T06:20:47Z
dc.date.issued 2010-06
dc.identifier.citation Biochimica et Biophysica Acta - Molecular Basis of Disease, 2010, 1802 (6), pp. 561 - 571
dc.identifier.issn 0925-4439
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. © 2010 Elsevier B.V.
dc.language eng
dc.relation.hasversion Accepted manuscript version en_US
dc.relation.isbasedon 10.1016/j.bbadis.2010.02.007
dc.title Deleterious effects of reactive aldehydes and glycated proteins on macrophage proteasomal function: Possible links between diabetes and atherosclerosis
dc.type Journal Article
dc.parent Biochimica et Biophysica Acta - Molecular Basis of Disease
dc.journal.volume 6
dc.journal.volume 1802
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 1101 Medical Biochemistry and Metabolomics
dc.personcode 000788
dc.personcode 999181
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 Advanced glycation end products
dc.description.keywords Diabetes-associated atherosclerosis
dc.description.keywords Glycated proteins
dc.description.keywords Proteasome
dc.description.keywords Protein turnover
dc.description.keywords Reactive aldehydes
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
utslib.copyright.status Open Access
utslib.copyright.date 2015-04-15 12:23:47.074767+10
pubs.consider-herdc true
utslib.collection.history School of Medical and Molecular Sciences (ID: 341)
utslib.collection.history General (ID: 2)


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