Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-2-7
pubmed:abstractText
Oxidised LDL has been implicated in the pathogenesis of atherosclerosis. Macrophages can oxidatively modify low-density lipoprotein (LDL) in vitro. The mechanisms of this oxidation process are presently unclear. In this study, we have investigated the effects of compounds and enzymes widely used to quench or scavenge active oxygen species to try to identify the oxidative species involved in this process. The data obtained suggest that hydrogen peroxide may possibly play a role in LDL oxidation by macrophages, whereas singlet oxygen and hydroxyl radicals may not. The role of superoxide anions was uncertain because copper-zinc superoxide dismutase (Cu/Zn-SOD) and manganese SOD (Mn-SOD), widely used to determine superoxide-dependency in other systems may be unsuitable in this particular system. Cu/Zn-SOD at high concentrations displayed a variability in its effects, sometimes augmenting LDL oxidation and sometimes inhibiting it. In the experiments in which Cu/Zn-SOD augmented LDL oxidation, heat inactivation of the enzyme decreased the augmentation; in the experiments in which Cu/Zn-SOD inhibited LDL oxidation, it retained its inhibitory effect after heat inactivation. Mn-SOD always inhibited modification even after heat inactivation. We have therefore concluded that superoxide involvement in LDL oxidation by macrophages is still uncertain and the uncertainty will remain until a suitable probe is found.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
1215
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
250-8
pubmed:dateRevised
2010-8-25
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
The effects of free radical scavengers on the oxidation of low-density lipoproteins by macrophages.
pubmed:affiliation
Department of Biochemistry and Physiology, School of Animal and Microbial Sciences, University of Reading, Berkshire, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't