Linked Life Data

10464157

Source:http://linkedlifedata.com/resource/pubmed/id/10464157

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1999-12-7
pubmed:abstractText
Although complement activation appears to have an important role both in the early and late phases of atherosclerosis, the exact mechanism of the initiation of this activation is still unknown. Since injuries of the endothelial cells are known to result in increased stress-protein expression we tested the complement-activating ability of recombinant human 60 kDa heat-shock protein (hsp60). Human hsp60 was found to activate the complement system in normal human serum in a dose-dependent manner. Activation took place through the classical pathway. The lack of complement activation in agammaglobulinemic serum indicates that the classical pathway is triggered by anti-hsp60 antibodies. Hsp60 activated complement in the sera of 74 patients with coronary heart disease as well, and a strong positive correlation (r = 0.459, P < 0.0001) was found between the extent of complement activation and the level of anti-hsp60 IgG antibodies but there was no correlation to the level of anti-hsp65 IgG antibodies. Further distinction between anti-hsp60 and anti-hsp65 antibodies was obtained from competitive ELISA experiments: binding of anti-hsp60 antibodies to hsp60-coated plates was inhibited only by recombinant hsp60 and vice versa. Our present findings indicate that anti-hsp60 and anti-hsp65 antibodies are distinct, showing only partial cross-reactivity. Since complement activation plays an important role in the development of atherosclerosis and the levels of complement-activating anti-hsp60 antibodies are elevated in atherosclerosis-related diseases, our present findings may have important pathological implications.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0953-8178
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1363-70
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10464157-Adult, pubmed-meshheading:10464157-Agammaglobulinemia, pubmed-meshheading:10464157-Aged, pubmed-meshheading:10464157-Antibodies, Bacterial, pubmed-meshheading:10464157-Antigens, Bacterial, pubmed-meshheading:10464157-Bacterial Proteins, pubmed-meshheading:10464157-Chaperonin 60, pubmed-meshheading:10464157-Chaperonins, pubmed-meshheading:10464157-Child, Preschool, pubmed-meshheading:10464157-Complement Pathway, Classical, pubmed-meshheading:10464157-Coronary Disease, pubmed-meshheading:10464157-Cross Reactions, pubmed-meshheading:10464157-Dose-Response Relationship, Immunologic, pubmed-meshheading:10464157-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:10464157-Female, pubmed-meshheading:10464157-Humans, pubmed-meshheading:10464157-Immunoglobulin G, pubmed-meshheading:10464157-Male, pubmed-meshheading:10464157-Middle Aged, pubmed-meshheading:10464157-Recombinant Proteins
pubmed:year
1999
pubmed:articleTitle
Antibodies against human heat-shock protein (hsp) 60 and mycobacterial hsp65 differ in their antigen specificity and complement-activating ability.
pubmed:affiliation
Third Department of Medicine, Semmelweis University of Medicine, Budapest, Hungary.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't