Linked Life Data

15879154

Source:http://linkedlifedata.com/resource/pubmed/id/15879154

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2005-5-9
pubmed:abstractText
Epidemiological studies suggest the potential importance of an inflammatory component in atherosclerosis and support the hypothesis that immune responses to Ags of pathogens cross-react with homologous host proteins due to molecular mimicry. Protein candidates involved may be the stress-induced proteins known as heat shock proteins (HSP). In this study, we report that atherosclerotic plaques harbor in vivo-activated CD4(+) T cells that recognize the human 60-kDa HSP. Such in vivo-activated 60-kDa HSP-specific T cells are not detectable in the peripheral blood. In patients with positive serology and PCR for Chlamydia pneumoniae DNA, but not in patients negative for both, most of plaque-derived T cells specific for human 60-kDa HSP also recognized the C. pneumoniae 60-kDa HSP. We characterized the submolecular specificity of such 60-kDa HSP-specific plaque-derived T cells and identified both the self- and cross-reactive epitopes of that autoantigen. On challenge with human 60-kDa HSP, most of the plaque-derived T cells expressed Th type 1 functions, including cytotoxicity and help for monocyte tissue factor production. We suggest that arterial endothelial cells, undergoing classical atherosclerosis risk factors and conditioned by Th type 1 cytokines, express self 60-kDa HSP, which becomes target for both autoreactive T cells and cross-reactive T cells to microbial 60-kDa HSP via a mechanism of molecular mimicry. This hypothesis is in agreement with the notion that immunization with HSP exacerbates atherosclerosis, whereas immunosuppression and T cell depletion prevent the formation of arteriosclerotic lesions in experimental animals.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
174
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6509-17
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:15879154-Aged, pubmed-meshheading:15879154-Amino Acid Sequence, pubmed-meshheading:15879154-Antigen Presentation, pubmed-meshheading:15879154-Arteriosclerosis, pubmed-meshheading:15879154-Autoantigens, pubmed-meshheading:15879154-CD4-Positive T-Lymphocytes, pubmed-meshheading:15879154-Cell Movement, pubmed-meshheading:15879154-Chaperonin 60, pubmed-meshheading:15879154-Chlamydophila pneumoniae, pubmed-meshheading:15879154-Clone Cells, pubmed-meshheading:15879154-Cytokines, pubmed-meshheading:15879154-Epitopes, T-Lymphocyte, pubmed-meshheading:15879154-Female, pubmed-meshheading:15879154-Humans, pubmed-meshheading:15879154-Jurkat Cells, pubmed-meshheading:15879154-Lymphocyte Activation, pubmed-meshheading:15879154-Male, pubmed-meshheading:15879154-Middle Aged, pubmed-meshheading:15879154-Molecular Mimicry, pubmed-meshheading:15879154-Molecular Sequence Data, pubmed-meshheading:15879154-Monocytes, pubmed-meshheading:15879154-Thromboplastin
pubmed:year
2005
pubmed:articleTitle
Human 60-kDa heat shock protein is a target autoantigen of T cells derived from atherosclerotic plaques.
pubmed:affiliation
Department of Internal Medicine, University of Florence, Florence, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't