Linked Life Data

8864826

Source:http://linkedlifedata.com/resource/pubmed/id/8864826

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1996-12-17
pubmed:abstractText
Autoantibodies to the thyrotropin receptor (TSHR) have been shown to mediate the hyperthyroidism associated with Graves' disease (GD). A number of hypotheses have been proposed which link an infectious agent to the mechanism(s) involved in the induction of GD. Several studies have suggested that the development of GD may be linked to infection with the enteric pathogen Yersinia enterocolitica. We have recently identified two low molecular weight (5.5 and 8 kDa) envelope proteins of Y. enterocolitica that are cross-reactive with the extracellular domain of human TSHR (ETSHR). In this study, we have purified these ETSHR-crossreactive Yersinia proteins (TSHR-CRP) and have further characterized their immunoreactivity. Both the 5.5 and 8 kDa TSHR-CRPs were shown to be mitogenic for mouse spleen cells. This mitogenic activity was specific for B cells and was not due to lipopolysaccharide (LPS) contamination. TSHR-CRPs were mitogenic for LPS-non-responsive spleen cells obtained from C3H/Hej mice, and polymyxin B did not inhibit the mitogenic activity of the TSHR-CRPs. TSHR-CRPs also induced high levels of IL-6 production in B cells and induced production and secretion of significant levels of IgG and IgM. Finally, culture supernatants from TSHR-CRP-stimulated spleen cells were shown by Western blot analysis to contain antibodies that recognized the ETSHR These results identify for the first time two envelope proteins of Yersinia that have mitogenic activity and therefore could represent important proteins involved in the pathogenesis of Yersinia infections. Because these mitogenic proteins also contain epitopes crossreactive with the TSHR, they are potentially important for advancing our understanding of the role molecular mimicry plays in the induction of autoimmunity to the TSHR.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0896-8411
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
509-16
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed-meshheading:8864826-Animals, pubmed-meshheading:8864826-Antibodies, pubmed-meshheading:8864826-Antibodies, Bacterial, pubmed-meshheading:8864826-Antibody Formation, pubmed-meshheading:8864826-B-Lymphocytes, pubmed-meshheading:8864826-Bacterial Outer Membrane Proteins, pubmed-meshheading:8864826-Cross Reactions, pubmed-meshheading:8864826-Epitopes, pubmed-meshheading:8864826-Female, pubmed-meshheading:8864826-Glutamate Decarboxylase, pubmed-meshheading:8864826-Immunoglobulin G, pubmed-meshheading:8864826-Immunoglobulin M, pubmed-meshheading:8864826-Interleukin-6, pubmed-meshheading:8864826-Lymphocyte Activation, pubmed-meshheading:8864826-Mice, pubmed-meshheading:8864826-Mice, Inbred C3H, pubmed-meshheading:8864826-Mice, Inbred CBA, pubmed-meshheading:8864826-Mitogens, pubmed-meshheading:8864826-Receptors, Thyrotropin, pubmed-meshheading:8864826-Spleen, pubmed-meshheading:8864826-Yersinia enterocolitica
pubmed:year
1996
pubmed:articleTitle
Yersinia enterocolitica envelope proteins that are crossreactive with the thyrotropin receptor (TSHR) also have B-cell mitogenic activity.
pubmed:affiliation
Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston 77555-1019, USA.
pubmed:publicationType
Journal Article