Linked Life Data

12614460

Source:http://linkedlifedata.com/resource/pubmed/id/12614460

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-3-4
pubmed:abstractText
Campylobacter jejuni is a leading cause of acute bacterial gastroenteritis in humans. The mechanism by which C. jejuni interacts with host cells, however, is still poorly understood. Our previous study has shown that the C. jejuni surface lipoprotein JlpA mediates adherence of the bacterium to epithelial cells. In this report, we demonstrated that JlpA interacts with HEp-2 cell surface heat shock protein (Hsp) 90alpha and initiates signalling pathways leading to activation of NF-kappaB and p38 MAP kinase. Gel overlay and GST pull down assays showed that JlpA interacts with Hsp90alpha. Geldanamycin, a specific inhibitor of Hsp90, and anti-human Hsp90alpha antibody significantly blocked the interaction between JlpA and Hsp90alpha, suggesting a direct interaction between JlpA and HEp-2 cell surface-exposed Hsp90alpha. The treatment of HEp-2 cells with GST-JlpA initiated two signalling pathways: one leading to the phosphorylation and degradation of IkappaB and nuclear translocation of NF-kappaB; and another one to the phosphorylation of p38 MAP kinase. The activation of NF-kappaB and p38 MAP kinase in HEp-2 cells suggest that JlpA triggers inflammatory/immune responses in host cells following C. jejuni infection.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1462-5814
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
165-74
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12614460-Adhesins, Bacterial, pubmed-meshheading:12614460-Antigens, Surface, pubmed-meshheading:12614460-Benzoquinones, pubmed-meshheading:12614460-Binding Sites, pubmed-meshheading:12614460-Campylobacter Infections, pubmed-meshheading:12614460-Campylobacter jejuni, pubmed-meshheading:12614460-Cell Line, pubmed-meshheading:12614460-Enzyme Activation, pubmed-meshheading:12614460-Epithelial Cells, pubmed-meshheading:12614460-HSP90 Heat-Shock Proteins, pubmed-meshheading:12614460-Humans, pubmed-meshheading:12614460-Lactams, Macrocyclic, pubmed-meshheading:12614460-Mitogen-Activated Protein Kinases, pubmed-meshheading:12614460-NF-kappa B, pubmed-meshheading:12614460-Quinones, pubmed-meshheading:12614460-Signal Transduction, pubmed-meshheading:12614460-p38 Mitogen-Activated Protein Kinases
pubmed:year
2003
pubmed:articleTitle
JlpA of Campylobacter jejuni interacts with surface-exposed heat shock protein 90alpha and triggers signalling pathways leading to the activation of NF-kappaB and p38 MAP kinase in epithelial cells.
pubmed:affiliation
Department of Medical Genetics and Microbiology, Medical Science Building, 1 King's College Circle, University of Toronto, Toronto, ON, M5S 1A8, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't