Linked Life Data

19018093

Source:http://linkedlifedata.com/resource/pubmed/id/19018093

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
2009-3-27
pubmed:abstractText
Heat shock protein 70 (HSP70) has gained plenty of attention because of its adjuvant capability to induce CD8(+) cytotoxic T lymphocyte and CD4(+) T-helper cell responses. We investigated the behavior of T-cell subsets stimulated with endotoxin-free HSP70 with respect to proliferation, cytokine expression, cytotoxicity against allogeneic B-lymphoblastoid cell line and K562 cells, as well as target-independent cytotoxicity. CD4(+) cells exhibited a strong increase in proliferation after stimulation with HSP70 (29%). In the presence of targets, a 35-fold up-regulation of granzyme B was observed after stimulation of CD4(+) T cells with HSP70 in combination with interleukin-7 (IL-7)/IL-12/IL-15. The target cell-independent secretion of granzyme B by CD4(+) cells was greatly augmented after stimulation with HSP70 plus IL-2 or IL-7/IL-12/IL-15. In this study, we showed that HSP70 is capable of inducing a cytotoxic response of T-helper cells in the absence of lipopolysaccharide. The granzyme B secretion and cytolytic activity of T-helper cells are induced in a target-independent way, whereas the cytotoxic activity of CD3(+) and CD8(+) T cells can be further enhanced in the presence of target cells. Our data provide novel insights into the role of extracellular HSP70 on T-cell immune response concerning the induction of target-independent T-helper cell cytotoxicity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1528-0020
pubmed:author
pubmed:issnType
Electronic
pubmed:day
26
pubmed:volume
113
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3008-16
pubmed:meshHeading
pubmed-meshheading:19018093-Antigens, CD3, pubmed-meshheading:19018093-CD4-Positive T-Lymphocytes, pubmed-meshheading:19018093-CD8-Positive T-Lymphocytes, pubmed-meshheading:19018093-Cell Proliferation, pubmed-meshheading:19018093-Cells, Cultured, pubmed-meshheading:19018093-Cytotoxicity, Immunologic, pubmed-meshheading:19018093-Enterotoxins, pubmed-meshheading:19018093-Fluorescent Dyes, pubmed-meshheading:19018093-Gene Expression Regulation, pubmed-meshheading:19018093-Granzymes, pubmed-meshheading:19018093-HSP70 Heat-Shock Proteins, pubmed-meshheading:19018093-Humans, pubmed-meshheading:19018093-Interleukin-15, pubmed-meshheading:19018093-Interleukin-2, pubmed-meshheading:19018093-K562 Cells, pubmed-meshheading:19018093-Recombinant Proteins, pubmed-meshheading:19018093-T-Lymphocytes, Helper-Inducer
pubmed:year
2009
pubmed:articleTitle
Heat shock protein 70 (HSP70) induces cytotoxicity of T-helper cells.
pubmed:affiliation
Institute for Transfusion Medicine, Hannover Medical School, Hannover, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't