Linked Life Data

7938054

Source:http://linkedlifedata.com/resource/pubmed/id/7938054

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-11-23
pubmed:abstractText
Intracellular signal transduction has been reported to be triggered by phosphorylation of interleukin-2 (IL-2) receptor by IL-2. In order to clarify the effect of tyrosine phosphorylation of IL-2 receptors on cell-mediated cytotoxicity by natural killer (NK) cells, we studied the effect of a tyrosine kinase inhibitor, genistein, on the lethal effects of NK-rich cells for K562 cells. Exposure of NK-rich cells to IL-2 (100 U/ml) for 3 days increased their cytotoxicities against K562 cells. The effect was reduced in the presence of 10 micrograms/ml of genistein. Samples immunoprecipitated by anti-IL-2R beta antibodies were prepared from NK-rich fractions with or without exposure to IL-2 and/or genistein. Coprecipitated proteins with 75, 65, and 56 kDa were detected with an antiphosphotyrosine antibody. The amount of phosphorylated tyrosine residues of 56-kDa protein, which was predominantly detected in NK-rich cells, was remarkably increased by IL-2 treatment. The enhanced phosphorylation of 56-kDa protein was reduced by the presence of genistein. These results suggested that IL-2 increased tyrosine phosphorylation and the affinity to IL-2R beta of the 56-kDa proteins in NK-rich cells. Immunoprecipitated samples by anti-IL-2R beta were reblotted with anti-p56lck antibody and revealed that the 56-kDa protein was identified to be p56lck. The increase of coprecipitated p56lck with anti-IL-2R beta antibody by the treatment with IL-2 suggested that the affinity of p56lck to IL-2R beta was increased by IL-2 in NK-rich cells. The amount of coprecipitated p56lck with IL-2R beta was reduced in the sample exposed to genistein. The affinity of p56lck to IL-2R beta was considered to be regulated by IL-2-induced tyrosine phosphorylation. Our results demonstrated a potential role for tyrosine kinase, p56lck, in the signaling events that regulate the cytotoxicity by NK-rich cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0037-9727
pubmed:author
pubmed:issnType
Print
pubmed:volume
207
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
227-33
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Genistein, a tyrosine kinase inhibitor, decreased the affinity of p56lck to beta-chain of interleukin-2 receptor in human natural killer (NK)-rich cells and decreased NK-mediated cytotoxicity.
pubmed:affiliation
Pharmacology Division, National Cancer Center Research Institute, Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't