Linked Life Data

3259228

Source:http://linkedlifedata.com/resource/pubmed/id/3259228

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1988-6-20
pubmed:abstractText
The ability of the T lymphocyte growth factor interleukin 2 (IL-2) to activate a tyrosine protein kinase in vivo was assessed by using antibodies to phosphotyrosine in conjunction with immunoblots. Treatment of the murine IL-2-dependent cytotoxic T cell line CTLL-2 with IL-2 resulted in an increase in tyrosine phosphorylation of several proteins of molecular weights ranging from 38,000 to 120,000. The tyrosine phosphorylation in the various proteins increased in a concomitant fashion and reached a maximum level within 15 min. The concentration of IL-2 required for inducing this phosphorylation was similar to that required for stimulating [3H]thymidine uptake, indicating that the increase in tyrosine phosphorylation correlated with the ability of IL-2 to stimulate the proliferation of the CTLL-2 cells. IL-2 was also found to induce the phosphorylation of proteins on tyrosine residues in short term cultures of human T lymphocytes. These results suggest that IL-2, like other polypeptide growth factors, acts by stimulating the activity of a tyrosine protein kinase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6956-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Activation of a tyrosine protein kinase is an early event in the stimulation of T lymphocytes by interleukin-2.
pubmed:affiliation
Department of Pharmacology and Cancer Center, University of Rochester Medical Center, New York 14642.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't