Linked Life Data

1911547

Source:http://linkedlifedata.com/resource/pubmed/id/1911547

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1991-11-5
pubmed:abstractText
CD8 T cell differentiation antigens, expressed on class I-restricted T cells, have a key role in the control of recognition and response of these cells to antigen. It has been suggested that these molecules function as co-receptors together with antigen-specific T cell receptors to regulate T cell responses. We have addressed the question of whether cytoplasmic serine phosphorylation, which occurs on CD8 molecules after activation by antigen or phorbol esters, is relevant to its co-receptor function. By mutagenesis, we show that phorbol ester-induced phosphorylation occurs exclusively on CD8 alpha serine residue 216. However, inhibition of CD8 polypeptide phosphorylation does not appear to have a detrimental effect on several responses of CD8-dependent transfectants to antigen. This is in contrast to results reported with CD4 (N.Glaichenhaus, N.Shastri, D.R. Littmann and J.M.Turner. 1991. Cell, 64:511), suggesting that CD4 and CD8 molecules may play somewhat different roles in the control of T cell activation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0953-8178
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
785-92
pubmed:dateRevised
2009-11-3
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Phosphorylation of murine CD8 alpha is not essential for responses of T cell hybridomas to antigen.
pubmed:affiliation
Imperial Cancer Research Fund Tumour Immunology Unit, Biology Department, University College London, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't