Linked Life Data

11599917

Source:http://linkedlifedata.com/resource/pubmed/id/11599917

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-10-15
pubmed:abstractText
Prominent in T cells and natural killer cells, CD2 binding protein 1 (CD2BP1) plays an important role in CD2-mediated adhesion and signal transduction. In the current study, we investigated CD2 and PSTPIP (proline, serine, threonine phosphatase interacting protein, murine homologue of CD2BP1) interactions in purified mouse splenic T cells. PSTPIP associated with CD2 in both resting and activated T cells. Following various stimuli, such as concanavalin A, anti-TCRbeta, anti-CD3epsilon, anti-CD3epsilon/phorbol myristate acetate (PMA), IL-2, or PMA/ionomycin, PSTPIP and CD2 expression, as well as their association, increased in a time-dependent fashion. While PSTPIP expression and CD2 expression were comparable across most groups, the PSTPIP-CD2 association stimulated by anti-CD3epsilon alone was significantly greater than with other stimuli. Stimulation by anti-CD3epsilon plus anti-CD28 induced even greater PSTPIP-CD2 association than anti-CD3epsilon treatment alone, indicating that CD28 initiated signals are involved in regulating this interaction. There was no direct association between CD3epsilon or CD28 and PSTPIP. Tyrosine phosphorylated PSTPIP bound poorly to CD2 compared to dephosphorylated PSTPIP, and protein tyrosine phosphatase was shown to affect both phosphorylation of PSTPIP and the CD2-PSTPIP association. In addition to CD2, PSTPIP associated with CD4, CD8, CD54, and CD62L. CD2 and CD4 ligation reciprocally regulated their association with PSTPIP. These findings indicate that T cell activation, particularly through the CD3 and CD28 signal transduction pathways, regulates PSTPIP-CD2 interactions. PSTPIP likely has additional broader effects through interactions with CD4, CD8, CD54, and CD62L, and this may influence T cell responses to antigen.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-4800
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Academic Press.
pubmed:issnType
Print
pubmed:volume
71
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
115-24
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:11599917-Adaptor Proteins, Signal Transducing, pubmed-meshheading:11599917-Animals, pubmed-meshheading:11599917-Antibodies, Monoclonal, pubmed-meshheading:11599917-Antigens, CD2, pubmed-meshheading:11599917-Antigens, CD28, pubmed-meshheading:11599917-Antigens, CD3, pubmed-meshheading:11599917-Blotting, Western, pubmed-meshheading:11599917-Carrier Proteins, pubmed-meshheading:11599917-Cytoskeletal Proteins, pubmed-meshheading:11599917-Female, pubmed-meshheading:11599917-Lymphocyte Activation, pubmed-meshheading:11599917-Mice, pubmed-meshheading:11599917-Mice, Inbred CBA, pubmed-meshheading:11599917-Mice, Knockout, pubmed-meshheading:11599917-Phosphorylation, pubmed-meshheading:11599917-Precipitin Tests, pubmed-meshheading:11599917-Protein Tyrosine Phosphatases, pubmed-meshheading:11599917-Receptors, Antigen, T-Cell, pubmed-meshheading:11599917-T-Lymphocytes
pubmed:year
2001
pubmed:articleTitle
Regulation of the association between PSTPIP and CD2 in murine T cells.
pubmed:affiliation
Institute for Gene Therapy and Molecular Medicine, Mount Sinai School of Medicine, New York, New York 10029-6574, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.