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Phospholipase C-gamma 1 association with CD3 structure in T cells.
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CD45 modulates T cell receptor/CD3-induced activation of human thymocytes via regulation of tyrosine phosphorylation.
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CD2/LFA-3 ligation induces phospholipase-C gamma 1 tyrosine phosphorylation and regulates CD3 signaling.
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Regulation of CD3-induced phospholipase C-gamma 1 (PLC gamma 1) tyrosine phosphorylation by CD4 and CD45 receptors.
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Sulfhydryl oxidation down-regulates T-cell signaling and inhibits tyrosine phosphorylation of phospholipase C gamma 1.
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Interaction of CD4:lck with the T cell receptor/CD3 complex induces early signaling events in the absence of CD45 tyrosine phosphatase.
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8
Functional activation of the T-cell antigen receptor induces tyrosine phosphorylation of phospholipase C-gamma 1.
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CD3 stimulation causes phosphorylation of phospholipase C-gamma 1 on serine and tyrosine residues in a human T-cell line.
Proc Natl Acad Sci U S A. 1991 Jun 15;88(12):5453-6. doi: 10.1073/pnas.88.12.5453.
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PLC gamma 1, a possible mediator of T cell receptor function.
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引用本文的文献
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The dietary sweetener sucralose is a negative modulator of T cell-mediated responses.
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Functional independence and interdependence of the Src homology domains of phospholipase C-gamma1 in B-cell receptor signal transduction.
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Cellular signalling mechanisms in B lymphocytes.
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4
G-proteins are not directly involved in the CD3-antigen-mediated production of inositol phosphates in HPB-ALL T-leukaemia cells expressing phospholipase C isoforms gamma 1 and beta 3.
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Cyclosporin A inhibits CD40 ligand expression in T lymphocytes.
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CD4-independent signal transduction through the T-cell receptor (TCR/CD3).
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Activation of phospholipase C-gamma 1 through transfected platelet-derived growth factor receptor enhances interleukin 2 production upon antigen stimulation in a T-cell line.
Mol Cell Biol. 1994 Feb;14(2):1213-9. doi: 10.1128/mcb.14.2.1213-1219.1994.
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Association of the tyrosine kinase LCK with phospholipase C-gamma 1 after stimulation of the T cell antigen receptor.
J Exp Med. 1992 Aug 1;176(2):373-9. doi: 10.1084/jem.176.2.373.
9
CD45 tyrosine phosphatase-activated p59fyn couples the T cell antigen receptor to pathways of diacylglycerol production, protein kinase C activation and calcium influx.
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Multiple kinases and signal transduction. Phosphorylation of the T cell antigen receptor complex.
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Inhibition of T-cell antigen receptor-mediated transmembrane signaling by protein kinase C activation.
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T cell CD3-zeta eta heterodimer expression and coupling to phosphoinositide hydrolysis.
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Increased intracellular cyclic adenosine monophosphate inhibits T lymphocyte-mediated cytolysis by two distinct mechanisms.
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Bivalent binding of an anti-CD3 antibody to Jurkat cells induces association of the T cell receptor complex with the cytoskeleton.
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Platelet-derived growth factor (PDGF) binding promotes physical association of PDGF receptor with phospholipase C.
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EGF induces tyrosine phosphorylation of phospholipase C-II: a potential mechanism for EGF receptor signaling.
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Inhibition of tyrosine phosphorylation prevents T-cell receptor-mediated signal transduction.
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Association of the fyn protein-tyrosine kinase with the T-cell antigen receptor.
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