scholarly journals Integrin-mediated Tyrosine Phosphorylation of Shc in T Cells Is Regulated by Protein Kinase C-dependent Phosphorylations of Lck

2003 ◽  
Vol 14 (2) ◽  
pp. 349-360 ◽  
Author(s):  
Shi Niu ◽  
Haichun Xie ◽  
Eugene E. Marcantonio
Keyword(s):  
T Cells ◽  
Protein Kinase C ◽  
T Cell ◽  
Protein Kinase ◽  
Tyrosine Phosphorylation ◽  
T Cell Receptor ◽  
T Cell Activation ◽  
Cell Receptor ◽  
Serine Phosphorylation ◽  
Kinase C

Integrin receptor signals are costimulatory for mitogenesis with the T-cell receptor during T-cell activation. A subset of integrin receptors can link to the adapter protein Shc and provide a mitogenic stimulus. Using a combination of genetic and pharmacological approaches, we show herein that integrin signaling to Shc in T cells requires the receptor tyrosine phosphatase CD45, the Src family kinase member Lck, and protein kinase C. Our results suggest a model in which integrin-dependent serine phosphorylation of Lck is the critical step that determines the efficiency of Shc tyrosine phosphorylation in T cells. Serine phosphorylation of Lck is dependent on PKC and is also linked to CD45 dephosphorylation. Mutants of Lck that cannot be phosphorylated on the critical serine residues do not signal efficiently to Shc and have greatly reduced kinase activity. This signaling from integrins to Lck may be an important step in the costimulation with the T-cell receptor during lymphocyte activation.

scholarly journals Regulation of T Cell Receptor- and CD28-induced Tyrosine Phosphorylation of the Focal Adhesion Tyrosine Kinases Pyk2 and Fak by Protein Kinase C

2000 ◽  
Vol 275 (2) ◽  
pp. 1344-1350 ◽  
Author(s):  
Masahiro Tsuchida ◽  
Eric R. Manthei ◽  
Tausif Alam ◽  
Stuart J. Knechtle ◽  
Majed M. Hamawy
Keyword(s):  
Protein Kinase C ◽  
T Cell ◽  
Protein Kinase ◽  
Tyrosine Phosphorylation ◽  
T Cell Receptor ◽  
Focal Adhesion ◽  
Tyrosine Kinases ◽  
Cell Receptor ◽  
Kinase C

Protein kinase C is required for responses to T cell receptor ligands but not to interleukin-2 in T cells

Cell ◽  
1988 ◽  
Vol 55 (1) ◽  
pp. 101-112 ◽  
Author(s):  
Viia E. Valge ◽  
Justin G.P. Wong ◽  
Barry M. Datlof ◽  
Anthony J. Sinskey ◽  
Anjana Rao
Keyword(s):  
T Cells ◽  
Protein Kinase C ◽  
T Cell ◽  
Protein Kinase ◽  
T Cell Receptor ◽  
Interleukin 2 ◽  
Cell Receptor ◽  
Receptor Ligands ◽  
Kinase C

scholarly journals Cyclosporine A inhibits Ca2+-dependent stimulation of the Na+/H+ antiport in human T cells.

1986 ◽  
Vol 103 (2) ◽  
pp. 457-463 ◽  
Author(s):  
P M Rosoff ◽  
G Terres
Keyword(s):  
T Cells ◽  
Protein Kinase C ◽  
T Cell ◽  
Protein Kinase ◽  
T Cell Receptor ◽  
Rat Kidney ◽  
Cell Receptor ◽  
Kinase C ◽  
Normal Rat ◽  
Stimulation Of

The cyclic undecapeptide cyclosporine A (CsA) is a potent immunosuppressive agent that inhibits the initial activation of T lymphocytes. This agent appears to be most effective in blocking the action of mitogens such as concanavalin A and the calcium ionophore A23187, which cause an influx of Ca2+, but not those that may act by alternate mechanisms. These observations suggest that CsA may block a Ca2+-dependent step in T cell activation. We have shown that stimulation of the T3-T cell receptor complex-associated Ca2+ transporter activates the Na+/H+ antiport (Rosoff, P. M., and L. C. Cantley, 1985, J. Biol. Chem., 260: 14053-14059). The tumor-promoting phorbol esters, which are co-mitogenic for T cells, activate the exchanger by a separate pathway which is mediated by protein kinase C. Both the rise in intracellular Ca2+ and intracellular pH may be necessary for the successful triggering of cellular activation. In this report we show that CsA blocks the T3-T cell receptor-stimulated, Ca2+ influx-dependent activation of Na+/H+ exchange, but not the phorbol ester-mediated pathway in a transformed human T cell line. CsA inhibited mitogen-stimulation of interleukin-2 production in a separate cell line. CsA also inhibited vasopressin stimulation of the antiporter in normal rat kidney fibroblasts, but had no effect on serum or 12-O-tetradecanoyl phorbol 13-acetate stimulation. CsA did not affect serum or vasopressin or serum stimulation of normal rat kidney cell proliferation. CsA also had no effect on lipopolysaccharide or phorbol ester stimulation of Na+/H+ exchange activity or induction of differentiation in 70Z/3 pre-B lymphocytes in which these events are initiated by the protein kinase C pathway. These data suggest that mechanisms of activation of Na+/H+ exchange that involve an elevation in cytosolic Ca2+ are blocked by CsA but that C kinase-mediated regulation is unaffected. The importance of the Na+/H+ antiport in the regulation of growth and differentiation of T cells is discussed.

scholarly journals A Model System for Activation-Induced Alternative Splicing of CD45 Pre-mRNA in T Cells Implicates Protein Kinase C and Ras

2000 ◽  
Vol 20 (1) ◽  
pp. 70-80 ◽  
Author(s):  
Kristen W. Lynch ◽  
Arthur Weiss
Keyword(s):  
T Cells ◽  
Protein Kinase C ◽  
Alternative Splicing ◽  
T Cell ◽  
Protein Kinase ◽  
Cell Line ◽  
T Cell Activation ◽  
Cell Activation ◽  
Model System ◽  
Kinase C

ABSTRACT Multiple isoforms of the protein tyrosine phosphatase CD45 are expressed on the surface of human T cells. Interestingly, the expression of these isoforms has been shown to vary significantly upon T-cell activation. In this report, we describe a novel cell line-based model system in which we can mimic the activation-induced alternative splicing of CD45 observed in primary T cells. Of the many proximal signaling events induced by T-cell stimulation, we show that activation of protein kinase C and activation of Ras are important for the switch toward the exclusion of CD45 variable exons, whereas events related to Ca2+ flux are not. In addition, the ability of cycloheximide to block the activation-induced alternative splicing of CD45 suggests a requirement for de novo protein synthesis. We further demonstrate that sequences which have previously been implicated in the tissue-specific regulation of CD45 variable exons are likewise necessary and sufficient for activation-induced splicing. These results provide an initial understanding of the requirements for CD45 alternative splicing upon T-cell activation, and they confirm the importance of this novel cell line in facilitating a more detailed analysis of the activation-induced regulation of CD45 than has been previously possible.

Endo- and exocytic rate constants for spontaneous and protein kinase C-activated T cell receptor cycling

2002 ◽  
Vol 32 (3) ◽  
pp. 616 ◽  
Author(s):  
Charlotte Menné ◽  
Tine Møller Sørensen ◽  
Volkert Siersma ◽  
Marina von Essen ◽  
Niels Ødum ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
T Cell ◽  
Protein Kinase ◽  
T Cell Receptor ◽  
Rate Constants ◽  
Cell Receptor ◽  
Kinase C ◽  
Activated T Cell

scholarly journals T Cell Receptor-induced Phosphorylation of Sos Requires Activity of CD45, Lck, and Protein Kinase C, but Not ERK

1997 ◽  
Vol 272 (34) ◽  
pp. 21625-21634 ◽  
Author(s):  
Haoran Zhao ◽  
Yi-Yang Li ◽  
Raymond V. Fucini ◽  
Susan E. Ross ◽  
Jeffrey E. Pessin ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
T Cell ◽  
Protein Kinase ◽  
T Cell Receptor ◽  
Cell Receptor ◽  
Kinase C

Protein kinase C-activating phorbol esters augment expression of T cell receptor genes

1987 ◽  
Vol 17 (6) ◽  
pp. 803-807 ◽  
Author(s):  
Daniel J. Noonan ◽  
Noah Isakov ◽  
Argyrios N. Theofilopoulos ◽  
Frank J. Dixon ◽  
Amnon Altman
Keyword(s):  
Protein Kinase C ◽  
T Cell ◽  
Protein Kinase ◽  
T Cell Receptor ◽  
Phorbol Esters ◽  
Cell Receptor ◽  
Kinase C ◽  
T Cell Receptor Genes
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