Definition of early Ca2+ signals induced by anti-CD3 antibody in a human Jurkat T-cell line using a selective protein kinase C inhibitor, Ro 31-8425

1993 ◽  
Vol 21 (4) ◽  
pp. 384S-384S
Author(s):  
LOUISE A. CONROY ◽  
JANET E. MERRITT ◽  
CHRYSANTHI F. GIAFI ◽  
ALAN G. LAMONT ◽  
TREVOR J. HALLAM
Keyword(s):  
Protein Kinase C ◽  
T Cell ◽  
Protein Kinase ◽  
Cell Line ◽  
Kinase C ◽  
Jurkat T Cell ◽  
Protein Kinase C Inhibitor ◽  
Definition Of

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.

The ζ Isoform of Protein Kinase C Controls Interleukin-2-Mediated Proliferation in a Murine T Cell Line: Evidence for an Additional Role of Protein Kinase C ϵ and β

1995 ◽  
Vol 218 (1) ◽  
pp. 105-113 ◽  
Author(s):  
Javier Gómez ◽  
Christina Pitton ◽  
Alphonse Garcı́a ◽  
Ana Martinez De Aragón ◽  
Augusto Silva ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
T Cell ◽  
Protein Kinase ◽  
Cell Line ◽  
Interleukin 2 ◽  
Kinase C ◽  
Additional Role

scholarly journals Evidence that interleukin-1 and phorbol esters activate NF-kappa B by different pathways: role of protein kinase C.

1991 ◽  
Vol 2 (4) ◽  
pp. 329-335 ◽  
Author(s):  
K Bomsztyk ◽  
J W Rooney ◽  
T Iwasaki ◽  
N A Rachie ◽  
S K Dower ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Line ◽  
Phorbol Esters ◽  
Interleukin 1 ◽  
Interleukin 2 ◽  
Nf Kappa B ◽  
Kinase C ◽  
Protein Kinase C Inhibitor

Nuclear factor kappa B (NF-kappa B) is a ubiquitous transcription factor that affects expression of many genes, including immunoglobulin kappa (kappa), the interleukin-2 receptor alpha chain, and two genes in HIV-1. NF-kappa B can be activated by a number of stimuli, including pharmacological stimulation of protein kinase C by phorbol 12-myristate 13-acetate (PMA) and treatment in vitro with either protein kinase C or protein kinase A. This has lead to the proposal that these kinases are key enzymes in the physiological activation of NF-kappa B as well. We have used a murine B cell line, 70Z/3, and T cell line, EL-4 6.1 C10, to study the activation of NF-kappa B by two physiological activators, interleukin-1 alpha (IL-1) and lipopolysaccharide (LPS). There are four reasons to propose that these agents activate pathways that do not include protein kinase C as a major component in these cell lines. First, the protein kinase C inhibitor 1-(5-isoquinolinesulfonyl)-2-methylpiperazine (H-7) strongly inhibited PMA-induced activation of NF-kappa B in 70Z/3 cells but had no effect on NF-kappa B activated by IL-1 or LPS. Second, depletion of protein kinase C by prolonged growth of 70Z/3 in PMA abrogated the capacity of the cells to activate NF-kappa B in response to further PMA treatment. However, these same cells activated NF-kappa B normally after either IL-1 or LPS treatment. Third, IL-1 effectively activated NF-kappa B in EL-4 6.1 C10 cells, but PMA did not. Fourth, interferon-gamma is a potent activator of protein kinase C in 70Z/3 cells, but is completely inactive in the mobilization of NF-kappa B. These results suggest that the physiological inducers IL-1 and LPS activate NF-kappa B by pathways independent of protein kinase C in both 70Z/3 and EL-4 6.1 C10 cells.

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