Negative Regulation of the SHPTP1 Protein Tyrosine Phosphatase by Protein Kinase C δ in Response to DNA Damage

2001 ◽  
Vol 60 (6) ◽  
pp. 1431-1438 ◽  
Author(s):  
Kiyotsugu Yoshida ◽  
Donald Kufe
Keyword(s):  
Dna Damage ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Negative Regulation ◽  
Protein Tyrosine ◽  
Kinase C

Effect of activation of protein kinase C on CD45 isoform expression and CD45 protein tyrosine phosphatase activity in T cells

1990 ◽  
Vol 20 (8) ◽  
pp. 1655-1660 ◽  
Author(s):  
Akira Yamada ◽  
Michel Streuli ◽  
Haruo Saito ◽  
David M. Rothstein ◽  
Stuart F. Schlossman ◽  
...  
Keyword(s):  
T Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Phosphatase Activity ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine ◽  
Kinase C ◽  
Isoform Expression

The Protein-Tyrosine-Phosphatase SHP2 Is Phosphorylated on Serine Residues 576 and 591 by Protein Kinase C Isoforms α, β1, β2, and η

Biochemistry ◽  
2002 ◽  
Vol 41 (2) ◽  
pp. 603-608 ◽  
Author(s):  
Volker Strack ◽  
Jan Krützfeldt ◽  
Monika Kellerer ◽  
Axel Ullrich ◽  
Reiner Lammers ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine ◽  
Kinase C ◽  
Protein Kinase C Isoforms

scholarly journals Lipid Raft Targeting of Hematopoietic Protein Tyrosine Phosphatase by Protein Kinase C θ-Mediated Phosphorylation

2006 ◽  
Vol 26 (5) ◽  
pp. 1806-1816 ◽  
Author(s):  
Konstantina Nika ◽  
Céline Charvet ◽  
Scott Williams ◽  
Lutz Tautz ◽  
Shane Bruckner ◽  
...  
Keyword(s):  
T Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Lipid Raft ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Tcr Signaling ◽  
Immune Synapse ◽  
Protein Tyrosine ◽  
Kinase C

ABSTRACT Protein kinase C θ (PKC θ) is unique among PKC isozymes in its translocation to the center of the immune synapse in T cells and its unique downstream signaling. Here we show that the hematopoietic protein tyrosine phosphatase (HePTP) also accumulates in the immune synapse in a PKC θ-dependent manner upon antigen recognition by T cells and is phosphorylated by PKC θ at Ser-225, which is required for lipid raft translocation. Immune synapse translocation was completely absent in antigen-specific T cells from PKC θ−/− mice. In intact T cells, HePTP-S225A enhanced T-cell receptor (TCR)-induced NFAT/AP-1 transactivation, while the acidic substitution mutant was as efficient as wild-type HePTP. We conclude that HePTP is phosphorylated in the immune synapse by PKC θ and thereby targeted to lipid rafts to temper TCR signaling. This represents a novel mechanism for the active immune synapse recruitment and activation of a phosphatase in TCR signaling.

Effects of Protein Tyrosine Kinase, Protein Tyrosine Phosphatase and Protein Kinase C on the Apoptotic Process of Leukemia Cells and Human Cortex Neurons Managed by Arsenic Trioxide.

Blood ◽  
2004 ◽  
Vol 104 (11) ◽  
pp. 4451-4451
Author(s):  
Jin Zhou ◽  
Ran Meng ◽  
Baofeng Yang ◽  
Baoxin Li
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Phosphatase ◽  
Protein Tyrosine Kinase ◽  
Tyrosine Phosphatase ◽  
Leukemia Cells ◽  
Protein Tyrosine ◽  
Nb4 Cells ◽  
Kinase C

Abstract Objective Study on the effects of protein tyrosine kinase, protein tyrosine phosphatase and protein kinase C (PKC)on apoptotic process, observe the changes of cytosolic calcium ([Ca2+]i) of human leukemia cells and cortex neurons after clinical relevant dosage of arsenic trioxide (As2O3) exposure in vitro. Methods Marked [Ca2+]I of human leukemia cells and cortex neurons with Fluo-3/AM, assayed the changes of [Ca2+]I with laser confocal microscopy in real-time after managed with As2O3 in different concentrations respectively, detected the effects of protein tyrosine kinase, the protein tyrosine phosphatase and the activation of protein kinase C on these changes with confocal microscopy and Phosphorus radioisotope assay. Assayed the DNA ladders of leukemia cells and cortex neurons after exposed in As2O3. Results As2O3 1μmol/L can increase the [Ca2+]I of NB4 cells remarkably but show no effects on neurons. Vanadate, a kind of protein tyrosine phosphatase inhibitor, can dose-dependently promote the increasing of [Ca2+]I caused by 2, 5, 10μmol/L As2O3.The mean value of total increased rate in 280 seconds after exposed in As2O3 in different concentrations were: 6.5±2.3%, 21.7±2.1 %,49.2±2.5% in NB4 cells, and 6.7±2.1%, 19.4±2.5 %, 52.3±2.7% in cortex neurons respectively. Genistein, a kind of protein tyrosine kinase inhibitor, can dose-dependently decrease the raising of [Ca2+]I caused by 2, 5, 10μmol/L As2O3.The mean value of total inhibited rate in 280 seconds after As2O3 management in different concentrations were 6.7±2.9%, 25.6±2.5 %, 52.2±3.5% in NB4 cells, and 7.8±3.1%, 18.1±2.8%, 51.3±3.3% in cortex neurons respectively. The activation of PKC began when exposed in As2O31μmol/L for 3 h, and keep raising continuously in NB4 cells., DNA ladders appeared after exposed in As2O31μmol/L for 24h. However, no appearances above were found in human cortex neurons. In 2μmol/L As2O3 exposedness, The activation of PKC and DNA ladders appeared in neurons. Conclusions The phosphorylation and dephosphorylation of protein tyrosine kinase and protein tyrosine phosphatase participated in nonspecific apoptosis signal transduction pathway of As2O3, and accompanied with PKC activation. The [Ca2+] elevation was closely related to PKC increasing activation. The tolerances between leukemia cell and cortex neuron to As2O3 were differ in dosage.

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