scholarly journals CD45 Negatively Regulates Monocytic Cell Differentiation by Inhibiting Phorbol 12-Myristate 13-Acetate-dependent Activation and Tyrosine Phosphorylation of Protein Kinase Cδ

2000 ◽  
Vol 276 (13) ◽  
pp. 10212-10217 ◽  
Author(s):  
Eric L. Deszo ◽  
Danett K. Brake ◽  
Keith A. Cengel ◽  
Keith W. Kelley ◽  
Gregory G. Freund
Keyword(s):  
Cell Differentiation ◽  
Protein Kinase ◽  
Tyrosine Phosphorylation ◽  
Monocytic Cell ◽  
Protein Kinase Cδ

scholarly journals Tyrosine phosphorylation and stimulation of protein kinase Cδ from porcine spleen by src in vitro

FEBS Letters ◽  
1994 ◽  
Vol 347 (1) ◽  
pp. 85-89 ◽  
Author(s):  
Michael Gschwendt ◽  
Kirsten Kielbassa ◽  
Walter Kittstein ◽  
Friedrich Marks
Keyword(s):  
Protein Kinase ◽  
Tyrosine Phosphorylation ◽  
Stimulation Of ◽  
Protein Kinase Cδ

scholarly journals Peroxisome Proliferator-activated Receptor γ Ligands Inhibit Mitogenic Induction of p21Cip1by Modulating the Protein Kinase Cδ Pathway in Vascular Smooth Muscle Cells

2001 ◽  
Vol 276 (50) ◽  
pp. 47650-47657 ◽  
Author(s):  
Shu Wakino ◽  
Ulrich Kintscher ◽  
Zhaowei Liu ◽  
Sarah Kim ◽  
Fen Yin ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Enzymatic Activity ◽  
Tyrosine Phosphorylation ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Induced Expression ◽  
Ligand Effects ◽  
Protein Kinase Cδ

The cyclin-dependent kinase inhibitor p21Cip1is up-regulated in response to mitogenic stimulation in various cells. PPARγ ligands troglitazone (TRO, 10 μm) and rosiglitazone (RSG, 10 μm) attenuated the induction of p21Cip1protein by platelet-derived growth factor (PDGF) and insulin without affecting cognate mRNA levels in rat aortic smooth muscle cells (RASMC). The protein kinase Cδ (PKCδ) inhibitor rottlerin also blocked the induction of p21Cip1protein, whereas the conventional PKC isotype inhibitor Gö 6976 had no effect. Kinetic studies using the protein synthesis inhibitor cycloheximide showed that TRO, RSG, and rottlerin shortened the half-life of p21Cip1protein. TRO, RSG, and rottlerin inhibited PDGF-induced expression of p21Cip1, but they did not affect insulin-induced expression of p21Cip1. Both ligands inhibited PKCδ enzymatic activity in PDGF-stimulated RASMC but not in insulin-stimulated cells. Adenovirus-mediated overexpression of PKCδ rescued the down-regulation of p21Cip1expression both by TRO and RSG in PDGF-treated RASMC. These data suggested that the PKCδ pathway plays a critical role in PDGF-induced expression of p21Cip1in RASMC and may be the potential target for PPARγ ligand effects. Src kinase-dependent tyrosine phosphorylation of PKCδ was decreased substantially by TRO and RSG. Tyrosine phosphorylation and activation of c-Src in response to PDGF were unaffected by either PPARγ ligand. Protein-tyrosine-phosphatase inhibitors sodium orthovanadate and dephostatin prevented PPARγ ligand effects on PKCδ tyrosine phosphorylation and enzymatic activity. Both inhibitors also reversed PPARγ ligand effects on p21Cip1expression in PDGF-treated RASMC. PPARγ ligands enhanced protein-tyrosine-phosphatase activity in RASMC, which may be the mechanism for decreased PKCδ tyrosine phosphorylation and activity. PPARγ ligands regulate p21Cip1at a post-translational level by blocking PKCδ signaling and accelerating p21Cip1turnover.

scholarly journals Tyrosine Phosphorylation Regulates the Proteolytic Activation of Protein Kinase Cδ in Dopaminergic Neuronal Cells

2005 ◽  
Vol 280 (31) ◽  
pp. 28721-28730 ◽  
Author(s):  
Siddharth Kaul ◽  
Vellareddy Anantharam ◽  
Yongjie Yang ◽  
Christopher J. Choi ◽  
Arthi Kanthasamy ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Tyrosine Phosphorylation ◽  
Neuronal Cells ◽  
Proteolytic Activation ◽  
Protein Kinase Cδ

scholarly journals Tyrosine Phosphorylation of Protein Kinase Cδ Is Essential for Its Apoptotic Effect in Response to Etoposide

2002 ◽  
Vol 22 (1) ◽  
pp. 182-195 ◽  
Author(s):  
Michal Blass ◽  
Ilana Kronfeld ◽  
Gila Kazimirsky ◽  
Peter M. Blumberg ◽  
Chaya Brodie
Keyword(s):  
Protein Kinase ◽  
Tyrosine Phosphorylation ◽  
Dominant Negative ◽  
C6 Glioma Cells ◽  
Dominant Negative Mutant ◽  
Tyrosine Residues ◽  
Apoptotic Effect ◽  
Induced Apoptosis ◽  
Protein Kinase Cδ

ABSTRACT Protein kinase Cδ (PKCδ) is involved in the apoptosis of various cells in response to diverse stimuli. In this study, we characterized the role of PKCδ in the apoptosis of C6 glioma cells in response to etoposide. We found that etoposide induced apoptosis in the C6 cells within 24 to 48 h and arrested the cells in the G1/S phase of the cell cycle. Overexpression of PKCδ increased the apoptotic effect induced by etoposide, whereas the PKCδ selective inhibitor rottlerin and the PKCδ dominant-negative mutant K376R reduced this effect compared to control cells. Etoposide-induced tyrosine phosphorylation of PKCδ and its translocation to the nucleus within 3 h was followed by caspase-dependent cleavage of the enzyme. Using PKC chimeras, we found that both the regulatory and catalytic domains of PKCδ were necessary for its apoptotic effect. The role of tyrosine phosphorylation of PKCδ in the effects of etoposide was examined using cells overexpressing a PKCδ mutant in which five tyrosine residues were mutated to phenylalanine (PKCδ5). These cells exhibited decreased apoptosis in response to etoposide compared to cells overexpressing PKCδ. Likewise, activation of caspase 3 and the cleavage of the PKCδ5 mutant were significantly lower in cells overexpressing PKCδ5. Using mutants of PKCδ altered at individual tyrosine residues, we identified tyrosine 64 and tyrosine 187 as important phosphorylation sites in the apoptotic effect induced by etoposide. Our results suggest a role of PKCδ in the apoptosis induced by etoposide and implicate tyrosine phosphorylation of PKCδ as an important regulator of this effect.

scholarly journals Inhibiting Tyrosine Phosphorylation of Protein Kinase Cδ (PKCδ) Protects the Salivary Gland from Radiation Damage

2014 ◽  
Vol 289 (15) ◽  
pp. 10900-10908 ◽  
Author(s):  
Sten M. Wie ◽  
Tariq S. Adwan ◽  
James DeGregori ◽  
Steven M. Anderson ◽  
Mary E. Reyland
Keyword(s):  
Salivary Gland ◽  
Protein Kinase ◽  
Radiation Damage ◽  
Tyrosine Phosphorylation ◽  
Protein Kinase Cδ

Protein kinase Cδ mediates retinoic acid and phorbol myristate acetate–induced phospholipid scramblase 1 gene expression: its role in leukemic cell differentiation

Blood ◽  
2004 ◽  
Vol 104 (12) ◽  
pp. 3731-3738 ◽  
Author(s):  
Ke-Wen Zhao ◽  
Xi Li ◽  
Qian Zhao ◽  
Ying Huang ◽  
Dong Li ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Cell Differentiation ◽  
Protein Kinase ◽  
Vitamin D3 ◽  
Active Form ◽  
Specific Inhibitor ◽  
Leukemic Cell ◽  
Phospholipid Scramblase ◽  
Phospholipid Scramblase 1 ◽  
Protein Kinase Cδ

Although phospholipid scramblase 1 (PLSCR1) was originally identified based on its capacity to promote transbilayer movement of membrane phospholipids, subsequent studies also provided evidence for its role in cell proliferation, maturation, and apoptosis. In this report, we investigate the potential role of PLSCR1 in leukemic cell differentiation. We show that all-trans retinoic acid (ATRA), an effective differentiation-inducing agent of acute promyelocytic leukemic (APL) cells, can elevate PLSCR1 expression in ATRA-sensitive APL cells NB4 and HL60, but not in maturation-resistant NB4-LR1 cells. ATRA- and phorbol 12-myristate 13-acetate (PMA)–induced monocytic differentiation is accompanied by increased PLSCR1 expression, whereas only a slight or no elevation of PLSCR1 expression is observed in U937 cells differentiated with dimethyl sulfoxide (DMSO), sodium butyrate, or vitamin D3. Cell differentiation with ATRA and PMA, but not with vitamin D3 or DMSO, results in phosphorylation of protein kinase Cδ (PKCδ), and the PKCδ-specific inhibitor rottlerin nearly eliminates the ATRA- and PMA-induced expression of PLSCR1, while ectopic expression of a constitutively active form of PKCδ directly increases PLSCR1 expression. Finally, decreasing PLSCR1 expression with small interfering RNA inhibits ATRA/PMA-induced differentiation. Taken together, these results suggest that as a protein induced upon PKCδ activation, PLSCR1 is required for ATRA- and PMA-triggered leukemic cell differentiation.

Sign in / Sign up

Export Citation Format

Share Document