scholarly journals Activation of protein kinase C family members by the novel polyphosphoinositides PtdIns-3,4-P2 and PtdIns-3,4,5-P3.

1994 ◽  
Vol 269 (51) ◽  
pp. 32358-32367
Author(s):  
A Toker ◽  
M Meyer ◽  
K K Reddy ◽  
J R Falck ◽  
R Aneja ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Family Members ◽  
The Novel ◽  
Kinase C

scholarly journals Physiological Role for Phosphatidic Acid in the Translocation of the Novel Protein Kinase C Apl II in Aplysia Neurons

2008 ◽  
Vol 28 (15) ◽  
pp. 4719-4733 ◽  
Author(s):  
Carole A. Farah ◽  
Ikue Nagakura ◽  
Daniel Weatherill ◽  
Xiaotang Fan ◽  
Wayne S. Sossin
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phosphatidic Acid ◽  
Physiological Role ◽  
C2 Domain ◽  
The Novel ◽  
Physiological Conditions ◽  
Kinase C ◽  
Neuronal Membranes ◽  
Novel Protein

ABSTRACT In Aplysia californica, the serotonin-mediated translocation of protein kinase C (PKC) Apl II to neuronal membranes is important for synaptic plasticity. The orthologue of PKC Apl II, PKCε, has been reported to require phosphatidic acid (PA) in conjunction with diacylglycerol (DAG) for translocation. We find that PKC Apl II can be synergistically translocated to membranes by the combination of DAG and PA. We identify a mutation in the C1b domain (arginine 273 to histidine; PKC Apl II-R273H) that removes the effects of exogenous PA. In Aplysia neurons, the inhibition of endogenous PA production by 1-butanol inhibited the physiological translocation of PKC Apl II by serotonin in the cell body and at the synapse but not the translocation of PKC Apl II-R273H. The translocation of PKC Apl II-R273H in the absence of PA was explained by two additional effects of this mutation: (i) the mutation removed C2 domain-mediated inhibition, and (ii) the mutation decreased the concentration of DAG required for PKC Apl II translocation. We present a model in which, under physiological conditions, PA is important to activate the novel PKC Apl II both by synergizing with DAG and removing C2 domain-mediated inhibition.

Differential Regulation of Myosin Regulatory Light Chain Phosphorylation by Protein Kinase C Isozymes in Human Uterine Myocytes

2018 ◽  
Vol 26 (7) ◽  
pp. 988-996
Author(s):  
Bryan F. Mitchell ◽  
Mei Chi ◽  
Elle Surgent ◽  
Bailey M. Sorochan ◽  
Curtis N. Tracey ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Ex Vivo ◽  
Neonatal Morbidity ◽  
The Novel ◽  
Uterine Contractility ◽  
Uterine Activity ◽  
Kinase C

Background: Preterm birth is the most common cause of neonatal morbidity and mortality and a common precedent to lifelong disability. Current treatment has minimal efficacy. Objective: We assessed the role of isozymes of the protein kinase C (PKC) family in regulating the phosphorylation of myosin regulatory light chains (RLCs), which regulate uterine contractility. We also explored the mechanisms through which these isozymes function. Study Design: We used a previously characterized and validated quantitative in-cell Western (ICW) assay to measure site-specific phosphorylations on myosin RLC and CPI-17. Cultures of human uterine myocytes (hUM) were treated with the potent contractile stimulant oxytocin to induce uterine contractility or a pharmacological mimic of diacyl-glycerol to stimulate the conventional and novel isozymes of the PKC family. Combinations of isozyme-selective inhibitors were used to determine the effects of the conventional and novel classes of isozymes. Results: Stimulation of PKC using phospho-dibutyrate caused immediate, concentration-dependent inhibition of uterine activity ex vivo. Using the ICW assay with hUM, the oxytocin-stimulated increase in the pro-contractile phosphorylations of myosin RLCs at serine19 and threonine18 was completely inhibited by prior treatment with phorbol-12-myristate-13-acetate, which stimulates both convention and novel classes of isozymes. Our results suggest that the conventional class of isozymes cause a reduction in phosphorylations at serine19 and threonine18 by reducing activity of myosin light chain kinase. The novel class of isozymes has 2 mechanisms of action: the first is activation of CPI-17 through phosphorylation at threonine38, which results in reduced activity of myosin light chain phosphatase and increased levels of activated myosin RLC; the second is increased phosphorylation of the N-terminal region of myosin RLC. Conclusions: Specific agonists for the conventional isozymes or inhibitors of the novel isozymes of the PKC family could be useful pharmacological agents for regulation of uterine activity.

scholarly journals Overexpression of Protein Kinase C Isoform  but not δ in Human Interleukin-3–Dependent Cells Suppresses Apoptosis and Induces bcl-2 Expression

Blood ◽  
1998 ◽  
Vol 91 (3) ◽  
pp. 823-829 ◽  
Author(s):  
E. Gubina ◽  
M.S. Rinaudo ◽  
Z. Szallasi ◽  
P.M. Blumberg ◽  
R.A. Mufson
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
The Novel ◽  
Facs Analysis ◽  
Interleukin 3 ◽  
Gm Csf ◽  
Kinase C ◽  
Intracellular Ca ◽  
Cellular Dna ◽  
Stimulating Factor

Hematopoietic progenitor cells die by apoptosis after removal of the appropriate colony-stimulating factor (CSF). Recent pharmacologic data have implicated protein kinase C (PKC) in the suppression of apoptosis in interleukin-3 (IL-3) and granulocyte-macrophage (GM)-CSF–dependent human myeloid cells. Because IL-3 and GM-CSF induce increases in diacylglycerol without mobilizing intracellular Ca++, it seemed that one of the novel Ca++ independent isoforms of PKC was involved. We report here that overexpression of PKC in factor-dependent human TF-1 cells extends cell survival in the absence of cytokine. Overexpression of PKCδ does not have this effect. By 72 to 96 hours after cytokine withdrawal, the PKC transfectants remain distributed in all phases of the cell cycle, as shown by fluorescence-activated cell sorting (FACS) analysis, while little intact cellular DNA is detectable in vector or PKCδ transfectants. PKC induces bcl-2 protein expression fivefold to sixfold over the levels in empty vector transfectants, whereas the levels in PKCδ transfectants are similar to those in vector controls.

Platelet P-selectin expression: requirement for protein kinase C, but not protein tyrosine kinase or phosphoinositide 3-kinase

2003 ◽  
Vol 89 (06) ◽  
pp. 1016-1023 ◽  
Author(s):  
Danielle Libersan ◽  
Yahye Merhi
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Human Platelet ◽  
The Novel ◽  
Protein Tyrosine ◽  
Kinase C ◽  
Activated Platelets ◽  
Phosphoinositide 3 Kinase

SummaryP-selectin is translocated from the α-granules to the surface of activated platelets where it participates in thrombosis and inflammation. We investigated the signaling pathways involved in thrombin-induced human platelet P-selectin expression. Assessed by flow cytometry, inhibition of protein kinase C (PKC) with chelerythrine reduced P-selectin expression by 66%, platelet/neutrophil binding, GPIIb/IIIa activation and aggregation (p<0.05). Gö 6976, an inhibitor of the conventional PKCs (α and β), did not alter P-selectin expression. However, rottlerin inhibited by 50% its expression (p<0.05), but only at doses that interfere with the novel (є, η) and atypical (ζ) PKCs. Inhibition of protein tyrosine kinase (PTK) and phosphoinositide 3-kinase (PI3-K) did not significantly affect P-selectin expression. In conclusion, thrombin-induced P-selectin expression is PKC-sensitive, but PTK and PI3-K-insensitive. The novel є and η and atypical ζ, but not the conventional α and β and the novel θ PKCs, may be involved in this process.

scholarly journals The Novel Immunosuppressive Protein Kinase C Inhibitor Sotrastaurin Has No Pro-Viral Effects on the Replication Cycle of Hepatitis B or C Virus

PLoS ONE ◽  
2011 ◽  
Vol 6 (9) ◽  
pp. e24142 ◽  
Author(s):  
Thomas von Hahn ◽  
Andreas Schulze ◽  
Ivan Chicano Wust ◽  
Benjamin Heidrich ◽  
Thomas Becker ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Hepatitis B ◽  
Replication Cycle ◽  
The Novel ◽  
Kinase C ◽  
Protein Kinase C Inhibitor
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