scholarly journals Critical Role of the Isoform-Specific Region in α1-Na,K-ATPase Trafficking and Protein Kinase C-Dependent Regulation

Biochemistry ◽  
2010 ◽  
Vol 49 (17) ◽  
pp. 3602-3610 ◽  
Author(s):  
Yoann Sottejeau ◽  
Aude Belliard ◽  
Marie-Josée Duran ◽  
Thomas A. Pressley ◽  
Sandrine V. Pierre
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Critical Role ◽  
Specific Region ◽  
Kinase C

scholarly journals Critical role of the Isoform‐Specific Region in Na,K‐ATPase trafficking and Protein Kinase C‐dependent regulation

2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Sandrine V Pierre ◽  
Yoann Sottejeau ◽  
Aude Belliard ◽  
Marie‐Josee Duran ◽  
Thomas A Pressley
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Critical Role ◽  
Specific Region ◽  
Kinase C

Protein kinase C and chemical-induced abnormal palate development

2005 ◽  
Vol 24 (4) ◽  
pp. 203-214 ◽  
Author(s):  
Chada S Reddy
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Single Gene ◽  
Critical Role ◽  
Early Death ◽  
Palate Development ◽  
Kinase C ◽  
A Cell ◽  
Context Specific

The protein kinase C (PKC) family of proteins mediates the action of growth factors and other ligands by activating a network of transcription factors that bind to TRE sequences in the promoters of many genes that regulate cell proliferation, differentiation, extracellular matrix synthesis, apoptosis and others in a cell type-, isozymeand context-specific manner. The critical role of PKC in embryonic development is indicated by early death of embryos in which one or more of these isozymes are inactivated. Our studies together with others show that palatal PKC signalling is functional and may be essential for normal palate development. Although single gene knockouts have failed to exhibit the cleft palate (CP) phenotype, owing to compensation by other kinases, many chemicals including the mycotoxin, secalonic acid D, disrupt palatal PKC signalling leading to altered palatal mesenchymal gene expression. The potential relevance of such effects to chemical-induced CP is discussed.

Influence of Protein Kinase C and Calcium in the Course of Thrombin Receptors Activation.

Blood ◽  
2007 ◽  
Vol 110 (11) ◽  
pp. 3194-3194
Author(s):  
Ying Xie ◽  
Yue Han ◽  
De Pei Wu ◽  
Aining Sun ◽  
Wei Zhang
Keyword(s):  
Protein Kinase C ◽  
Platelet Aggregation ◽  
Protein Kinase ◽  
Membrane Surface ◽  
Signal Transmission ◽  
Critical Role ◽  
Signal Pathways ◽  
Kinase C ◽  
Thrombin Receptors

Abstract Object In order to compare the functions of protein kinase C (PKC) and calcium (Ca2+) in platelet aggregation and platelet membrane surface glycoproteins GPIb expression after thrombin receptors activation, then to investigate the role of Gq signal transmission pathway in the course of thrombin receptors activation. Methods Peptide SFLLRN (PAR1-AP) and AYPGKF (PAR4-AP) were used for stimulating platelet at different time point (0, 1, 2, 5, 10, 30min), then the alterations of platelet aggregation and GPIb were analyzed in the involvement of Ro-31-2220 (inhibitor of PKC) and BAPTA/AM (calcium chelator). Results Either PAR1 or PAR4 peptide can induce absolute platelet aggregation, together with a reversible internalization of GPIb. Platelet aggregation was inhibited by Ro-31-2220 or BAPTA/AM while the shape change curve still occurred upon PARs activation. In addition, Ro-31-2220 decreases GPIb centralisation upon PAR1 stimulation (P <0.05 at 1, 2 min), though it blocks the pool of GPIb inside platelet in PAR4 activation (P <0.05 at 10, 30 min). Meanwhile, GPIb internalization was blocked by BAPTA for both peptides (P <0.05 at 1∼10 min). Conclusion All the results confirm a critical role of Gq pathway in thrombin signal transmission through the involvement of protein kinase C and calcium. Calcium is closely correlated with the thrombin receptors activation, seemed to be similar for two PARs signal pathways. Protein kinase C urges GPIb centralisation in PAR1 pathway and accelerates GPIbα return in PAR4 pathway.

scholarly journals Critical role of protein kinase C ε for lipopolysaccharide-induced IL-12 synthesis in monocyte-derived dendritic cells

2002 ◽  
Vol 32 (11) ◽  
pp. 3040-3049 ◽  
Author(s):  
Ezra Aksoy ◽  
Zoulikha Amraoui ◽  
Stanislas Goriely ◽  
Michel Goldman ◽  
Fabienne Willems
Keyword(s):  
Dendritic Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Critical Role ◽  
Kinase C

scholarly journals Evidence for a role of protein kinase C zeta subspecies in maturation of Xenopus laevis oocytes.

1992 ◽  
Vol 12 (9) ◽  
pp. 3776-3783 ◽  
Author(s):  
I Dominguez ◽  
M T Diaz-Meco ◽  
M M Municio ◽  
E Berra ◽  
A García de Herreros ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Growth Factors ◽  
Protein Kinase ◽  
Xenopus Laevis ◽  
Critical Role ◽  
Study Data ◽  
Xenopus Laevis Oocytes ◽  
Kinase C ◽  
Protein Kinase C Zeta

A number of studies have demonstrated the activation of phospholipase C-mediated hydrolysis of phosphatidylcholine (PC-PLC) both by growth factors and by the product of the ras oncogene, p21ras. Evidence has been presented indicating that the stimulation of this phospholipid degradative pathway is sufficient to activate mitogenesis in fibroblasts as well as that it is sufficient and necessary for induction of maturation in Xenopus laevis oocytes. However, the mechanism whereby PC-PLC transduces mitogenic signals triggered by growth factors or oncogenes remains to be elucidated. In this study, data are presented that show the involvement of protein kinase C zeta subspecies in the channelling of the mitogenic signal activated by insulin-p21ras-PC-PLC in Xenopus oocytes as well as the lack of a critical role of protein kinase C isotypes alpha, beta, gamma, delta, and epsilon in these pathways.

scholarly journals The critical role of atypical protein kinase C in activating hepatic SREBP-1c and NFκB in obesity

2009 ◽  
Vol 50 (6) ◽  
pp. 1133-1145 ◽  
Author(s):  
Mini P. Sajan ◽  
Mary L. Standaert ◽  
Sonali Nimal ◽  
Usha Varanasi ◽  
Tina Pastoor ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Critical Role ◽  
Atypical Protein Kinase C ◽  
Atypical Protein Kinase ◽  
Kinase C

scholarly journals The Drosophila Atypical Protein Kinase C-Ref(2)P Complex Constitutes a Conserved Module for Signaling in the Toll Pathway

2002 ◽  
Vol 22 (24) ◽  
pp. 8787-8795 ◽  
Author(s):  
Antonia Avila ◽  
Neal Silverman ◽  
María T. Diaz-Meco ◽  
Jorge Moscat
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Nuclear Translocation ◽  
Critical Role ◽  
Atypical Protein Kinase C ◽  
Atypical Protein Kinase ◽  
Kinase C ◽  
P Protein ◽  
Toll Signaling

ABSTRACT Recent results showed the critical role of the mammalian p62-atypical protein kinase C (aPKC) complex in the activation of NF-κB in response to different stimuli. Here we demonstrate using the RNA interference technique on Schneider cells that the Drosophila aPKC (DaPKC) is required for the stimulation of the Toll-signaling pathway, which activates the NF-κB homologues Dif and Dorsal. However, DaPKC does not appear to be important for the other Drosophila NF-κB signaling cascade, which activates the NF-κB homologue Relish in response to lipopolysaccharides. Interestingly, DaPKC functions downstream of the nuclear translocation of Dorsal or Dif, controlling the transcriptional activity of the Drosomycin promoter. We also show that the Drosophila Ref(2)P protein is the homologue of mammalian p62 as it binds to DaPKC, its overexpression is sufficient to activate the Drosomycin but not the Attacin promoter, and its depletion severely impairs Toll signaling. Collectively, these results demonstrate the conservation of the p62-aPKC complex for the control of innate immunity signal transduction in Drosophila melanogaster.

scholarly journals Critical role of protein kinase C α and calcium in growth factor induced activation of the Na+ /H+ exchanger NHE1

FEBS Letters ◽  
2002 ◽  
Vol 521 (1-3) ◽  
pp. 205-210 ◽  
Author(s):  
Karl Maly ◽  
Kukka Strese ◽  
Sonja Kampfer ◽  
Florian Ueberall ◽  
Gottfried Baier ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Critical Role ◽  
Kinase C

Evidence for a role of protein kinase C zeta subspecies in maturation of Xenopus laevis oocytes

1992 ◽  
Vol 12 (9) ◽  
pp. 3776-3783
Author(s):  
I Dominguez ◽  
M T Diaz-Meco ◽  
M M Municio ◽  
E Berra ◽  
A García de Herreros ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Growth Factors ◽  
Protein Kinase ◽  
Xenopus Laevis ◽  
Critical Role ◽  
Study Data ◽  
Xenopus Laevis Oocytes ◽  
Kinase C ◽  
Protein Kinase C Zeta

A number of studies have demonstrated the activation of phospholipase C-mediated hydrolysis of phosphatidylcholine (PC-PLC) both by growth factors and by the product of the ras oncogene, p21ras. Evidence has been presented indicating that the stimulation of this phospholipid degradative pathway is sufficient to activate mitogenesis in fibroblasts as well as that it is sufficient and necessary for induction of maturation in Xenopus laevis oocytes. However, the mechanism whereby PC-PLC transduces mitogenic signals triggered by growth factors or oncogenes remains to be elucidated. In this study, data are presented that show the involvement of protein kinase C zeta subspecies in the channelling of the mitogenic signal activated by insulin-p21ras-PC-PLC in Xenopus oocytes as well as the lack of a critical role of protein kinase C isotypes alpha, beta, gamma, delta, and epsilon in these pathways.

A critical role of conventional protein kinase C in morphological changes of rodent mast cells

2010 ◽  
Vol 89 (1) ◽  
pp. 149-159 ◽  
Author(s):  
Yuhki Yanase ◽  
Izumi Hide ◽  
Shoji Mihara ◽  
Yasuhito Shirai ◽  
Naoaki Saito ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Mast Cells ◽  
Protein Kinase ◽  
Morphological Changes ◽  
Critical Role ◽  
Kinase C
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