scholarly journals The Role of Tyrosine Phosphorylation of Protein Kinase C Delta in Infection and Inflammation

2019 ◽  
Vol 20 (6) ◽  
pp. 1498 ◽  
Author(s):  
Qingliang Yang ◽  
Jordan Langston ◽  
Yuan Tang ◽  
Mohammad Kiani ◽  
Laurie Kilpatrick
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Inflammatory Response ◽  
Tyrosine Phosphorylation ◽  
Critical Role ◽  
In Vivo Models ◽  
Kinase C ◽  
Microfluidic Assays

Protein Kinase C (PKC) is a family composed of phospholipid-dependent serine/threonine kinases that are master regulators of inflammatory signaling. The activity of different PKCs is context-sensitive and these kinases can be positive or negative regulators of signaling pathways. The delta isoform (PKCδ) is a critical regulator of the inflammatory response in cancer, diabetes, ischemic heart disease, and neurodegenerative diseases. Recent studies implicate PKCδ as an important regulator of the inflammatory response in sepsis. PKCδ, unlike other members of the PKC family, is unique in its regulation by tyrosine phosphorylation, activation mechanisms, and multiple subcellular targets. Inhibition of PKCδ may offer a unique therapeutic approach in sepsis by targeting neutrophil-endothelial cell interactions. In this review, we will describe the overall structure and function of PKCs, with a focus on the specific phosphorylation sites of PKCδ that determine its critical role in cell signaling in inflammatory diseases such as sepsis. Current genetic and pharmacological tools, as well as in vivo models, that are used to examine the role of PKCδ in inflammation and sepsis are presented and the current state of emerging tools such as microfluidic assays in these studies is described.

scholarly journals Role of protein kinase C in constrictor responses of the rat basilar artery in vivo.

1992 ◽  
Vol 445 (1) ◽  
pp. 169-179 ◽  
Author(s):  
M A Murray ◽  
F M Faraci ◽  
D D Heistad
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Basilar Artery ◽  
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.

scholarly journals In vivo evidence for a role of protein kinase C in peripheral nociceptive processing

2002 ◽  
Vol 135 (1) ◽  
pp. 239-247 ◽  
Author(s):  
Adriano L S Souza ◽  
Fabrício A Moreira ◽  
Karine R Almeida ◽  
Caryne M Bertollo ◽  
Karina A Costa ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase C ◽  
Nociceptive Processing

scholarly journals Regulation of Impaired Protein Kinase C Signaling by Chemokines in Murine Macrophages during Visceral Leishmaniasis

2005 ◽  
Vol 73 (12) ◽  
pp. 8334-8344 ◽  
Author(s):  
Ranadhir Dey ◽  
Arup Sarkar ◽  
Nivedita Majumder ◽  
Suchandra Bhattacharyya (Majumdar) ◽  
Kaushik Roychoudhury ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Leishmania Donovani ◽  
Disease Process ◽  
Kinase C ◽  
Parasitic Burden ◽  
Infected Cells

ABSTRACT The protein kinase C (PKC) family regulates macrophage function involved in host defense against infection. In the case of Leishmania donovani infection, the impairment of PKC-mediated signaling is one of the crucial events for the establishment of parasite into the macrophages. Earlier reports established that C-C chemokines mediated protection against leishmaniasis via the generation of nitric oxide after 48 h. In this study, we investigated the role of MIP-1α and MCP-1 in the regulation of impaired PKC activity in the early hours (6 h) of infection. These chemokines restored Ca2+-dependent PKC activity and inhibited Ca2+-independent atypical PKC activity in L. donovani-infected macrophages under both in vivo and in vitro conditions. Pretreatment of macrophages with chemokines induced superoxide anion generation by activating NADPH oxidase components in infected cells. Chemokine administration in vitro induced the migration of infected macrophages and triggered the production of reactive oxygen species. In vivo treatment with chemokines significantly restricted the parasitic burden in livers as well as in spleens. Collectively, these results indicate a novel regulatory role of C-C chemokines in controlling the intracellular growth and multiplication of L. donovani, thereby demonstrating the antileishmanial properties of C-C chemokines in the disease process.

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 Phosphorylation of human pleckstrin on Ser-113 and Ser-117 by protein kinase C

1996 ◽  
Vol 314 (3) ◽  
pp. 937-942 ◽  
Author(s):  
Karen L. CRAIG ◽  
Calvin B. HARLEY
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phosphorylation Sites ◽  
Wild Type ◽  
Cos Cells ◽  
Phospholipid Hydrolysis ◽  
Kinase C

During platelet activation, receptor-coupled phospholipid hydrolysis stimulates protein kinase C (PKC) and results in the phosphorylation of several proteins, the most prominent being pleckstrin. Pleckstrin is composed of two repeated domains, now called pleckstrin homology (PH) domains, separated by a spacer region that contains several consensus PKC phosphorylation sites. To determine the role of PKC-dependent phosphorylation in pleckstrin function, we mapped the phosphorylation sites in vivo of wild-type and site-directed mutants of pleckstrin expressed in COS cells. Phosphorylation was found to occur almost exclusively on Ser-113 and Ser-117 within the sequence 108-KFARKS*TRRS*IRL-120. Phosphorylation of these sites was confirmed by phosphorylation of the corresponding wild-type and mutant synthetic peptides in vitro.

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 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
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