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The results indicate that PKC (show FYN Proteins) could be the final target and an integrator molecule of different signaling pathways triggered by angiotensin II (Ang II), which could explain the sustained activation of Na(+)-ATPase by Ang II (show AGT Proteins).
Phorbol 12-myristate 13-acetate activation of ERK (show MAPK1 Proteins) and JNK (show MAPK8 Proteins) signaling is relevant in the regulation of gene expression during follicular development, ovulation, and luteinization.
PCR and transcriptome analysis suggest that the genes CD3D (show CD3D Proteins) and PKRCQ together can be used as a model for differentiating between B-cell and T-cell acute lymphoblastic leukemia.
PKC-theta; is a critical factor for type 2 innate lymphoid cells activation that contributes to TH2 cell differentiation, which is associated with IRF4 (show IRF4 Proteins) and NFAT1 (show NFAT1 Proteins) expression in allergic lung inflammation.
Enhanced PRKCQ/PKCtheta; expression can promote growth-factor-independent growth, anoikis resistance, and migration. PRKCQ critically regulates growth and survival of a subset of TNBC.
Data suggest that, in T-lymphocytes, nitric oxide generated by eNOS (show NOS3 Proteins) S-nitrosylates Cys374 on ACTB (show ACTB Proteins) and thus regulates activation/recruitment of PRKCQ at immune synapse; S-nitrosylation of beta-actin (show ACTB Proteins) impairs actin binding to PFN1 (show PFN1 Proteins) and regulates protein transport in lamellipodia. (eNOS (show NOS3 Proteins) = nitric oxide synthase 3; ACTB (show ACTB Proteins) = beta-actin (show ACTB Proteins); PRKCQ = protein kinase C-theta; PFN1 (show PFN1 Proteins) = profilin-1 (show PFN1 Proteins))
PKCtheta;-induced phosphorylations control the ability of Fra-1 (show FOSL1 Proteins) to stimulate gene expression and breast cancer cell migration.
Within the nucleus, PKC-theta; catalytic activity maintains the Ser536 phosphorylation on the p65 subunit of NF-kappaB (also known as RelA) and can directly influence chromatin accessibility at transcriptional memory genes by regulating H2B deposition.
Data show that tonantzitlolone (TZL) was able to induce protein kinase c theta (PKCtheta;)-dependent heat shock transcription factor 1 (HSF1 (show HSF1 Proteins))phosphorylation.
The PRKCQ polymorphism is not associated with Behcet's Disease.
Sumoylation of PKC-theta; was essential for T cell activation. Desumoylation did not affect the catalytic activity of PKC-theta; but inhibited the association of CD28 (show CD28 Proteins) with PKC-theta; and filamin A (show FLNA Proteins) and impaired the assembly of a mature immunological synapse.
Together, these findings both in Jurkat T cells as well as in primary T cells indicate a regulatory role of Coro1A (show CORO1A Proteins) on PKCtheta; recruitment and function downstream of the TCR leading to NF-kappaB (show NFKB1 Proteins) transactivation.
PKCtheta; selectively inactivates the negative regulator of F-actin generation, Coronin 1A (show CORO1A Proteins), at the center of the T cell interface with the antigen presenting cell (APC (show APC Proteins)). This allows for effective generation of the large actin-based lamellum required for recruitment of the Notch (show NOTCH1 Proteins)-processing membrane metalloproteinase ADAM10 (show ADAM10 Proteins).
Results suggest that while PKCtheta; is involved in Treg cell differentiation in vivo, it is dispensable for Treg-mediated suppression.
Data show that pharmacological inhibition of Protein Kinase C theta (PKCtheta;) in Duchenne Muscular Dystrophy (DMD (show DMD Proteins)) can be considered an attractive strategy to modulate immune response and prevent the progression of the disease.
Knockdown of PKCtheta suppresses phosphorylation of IKK (show CHUK Proteins) and JNK (show MAPK8 Proteins) and consequently attenuates the HOCl-impaired insulin (show INS Proteins) signaling pathway.
Data indicate that Protein kinase C theta; (PKCtheta;) is critical for stabilizing Th17 cell phenotype.
Data suggest that protein kinase (show CDK7 Proteins) Ctheta (PKCtheta;) inhibition alone is insufficient for complete efficacy in rodent arthritis model.
Inhibition of PKC-theta preserves cardiac function and reduces fibrosis in streptozotocin-induced diabetic cardiomyopathy
Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role. The protein encoded by this gene is one of the PKC family members. It is a calcium-independent and phospholipid-dependent protein kinase. This kinase is important for T-cell activation. It is required for the activation of the transcription factors NF-kappaB and AP-1, and may link the T cell receptor (TCR) signaling complex to the activation of the transcription factors.
protein kinase C theta type
, PKC theta