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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 02 Oct 2014.

Protein kinase C, beta

PKCbeta, protein kinase C beta
Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and 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 in cells. The protein encoded by this gene is one of the PKC family members. This protein kinase has been reported to be involved in many different cellular functions, such as B cell activation, apoptosis induction, endothelial cell proliferation, and intestinal sugar absorption. Studies in mice also suggest that this kinase may also regulate neuronal functions and correlate fear-induced conflict behavior after stress. Alternatively spliced transcript variants encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Protein Kinase C-alpha, HAD, V1a, CAN, ACID
Papers on PKCbeta
Open-label, single-arm, phase II study of enzastaurin in patients with follicular lymphoma.
Dreyling et al., Memphis, United States. In Br J Haematol, Jul 2014
This open-label, phase II study investigated whether enzastaurin, a protein kinase C-beta (PKCβ) inhibitor, had activity in patients with grade 1 or 2 follicular lymphoma (FL).
Corticosteroids modulate the expression of the PKC-anchoring protein RACK-1 and cytokine release in THP-1 cells.
Racchi et al., Milano, Italy. In Pharmacol Res, Mar 2014
Furthermore, to by-pass the defective PKC activation due to the decrease in RACK-1, we used a RACK-1 pseudosubstrate, that directly activates PKC-beta.
Neuron-specific alterations in signal transduction pathways associated with Alzheimer's disease.
Monoranu et al., Würzburg, Germany. In J Alzheimers Dis, Dec 2013
Mitogen activated protein kinase 1 (MAPK1) and protein kinase C beta (PRKCB) are thought to play a role in hyperphosphorylation, and PRCKB is thought to be involved in hypoxic stress and vascular dysfunction, and to trigger MAPK phosphorylation pathways.
Nephrilin peptide modulates a neuroimmune stress response in rodent models of burn trauma and sepsis.
Finnerty et al., Sunnyvale, United States. In Int J Burns Trauma, 2012
In a rat scald burn model, daily subcutaneous bolus injection of 4 mg/kg nephrilin significantly reduced the elevation of kidney tissue substance P, S100A9 gene expression, PMN infiltration and plasma inflammatory markers in the acute phase, while suppressing plasma CCL2 and insulin C-peptide, kidney p66shc-S36 phosphorylation and PKC-beta and CGRP in dorsal root ganglia at 14 days (chronic phase).
Computational investigation of pkcβ inhibitors for the treatment of diabetic retinopathy.
Lavanaya et al., Kākināda, India. In Bioinformation, 2012
The key gene responsible for causing diabetic retinopathy is protein kinase C beta (PKCβ).
Spatiotemporal regulation of PKC via interactions with AKAP7 isoforms.
Dodge-Kafka et al., Farmington, United States. In Biochem J, 2012
Data from studies using recombinant proteins suggest that isoforms of PRKA (A kinase anchor protein 7) exhibit high-affinity interactions with isoforms of PKC (primarily PKCalpha and PKCbeta used here); AKAP7 could dictate PKC localization/function.
Targeting the EWSR1-FLI1 oncogene-induced protein kinase PKC-β abolishes ewing sarcoma growth.
Tirode et al., Paris, France. In Cancer Res, 2012
We found that transcriptional activation of PRKCB was directly regulated by the chimeric fusion oncogene EWSR1-FLI1 that drives ewing sarcoma growth.
PKCβII modulation of myocyte contractile performance.
Westfall et al., Ann Arbor, United States. In J Mol Cell Cardiol, 2012
Results provide evidence PKCbeta(II) modulates contractile function via intermediate downstream pathway(s) in cardiac myocytes.
DOR activation inhibits anoxic/ischemic Na+ influx through Na+ channels via PKC mechanisms in the cortex.
Xia et al., Changzhou, China. In Exp Neurol, 2012
delta opioid receptor activation inhibits anoxia-induced Na(sodium)+ influx through Na+ channels via PKC, especially via PKCbetaII and PKCtheta; isozyme-dependent mechanisms in the cortex.
Protein quality control disruption by PKCβII in heart failure; rescue by the selective PKCβII inhibitor, βIIV5-3.
Mochly-Rosen et al., Stanford, United States. In Plos One, 2011
Data indicate PKCbetaII as a novel inhibitor of proteasomal function.
Increased sensitivity of serotonin on the voltage-dependent K+ channels in mesenteric arterial smooth muscle cells of OLETF rats.
Han et al., Pusan, South Korea. In Prog Biophys Mol Biol, 2010
The expression level of 5-HT(2A), but not 5-HT(2B), receptor and the expression levels of total PKC, PKCbeta, and PKCepsilon, but not PKCalpha, were higher in the mesenteric arteries of OLETF rats compared with LETO rats.
Genetic variants of the protein kinase C-beta 1 gene and development of end-stage renal disease in patients with type 2 diabetes.
Chan et al., Hong Kong, Hong Kong. In Jama, 2010
Genetic variants in the PRKCB1 gene were independently associated with development of ESRD in Chinese patients with type 2 diabetes.
Activation of protein kinase C isoforms and its impact on diabetic complications.
King et al., Boston, United States. In Circ Res, 2010
Clinical trials using a PKC-beta isoform inhibitor have been conducted, with some positive results for diabetic nonproliferative retinopathy, nephropathy, and endothelial dysfunction.
Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4.
Schüle et al., Freiburg, Germany. In Nature, 2010
phosphorylation of histone H3 at threonine 6 (H3T6) by protein kinase C beta I (PKCbeta(I), also known as PRKCbeta) is the key event that prevents LSD1 from demethylating H3K4 during AR-dependent gene activation
Small molecule kinase inhibitors in glioblastoma: a systematic review of clinical studies.
De Witt Hamer, Amsterdam, Netherlands. In Neuro Oncol, 2010
The main findings were that (i) efficacy of small-molecule kinase inhibitors in clinical studies with glioblastoma patients does not yet warrant a change in standard clinical practice and (ii) 6 main kinase targets for inhibitors have been evaluated in these studies: EGFR, mTOR, KDR, FLT1, PKCbeta, and PDGFR.
Diverse functions of protein kinase C isoforms in platelet activation and thrombus formation.
Poole et al., Bristol, United Kingdom. In J Thromb Haemost, 2010
Similarly, PKCbeta, PKCdelta and PKCtheta have non-redundant roles in platelet spreading, as absence of either PKCbeta or PKCtheta reduces spreading, whereas PKCdelta negatively regulates filopodial formation.
Signal transduction inhibitor therapy for lymphoma.
Gupta et al., Rochester, United States. In Hematology Am Soc Hematol Educ Program, 2009
This review focuses on three signaling pathways: the phosphatidylinositol 3-kinase/mammalian target of rapamycin (PI3K/mTOR) pathway, the B-cell receptor/spleen tyrosine kinase (BCR/Syk) pathway, and the protein kinase C-beta (PKC-β) pathway, known to be important to lymphoma cells.
Phase II study of enzastaurin, a protein kinase C beta inhibitor, in patients with relapsed or refractory diffuse large B-cell lymphoma.
Shipp et al., Indianapolis, United States. In J Clin Oncol, 2007
PURPOSE: Protein kinase C beta (PKCbeta) was identified by gene-expression profiling, preclinical evaluation, and independent immunohistochemical analysis as a rational therapeutic target in diffuse large B-cell lymphoma (DLBCL).
Protein kinase C beta and prolyl isomerase 1 regulate mitochondrial effects of the life-span determinant p66Shc.
Rizzuto et al., Ferrara, Italy. In Science, 2007
results show Pkcb, activated by oxidative conditions, induces phosphorylation of p66Shc & triggers its accumulation in mitochondria after it is recognized by Pin1; data identify a signaling route that activates an apoptotic inducer shortening life span
Control of local actin assembly by membrane fusion-dependent compartment mixing.
Bement et al., Madison, United States. In Nat Cell Biol, 2007
DAG, in turn, directs long-term recruitment of protein kinase Cbeta (PKCbeta) to exocytosing cortical granules, where it is required for activation of Cdc42 localized on the cortical granules.
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