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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

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
Expression and activity of eIF6 trigger malignant pleural mesothelioma growth in vivo.
Biffo et al., Milano, Italy. In Oncotarget, Dec 2015
Enzastaurin is a PKC beta inhibitor used in clinical trials.
Current status and future directions of anti-angiogenic therapy for gliomas.
Winkler et al., Heidelberg, Germany. In Neuro Oncol, Nov 2015
UNASSIGNED: Molecular targets for the pathological vasculature are the vascular endothelial growth factor (VEGF)/VEGF receptor axis, integrins, angiopoietins, and platelet-derived growth factor receptor (PDGFR), as well as several intracellular or downstream effectors like protein kinase C beta and mammalian target of rapamycin (mTOR).
An avian model for ascertaining the mechanisms of organophosphate neuroteratogenicity and its therapy with mesenchymal stem cell transplantation.
Yanai et al., Israel. In Neurotoxicol Teratol, Jul 2015
no changes in gene expression of choline transporter, PKC beta and D2 were found following chlorpyrifos exposure.
Apoptin interacts with and regulates the activity of protein kinase C beta in cancer cells.
Tavassoli et al., London, United Kingdom. In Apoptosis, Jun 2015
Apoptin, the VP3 protein from chicken anaemia virus (CAV), induces tumour cell-specific cell death and represents a potential future anti-cancer therapeutic.
A deleterious gene-by-environment interaction imposed by calcium channel blockers in Marfan syndrome.
MIBAVA Leducq Consortium et al., Baltimore, United States. In Elife, 2014
We have identified protein kinase C beta (PKCβ) as a critical mediator of this pathway and demonstrate that the PKCβ inhibitor enzastaurin, and the clinically available anti-hypertensive agent hydralazine, both normalize aortic growth in Marfan mice, in association with reduced PKCβ and ERK1/2 activation.
Different localization and expression of protein kinase C-beta in kidney cortex of diabetic nephropathy mice and its role in telmisartan treatment.
Yao et al., Hangzhou, China. In Am J Transl Res, 2014
The expression of transforming growth factor-beta 1 and vascular endothelial growth factor in glomeruli was detected by immunohistochemistry. RESULTS: Compared to the normal mice, the expression and localization of protein kinase C-beta I and beta II are differed in diabetic nephropathy mice, with increased expression of protein kinase C-beta I but decreased level of protein kinase C-beta II.
Protein kinase C-beta: An emerging connection between nutrient excess and obesity.
Mehta et al., Columbus, United States. In Biochim Biophys Acta, 2014
There is considerable evidence now supporting a possible role of protein kinase C beta (PKCβ) in energy homeostasis.
Molecular mechanisms of FK506-induced hypertension in solid organ transplantation patients.
Zuo et al., Changsha, China. In Chin Med J (engl), 2013
The conventional protein kinase C beta II (cPKCβII)-mediated phosphorylation of endothelial nitric oxide (NO) synthase at Thr495, which reduces the production of NO, was activated by calcium ion leakage.
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.
Painful diabetic neuropathy: an update.
Dutta et al., Chandīgarh, India. In Ann Neurosci, 2011
The newer therapies under studies are NMDA antagonists, aldose reductase inhibitors, neurotropic factors, vascular endothelial growth factor, Gamma linolenic acid, protein kinase C beta inhibitors, immune therapy, hyperbaric oxygen and alpha lipoic acid.
Recent advances in the management of diabetic distal symmetrical polyneuropathy.
Tesfaye, Sheffield, United Kingdom. In J Diabetes Investig, 2011
Studies in experimental diabetes examining the pathogenesis of DPN have identified a number of metabolic abnormalities including polyol pathway hyperactivity, increased advanced glycation end-point formation, alterations in the protein kinase C beta pathway through diacylglycerol and oxidative stress.
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.
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
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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