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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 10 Nov 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
Molecular mechanisms of FK506-induced hypertension in solid organ transplantation patients.
New
Zuo et al., Changsha, China. In Chin Med J (engl), 31 Oct 2014
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.
S-allylcysteine prevents cisplatin-induced nephrotoxicity and oxidative stress.
New
Pedraza-Chaverri et al., Mexico. In J Pharm Pharmacol, Sep 2014
In the second stage, the effect of a single dose of SAC on the expression of nuclear factor-erythroid 2-related factor-2 (Nrf2), protein kinase C beta 2 (PKCβ2) and nicotinamide adenine dinucleotide phosphate oxidase subunits (p47(phox) and gp91(phox) ) was studied.
Protein kinase C-beta: an emerging connection between nutrient excess and obesity.
Review
New
Mehta et al., Columbus, United States. In Biochim Biophys Acta, Aug 2014
There is considerable evidence now supporting a possible role of protein kinase C beta (PKCβ) in energy homeostasis.
Open-label, single-arm, phase II study of enzastaurin in patients with follicular lymphoma.
New
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).
Indole diterpenoids and isocoumarin from the fungus, Aspergillus flavus, isolated from the prawn, Penaeus vannamei.
New
Zhu et al., Qingdao, China. In Mar Drugs, Jul 2014
Compound 1 showed PKC-beta inhibition with an IC50 value of 15.6 μM.
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
Review
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.
Review
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.
Impact
GeneRIF
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.
Review
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.
Impact
GeneRIF
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
Signal transduction inhibitor therapy for lymphoma.
Review
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.
Impact
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.
Impact
GeneRIF
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.
Impact
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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