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Protein kinase C, alpha

Protein Kinase C-alpha, PKCalpha
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 in cells. The protein encoded by this gene is one of the PKC family members. This kinase has been reported to play roles in many different cellular processes, such as cell adhesion, cell transformation, cell cycle checkpoint, and cell volume control. Knockout studies in mice suggest that this kinase may be a fundamental regulator of cardiac contractility and Ca(2+) handling in myocytes. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: V1a, CAN, ACID, HAD, ERK
Papers on Protein Kinase C-alpha
Keratin Isotypes Control Desmosome Stability and Dynamics through PKCα.
Magin et al., Leipzig, Germany. In J Invest Dermatol, Jan 2016
This revealed that K5/K14 filaments support stable desmosomes, whereas "wound healing" keratins K6/K17 induce elevated protein kinase C alpha-mediated desmosome disassembly and subsequent destabilization of epithelial sheets.
Pigment-Synthesizing Melanocytic Neoplasm With Protein Kinase C Alpha (PRKCA) Fusion.
Barnhill et al., Paris, France. In Jama Dermatol, Jan 2016
RNA sequencing identified a novel ATPase, Ca2+ transporting, plasma membrane 4(ATP2B4)-protein kinase C-alpha (PRKCA) fusion transcript.
Lipin-1 expression is critical for keratinocyte differentiation.
Shin et al., In J Lipid Res, Jan 2016
Lipin-1 knockdown also decreased the phosphorylation/activation of protein kinase C alpha (PKCα), whereas lipin-1 overexpression increased PKCα phosphorylation.
Calcium and Superoxide-Mediated Pathways Converge to Induce Nitric Oxide-Dependent Apoptosis in Mycobacterium fortuitum-Infected Fish Macrophages.
Mazumder et al., Delhi, India. In Plos One, Dec 2015
M. fortuitum could trigger intracellular-Ca+2 influx leading to the activation of calmodulin (CaM), protein kinase C alpha (PKCα) and Calmodulin kinase II gamma (CaMKIIg).
Anti-Tumor Activity of Yuanhuacine by Regulating AMPK/mTOR Signaling Pathway and Actin Cytoskeleton Organization in Non-Small Cell Lung Cancer Cells.
Lee et al., Seoul, South Korea. In Plos One, 2014
Further study revealed that YC modulates mTORC2-associated downstream signaling pathways with a decreased expressions of p-Akt, p-protein kinase C alpha (PKCα), p-ras-related C3 botulinum toxin substrate 1 (Rac1) and filamentous actin (F-actin) that are known to activate cell growth and organize actin cytoskeleton.
What the Genetic Background of Individuals with Asthma and Obesity Can Reveal: Is β2-Adrenergic Receptor Gene Polymorphism Important?
Danielewicz, Wrocław, Poland. In Pediatr Allergy Immunol Pulmonol, 2014
Genetic factors are essential for both conditions, and some of the candidate pleiotropic genes thought to be involved in the development of these diseases are ADRB2, vitamin D receptor (VDR), leptin (LEP), protein kinase C alpha (PRKCA), and tumor necrosis factor alpha (TNFα).
Mechanism of antiplatelet action of hypolipidemic, antidiabetic and antihypertensive drugs by PPAR activation: PPAR agonists: new antiplatelet agents.
Palomo et al., Talca, Chile. In Vascul Pharmacol, 2014
The mechanism of antiplatelet action of the drugs is by direct activation of PPARs with the inhibition of cyclooxygenase-1, protein kinase C-alpha, calcium mobilization, thromboxane A2, sCD40L, platelet microparticles and cAMP-phosphodiesterase, and the stimulation of proteins kinase G and A. Thus, these observations highlight PPARs as a novel therapeutic target for the treatment and prevention of cardiovascular diseases.
Regulation of chondrogenesis by protein kinase C: Emerging new roles in calcium signalling.
Mobasheri et al., Debrecen, Hungary. In Cell Signal, 2014
There is evidence that calcium signalling is a central regulator in differentiating chondroprogenitors; still, clear links between intracellular calcium signalling and prototypical calcium-dependent PKC subtypes such as PKCalpha have not been established.
Annexin A7 and SNAP23 interactions in alveolar type II cells and in vitro: a role for Ca(2+) and PKC.
Chander et al., Stony Brook, United States. In Biochim Biophys Acta, 2012
Annexin A7 may function in co-ordination with SNARE proteins and that protein kinase activation may be required for annexin A7 trafficking.
Reactive cysteine in the structural Zn(2+) site of the C1B domain from PKCα.
Igumenova et al., College Station, United States. In Biochemistry, 2012
Cys151 serves as an entry point for the reactive oxygen species that activate PKCalpha in a process involving Zn(2+) release.
Protein kinase Cα (PKCα) regulates p53 localization and melanoma cell survival downstream of integrin αv in three-dimensional collagen and in vivo.
Strömblad et al., Huddinge, Sweden. In J Biol Chem, 2012
PKCalpha constitutes a crucial component of the integrin alphav-mediated pathway(s) that promote p53 relocalization and melanoma survival.
PKCα suppresses 7,12-dimethylbenz[a]anthracene-induced skin tumor formation.
Chida et al., Tokyo, Japan. In Anticancer Res, 2012
PKCalpha suppresses tumor formation, but not tumor growth and progression in skin carcinogenesis.
Protein kinase Cα phosphorylates a novel argininosuccinate synthase site at serine 328 during calcium-dependent stimulation of endothelial nitric-oxide synthase in vascular endothelial cells.
Eichler et al., Tampa, United States. In J Biol Chem, 2012
calcium-dependent phosphorylation of argininosuccinate synthase Ser-328 is mediated by PKCalpha
Role and regulation of EGFR in actin remodeling in sperm capacitation and the acrosome reaction.
Etkovitz et al., Ramat Gan, Israel. In Asian J Androl, 2011
Protein kinase C alpha (PKCα), which is already activated at the beginning of the capacitation, also participates in PLD activation.
Adenosine inhibits the release of arachidonic acid in activated human peripheral mononuclear cells. A proposed model for physiologic and pathologic regulation in systemic lupus erythematosus.
Sipka, Debrecen, Hungary. In Scientificworldjournal, 2010
PKC alpha phosphorylates the cytosolic, Ca2+-dependent and steroid-sensitive PLA2 (type IV), whereas PKC delta phosphorylates the Ca2+-independent PLA2 (type VI).
Identification of RACK1 and protein kinase Calpha as integral components of the mammalian circadian clock.
Weitz et al., Boston, United States. In Science, 2010
findings show that Receptor for activated C kinase-1 (RACK1) and protein kinase C-alpha (PKCalpha) were recruited in a circadian manner into a nuclear BMAL1 complex during the negative feedback phase of the cycle
Inhibition of Fc epsilon RI-mediated mast cell responses by ES-62, a product of parasitic filarial nematodes.
Harnett et al., Singapore, Singapore. In Nat Med, 2007
ES-62 mediates these effects by forming a complex with Toll-like receptor 4, which results in the sequestration of protein kinase C-alpha (PKC-alpha).
Toll-like receptors modulate adult hippocampal neurogenesis.
Schwartz et al., Israel. In Nat Cell Biol, 2007
The activation of TLRs on the NPCs was mediated via MyD88 and induced PKCalpha/beta-dependent activation of the NF-kappaB signalling pathway.
Phase III study of gemcitabine and cisplatin with or without aprinocarsen, a protein kinase C-alpha antisense oligonucleotide, in patients with advanced-stage non-small-cell lung cancer.
Gandara et al., Madrid, Spain. In J Clin Oncol, 2006
PURPOSE: To determine whether aprinocarsen, an antisense oligonucleotide directed against protein kinase C-alpha, when added to the chemotherapy regimen of gemcitabine and cisplatin improved survival in patients with advanced non-small-cell lung cancer (NSCLC).
PKC-alpha regulates cardiac contractility and propensity toward heart failure.
Molkentin et al., Cincinnati, United States. In Nat Med, 2004
Results suggest that protein kinase C-alpha functions as a nodal integrator of cardiac contractility by sensing intracellular calcium and signal transduction events, which can profoundly affect propensity toward heart failure.
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