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PRKCA / PKC-Alpha

protein kinase C, alpha

Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. Involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation in glioma cells. In intestinal cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Exhibits anti-apoptotic function in glioma cells and protects them from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, and in leukemia cells mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. Is highly expressed in a number of cancer cells where it can act as a tumor promoter and is implicated in malignant phenotypes of several tumors such as gliomas and breast cancers. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription.

Gene Name: protein kinase C, alpha
Family/Subfamily: Protein Kinase , PKC
Synonyms: PRKCA, Aging-associated gene 6, AAG6, Alpha PKC, PKC-A, Pkcalpha, Protein kinase C alpha type, PKC Alpha, PKC-alpha, PKCA, Protein kinase c alpha, Protein kinase C, alpha
Target Sequences: NM_002737 NP_002728.1 P17252

Publications (4)

1
Rod bipolar cells and horizontal cells form displaced synaptic contacts with rods in the outer nuclear layer of the nob2 retina. Bayley PR, Morgans CW. The Journal of comparative neurology. 2007 500:286-98. [PubMed:17111373]
2
Distribution of group-III metabotropic glutamate receptors in the retina. Quraishi S, Gayet J, Morgans CW, Duvoisin RM. The Journal of comparative neurology. 2007 501:931-43. [PubMed:17311335]
3
PKCalpha tumor suppression in the intestine is associated with transcriptional and translational inhibition of cyclin D1. Pysz MA, Leontieva OV, Bateman NW, Uronis JM, Curry KJ, Threadgill DW, Janssen KP, Robine S, Velcich A, Augenlicht LH, Black AR, Black JD. Experimental cell research. 2009 315:1415-28. (IHC, WB) [PubMed:19232344] [PMC:PMC2721478]
4
Protein kinase C mRNA and protein expressions in hypobaric hypoxia-induced cardiac hypertrophy in rats. Uenoyama M, Ogata S, Nakanishi K, Kanazawa F, Hiroi S, Tominaga S, Seo A, Matsui T, Kawai T, Suzuki S. Acta physiologica (Oxford, England). 2010 198:431-40. (IHC) [PubMed:19995357]
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PRKCA / PKC-Alpha (4)
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PRKCA / PKC-Alpha Protein - 12.5% SDS-PAGE Stained with Coomassie Blue.
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PRKCA / PKC-Alpha Protein - Western validation with an anti-DDK antibody * L: Control HEK293 lysate R: Over-expression lysate
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PRKCA / PKC-Alpha Protein - Western validation with an anti-DDK antibody * L: Control HEK293 lysate R: Over-expression lysate
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10 µg/$271; 50 µg/$382; 100 µg/$610; 200 µg/$762; 1 mg/$1,817; 500 µg/$1,378; 5 mg/$2,775; 2 mg/$1,998
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The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).