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p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Two widely expressed mammalian phosphatidylcholine (PC)-specific phospholipases D (PLD), PLD1 and PLD2, have been identified. Recombinantly expressed PLD2 has high basal activity and is insensitive to GTP-binding protein activators of PLD1 [Colley, W. C., et al. (1997) Curr. Biol. 7, 191-201]. To investigate the regulation of PLD2 we isolated PLD2, from mouse brain by immunoaffinity chromatography. The native and recombinant proteins have indistinguishable properties: PLD2 is potently activated by phosphoinositides with a vicinal 4,5-phosphate pair but is not stimulated by guanosine 5-O-(3-thio triphosphate)-activated ADP-ribosylation factor-1, Rho family GTP-binding proteins, or protein kinases C-alpha, or -beta1 ...
... , Authors: Jean-Loup Huret, Philippe Dessen. Published in: Atlas Genet Cytogenet Oncol Haematol.
Predicted to have protein serine/threonine kinase activity. Involved in blood coagulation. Is expressed in EVL; hatching gland; nervous system; neural tube; and trigeminal placode. Human ortholog(s) of this gene implicated in dilated cardiomyopathy; large cell carcinoma; malignant glioma (multiple); and reproductive organ cancer (multiple). Orthologous to human PRKCA (protein kinase C alpha ...
Reagents, Tools and Custom Services for molecular biology, specializing in the fields of Nano-Antibody development (nAb), Cellular Reprogramming (iPSC), Genome Editing, Fluorescent Proteins, RNAi, Viral Packaging and Protein expression.
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Plasmid PKCalpha.K/N.FLAG from Dr. Alex Tokers lab contains the insert PKC alpha and is published in Adv Exp Med Biol. 2002 . 506(Pt A):237-41. This plasmid is available through Addgene.
article{8dbcd382-933d-4ca5-9453-b9238b0812ee, abstract = {BACKGROUND: To investigate, in a rabbit model, the effect of two different doses of vigabatrin (VGB) on retinal function and morphology. METHODS: Twenty-nine rabbits of mixed strain were divided into two groups, receiving either high-dose (n = 15) or low-dose (n = 14) oral VGB treatment (cumulative dose 29.8 +/- 2.9 g and 14.2 +/- 0.6 g respectively). Ten rabbits receiving water served as control animals. The rabbits underwent three baseline ff-ERG measurements before initiation of VGB medication and two ff-ERG registrations during treatment, after 8 and 12-14 weeks respectively. At the end of the study, the expression of protein kinase C-alpha (PKC-alpha), gamma amino butyric acid (GABA) A receptors, vimentin, glial fibrillary acidic protein (GFAP) and peanut agglutinin (PNA) was examined in retinal sections from all rabbits. RESULTS: In animals of the high-dose group, the ff-ERG measurements revealed a significant decrease of isolated ...
Catalytic domain of the Protein Serine/Threonine Kinase, Classical Protein Kinase C. Serine/Threonine Kinases (STKs), Classical (or Conventional) Protein Kinase C (cPKC) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC ...
banhabackchulchunmatang: a Chinese medicine, widely used herbal medicine with vasodilatory actions; is associated with negative modulation of PKCalpha activation and NO production
Rapamycin-insensitive companion of mTOR (Rictor) is encoded by the RICTOR gene in humans. Rictor shares homology with pianissimo from D. discoidieum, STE20p from S. pombe, and AVO3p from S. cerevisiae. It is involved in the control of the mammalian target of rapamycin (mTOR) and is a subunit of mTORC2. mTORC2 is activated by growth factors but, unlike mTORC1, the complex is insensitive to nutrient levels. Rictor interacts with mTOR kinase to modulate the phosphorylation of protein Kinase C alpha (PKC alpha) and the actin cytoskeleton. Rictor is also known as RPTOR independent companion of MTOR, complex 2; PIA, KIAA1999, AVO3 homolog, hAVO3, AVO3, MGC39830, and TORC2-specific protein AVO3.. ...
Rapamycin-insensitive companion of mTOR (Rictor) is encoded by the RICTOR gene in humans. Rictor shares homology with pianissimo from D. discoidieum, STE20p from S. pombe, and AVO3p from S. cerevisiae. It is involved in the control of the mammalian target of rapamycin (mTOR) and is a subunit of mTORC2. mTORC2 is activated by growth factors but, unlike mTORC1, the complex is insensitive to nutrient levels. Rictor interacts with mTOR kinase to modulate the phosphorylation of protein Kinase C alpha (PKC alpha) and the actin cytoskeleton. Rictor is also known as RPTOR independent companion of MTOR, complex 2; PIA, KIAA1999, AVO3 homolog, hAVO3, AVO3, MGC39830, and TORC2-specific protein AVO3.. ...
Complete information for PICK1 gene (Protein Coding), Protein Interacting With PRKCA 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
References for Abcams Recombinant |em|X. laevis|/em| PKC alpha protein (ab60839). Please let us know if you have used this product in your publication
Urrence No Yes PKCa overexpression Negative Positive 1 0.677 0.444?.032 0.0699 1 3.494 2.117?.766 ,0.0001 1 5.224 3.435?.944 ,0.0001 1 6.147 3.627?0.420 ,0.0001
Institute of Human Nutrition, Columbia University, New York, New York 10032, USA. As F9 embryonal carcinoma cells differentiate into parietal endoderm-like cells, expression of conventional protein kinase C (PKC) changes. Undifferentiated stem cells express PKCbeta but not PKCalpha, whereas differentiated parietal endoderm cells express PKCalpha but not PKCbeta. To determine whether changes in PKCalpha and/or PKCbeta expression control retinoic acid (RA)- and dibutyryl cyclic AMP-induced F9 cell differentiation, we established cell lines stably expressing PKCalpha, PKCbeta, antisense PKCalpha, or antisense PKCbeta RNAs. Constitutive expression of PKCalpha or inhibition of PKCbeta expression in F9 stem cells enhanced RA induced differentiation, both by increasing total expression and accelerating RA-induced expression of laminins A, B1, B2, and type IV collagen. In addition, expressing PKCbeta in a parietal endoderm cell line caused these cells to retrodifferentiate into stem cells. Based on ...
PRKACA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 578 amino acids.
TY - JOUR. T1 - Phase II study of ISIS 3521, an antisense oligodeoxynucleotide to protein kinase C alpha, in patients with previously treated low-grade non-Hodgkins lymphoma. AU - Rao, S.. AU - Watkins, D.. AU - Cunningham, D.. AU - Dunlop, D.. AU - Johnson, P.. AU - Selby, P.. AU - Hancock, B.W.. AU - Fegan, C.. AU - Culligan, D.. AU - Schey, S.. AU - Morris, T. AU - Lissitchkov, T.. AU - Oliver, J.W.. AU - Holmlund, J.T.. PY - 2004/1. Y1 - 2004/1. N2 - Background: The purpose of this study was to assess the efficacy and safety of ISIS 3521, an antisense phosphorothioate oligonucleotide to protein kinase C in patients with relapsed low-grade non-Hodgkins lymphoma (NHL). Patients and methods: Twenty-six patients received ISIS 3521 (2 mg/kg/day) as a continuous infusion over 21 days of each 28-day cycle. Results: The median age of the patients was 53 years (range 37-77). Histological subtypes were low-grade follicular lymphoma (n=22) and B-cell small lymphocytic lymphoma (n=4). Twenty-one (81%) ...
The findings reported here suggest that AKAP150 is required for stuttering persistent Ca2+ sparklets and for the regulation of myogenic tone, blood pressure, and the development of angiotensin II-induced hypertension. Indeed, our data support a new model of Ca2+ signaling in vascular smooth muscle in which AKAP150 targets PKCα to relatively small regions of the sarcolemma of arterial myocytes. Local targeting of PKCα by AKAP150 is responsible for persistent Ca2+ sparklet activity, but not for rare, stochastic L-type Ca2+ channel openings (ie, low-activity Ca2+ sparklets). Our data suggest that AKAP150 is required for PKCα-dependent persistent Ca2+ sparklets and thus regulates arterial [Ca2+]i, myogenic tone, and blood pressure. Furthermore, AKAP150 is necessary for the development of angiotensin II-induced hypertension. Thus, we propose that AKAP150 regulates myogenic tone, blood pressure, and the development of angiotensin II-induced hypertension, at least in part, by local control of ...
Translocation of PKC isoforms has been implicated in mechanisms involved in heart failure, 22myocardial hypertrophy, 23and preconditioning. PKC isoforms are activated by phosphorylating enzymes such as G proteins and are modified in enzyme activity by phospholipids, diacylglycerol, increased Ca2+, nitric oxide, and superoxide anions. This is followed by translocation in an isoform-specific and cytoskeleton-mediated manner to subcellular targets, which can be directly visualized by immunohistochemical methods. Only 10 min of ischemia 24or brief administrations of pharmacologic agents 11,25may elicit significant PKC translocation. Recent evidence indicates that translocation is dependent on PKC binding to a family of proteins called receptors of activated C kinase. 26These anchoring proteins are highly specific, and each PKC isoenzyme can bind to only one receptor of activated C kinase. Thus, different PKC isoforms may be linked to distinctive aspects of myocardial function, and this functional ...
Receptor tyrosine kinase (RTK) c-Kit signalling is crucial for the proliferation, survival and differentiation of haematopoietic stem cells (HSCs). To further understand the mechanisms underlying these events we explored how the downstream mediators interact. The present study investigated the function of conventional protein kinase Cs (c-PKC) in c-Kit mediated signalling pathways in HSC-like cell lines. This analysis supported earlier findings, that steel factor (SF) activates c-PKC, extracellular signal-regulated kinase (Erk) and protein kinase B (PKB). The present results were consistent with an important role of c-PKC in the positive activation of Erk and for proliferation. Further, it was observed that c-PKC negatively regulated PKB activity upon SF stimulation, indicating that c-PKC acts as a suppressor of c-Kit signalling. Finally, these observations were extended to show that c-PKC mediated the phosphorylation of the endogenous c-Kit receptor on serine 746, resulting in decreased overall ...
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Plays an important role in caveolar biogenesis and morphology. Regulates caveolae morphology by inducing membrane curvature within caveolae (PubMed:19525939). Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in the lung and fat endothelia but not in the heart endothelia. Negatively regulates the size or stability of CAVIN complexes in the lung endothelial cells. May play a role in targeting PRKCA to caveolae (By similarity).
49 products from 14 suppliers. Compare and order PKC alpha ELISA Kits. View citations, images, detection ranges, sensitivity, prices and more. Recommended products for the most popular species. Our scientists will help you find the right ELISA kit for your needs.
Proteins Classical protein biochemistry concerns itself with the understanding of the biological function of a protein, its amino acid composition, its structure and binding partners, the subcellular localization of the protein and finally its physiological role in the organism. Besides applications in research, biochemical methods are used in the food industry for the detection of allergens and pathogens, in drug discovery for the identification and validation of target molecules and for the analysis of transgenic organisms. An additional important field is biotechnological protein production (e.g. enzymes, antibodies). ...
Proteins Classical protein biochemistry concerns itself with the understanding of the biological function of a protein, its amino acid composition, its structure and binding partners, the subcellular localization of the protein and finally its physiological role in the organism. Besides applications in research, biochemical methods are used in the food industry for the detection of allergens and pathogens, in drug discovery for the identification and validation of target molecules and for the analysis of transgenic organisms. An additional important field is biotechnological protein production (e.g. enzymes, antibodies). ...
K04166 AGTR1; angiotensin II receptor type 1 K04634 GNAQ; guanine nucleotide-binding protein G(q) subunit alpha K04635 GNA11; guanine nucleotide-binding protein subunit alpha-11 K05858 PLCB; phosphatidylinositol phospholipase C, beta [EC:3.1.4.11] K05858 PLCB; phosphatidylinositol phospholipase C, beta [EC:3.1.4.11] K05858 PLCB; phosphatidylinositol phospholipase C, beta [EC:3.1.4.11] K05858 PLCB; phosphatidylinositol phospholipase C, beta [EC:3.1.4.11] K04958 ITPR1; inositol 1,4,5-triphosphate receptor type 1 K04959 ITPR2; inositol 1,4,5-triphosphate receptor type 2 K04960 ITPR3; inositol 1,4,5-triphosphate receptor type 3 K02677 PRKCA; classical protein kinase C alpha type [EC:2.7.11.13] K19662 PRKCB; classical protein kinase C beta type [EC:2.7.11.13] K19663 PRKCG; classical protein kinase C gamma type [EC:2.7.11.13] K18050 PRKCE; novel protein kinase C epsilon type [EC:2.7.11.13] K06070 PKD; protein kinase D [EC:2.7.11.13] K06070 PKD; protein kinase D [EC:2.7.11.13] K06070 PKD; protein ...
Mounting evidence points to a key role of PKC signaling in the pathology of AD, a degenerative disease characterized by loss of synapses and plasticity mechanisms in the brain. The disease is associated with the appearance of extracellular amyloid plaques caused by the mis-cleavage of amyloid precursor protein (APP) and intracellular neurofibrillary tangles composed of hyperphosphorylated tau protein [83,84], two pathologies for which PKC involvement has been implicated over the years. But the critical importance of deregulated PKC signaling in AD was recently cemented by the results of an unbiased and comprehensive phosphoproteomic analysis of both human AD postmortem brains and brains from four AD mouse models [85]: PKC substrates accounted for over half of the core molecules that displayed increased phosphorylation in AD compared with control brains. The most robust increase in phosphorylation in AD compared with control brains occurred on MARCKS but also included PKC substrates such as ...
Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on Ser-473 of AKT2 and AKT3, Ser-660 of PRKCB and Ser-657 of PRKCA (PubMed:15808505, PubMed:17386267, PubMed:18162466). Isoform 2 seems to have a major role in regulating Akt signaling in hippocampal neurons (By similarity). Akt regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of Ser-473 of Akt triggers apoptosis and suppression of tumor growth. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation (PubMed:18162466). Dephosphorylates STK4 on Thr-387 leading to STK4 activation and apoptosis (PubMed:20513427). Dephosphorylates RPS6KB1 and is involved in regulation of cap-dependent translation ...
The perfect treatment for IgA nephropathy (IgAN) remains unknown. in 13 patients in group 1 (12.9% 95 CI 7.5 to 20.9%) and 12 patients in group 2 (11.3% CI 6.5 to 18.9%) (= 0.83). Five-year cumulative renal survival was comparable between groups (88 89%; = 0.83). Multivariate Cox regression analysis revealed that female gender systolic BP number of antihypertensive drugs ACE inhibitor use and proteinuria during follow-up predicted the risk of reaching the primary endpoint. Treatment significantly decreased proteinuria from 2.00 to 1 1.07 g/d during follow-up (< 0.001) on average with no difference between groups. Treatment-related adverse events were more frequent among those receiving azathioprine. In summary adding low-dose azathioprine to corticosteroids for 6 months does not provide additional benefit to patients with IgAN and may increase the risk for undesirable occasions. IgA nephropathy (IgAN) causes ESRD in a substantial percentage of sufferers.1-3 non-e of the procedure strategies ...
PKC activation constitutes one of the most widespread mechanisms for regulating PLD in eukaryotic cells (Liscovitch and Chalifa, 1994). PKC comprises a family of related enzymes that are differentially expressed in a variety of tissues and cell types (Nishizuka, 1995). At least 10 PKC isoforms have been described; recently, much effort has been directed at defining the role of PKC isoforms in the regulation of various biological processes, including activation of PLD. By reducing the levels of PKCα by an antisense method, we have demonstrated previously that PKCαregulates P2-purinergic activation of PLD in MDCK-D1 cells (Balboa et al., 1994). Data in this study have extended this observation by showing a good correspondence between the time-course of translocation of PKCα to membranes in response to ATP and the time-course of activation of PLD in response to this agonist. However, additional new data implicate a different mechanism for PLD activation in epinephrine-treated cells.. We have ...
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BACKGROUND: Runx transcription factors play critical roles in the developmental control of cell fate and contribute variously as oncoproteins and tumor suppressors to leukemia and other cancers. To discover fundamental Runx functions in the cell biology of animal development, we have employed morpholino antisense-mediated knockdown of the sea urchin Runx protein SpRunt-1. Previously we showed that embryos depleted of SpRunt-1 arrest development at early gastrula stage and underexpress the conventional protein kinase C SpPKC1. RESULTS: We report here that SpRunt-1 deficiency leads to ectopic cell proliferation and extensive apoptosis. Suppression of the apoptosis by pharmacological inhibition of caspase-3 prevents the ectopic proliferation and rescues gastrulation, indicating that many of the overt defects obtained by knockdown of SpRunt-1 are secondary to the apoptosis. Inhibition or knockdown of SpPKC1 also causes apoptosis, while cell survival is rescued in SpRunt-1 morphant embryos coinjected with
Extensions of the folding problem have become particularly important in the last ten years or so because of interest in such possibilities as the preparation of totally synthetic vaccines. Can one look at the structure of a protein, preferably in three dimensions, and select areas on the surface which might be expected to have a strong tendency to fold properly even when chopped out of the total structure? I will describe to you a few experiments relating to this biological problem in a few moments. My own interest began with some work that was carried out with Ruth Arnon and Michael Sela at the Weizmann Institute on the so-called lysozyme loop -- a small disulphide-stabilized extension on the enzyme. When this loop was prepared synthetically and attached to a non-immunogenic carrier, injection into animals produced antibodies which did indeed recognize the parent enzyme molecule. One might say that this material constituted a synthetic vaccine against the lysozyme molecule. Through the activity ...
We explored the influence of external electric fields (EEFs) on the stability of a glycine dipeptide model radical using high-level quantum chemical methods. Remotely located ions (Cl-/Na+) are used to implement EEF effects. The effects of these ions are reproduced using background point charges and oriented EEFs. Remote charges as far as 900 pm from the C-alpha radical center can be significantly stabilizing or destabilizing as a function of their relative orientation. The magnitude of these effects is also strongly dependent on the distance between the radical center and the charge location. After examining the strengths and weaknesses of some frequently used quantum mechanics methods in describing these effects properly, a comparison is made on the stability of dipeptide radicals bearing protonable or deprotonable side chains. In this group, the stability of the respective C-alpha radicals mainly depends on the preferred orientation of the charge-carrying side chain. ...
Gnificance of PKCa protein overexpression in gastric carcinoma was also investigated.Quantitative Real-Time PCR TestAt first quantitative real-time PCR test was
Two peptides derived from the C1B domain of protein kinase Cγ (PKCγ) were shown to associate with classical PKC isozymes and modulate their activities. These C1B peptides are designated C1B1 (amino acid residues 101-112 ...
PKC gamma, 0.1 ml. PKC gamma is an 80 kDa member of the conventional group (cPKCs: sensitive to calcium, diacylglycerol and phorbol esters) of the PKC family of serine/threonine family kinases that are involved in a wide range of physiological processes
Translocation of these novel PKC isoenzymes occurred significantly more slowly than either eGFP-PKCα or Ca2+, with t10-90 times in the range 25-30 s. Translocation of the DAG sensor (eGFP-C12) occurred with a similar time course which, together with the lack of requirement for an elevation of [Ca2+]i (Fig. 6), suggests that translocation of both eGFP-PKCδ and eGFP-PKCε is predominantly driven by changes in DAG. This is consistent with the dogma that nPKCs are DAG sensitive and Ca2+ insensitive. However, our experiments using BAPTA to annul changes in [Ca2+]i revealed additional complexity. eGFP-PKCδ translocated more rapidly in BAPTA-loaded cells and at the peak of the response a greater proportion of eGFP-PKCδ had translocated to the membrane. However, the total translocation during the response was similar in the presence or absence of BAPTA, suggesting that eGFP-PKCδ translocated more quickly, but not to a greater degree, in the absence of a Ca2+ response. It seems unlikely that this ...
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The roles of MEK, ERK, the epsilon and alpha isoforms of protein kinase C (PKC), and caveolin-1 in regulating collagen expression were studied in normal lung fibroblasts. Knocking down caveolin-1 gave particularly striking results. A 70% decrease caused a 5-fold increase in MEK/ERK activation and collagen expression. The combined data reveal a branched signaling pathway. In its central portion MEK activates ERK, leading to increased collagen expression. Two branches converge on MEK/ERK. In one, increased PKCepsilon leads to MEK/ERK activation. In another, increased PKCalpha induces caveolin-1 expression, which in turn inhibits MEK/ERK activation and collagen expression. Lung fibroblasts from scleroderma patients with pulmonary fibrosis showed altered signaling. Consistent with their overexpression of collagen, scleroderma lung fibroblasts contain more activated MEK/ERK and less caveolin-1 than normal lung fibroblasts. Because cutaneous fibrosis is the hallmark of scleroderma, we also studied ...
TY - JOUR. T1 - Amelioration of denervation-induced atrophy by clenbuterol is associated with increased PKC-alpha activity. AU - Sneddon, Alan Arthur. AU - Delday, Margaret Inkster. AU - Maltin, Charlotte. PY - 2000/7. Y1 - 2000/7. N2 - Rat soleus muscle was denervated for 3 or 7 days, and total membrane protein kinase C (PKC) activity and translocation and immunocytochemical localization of PKC isoforms were examined. Dietary administration of clenbuterol concomitant with denervation ameliorated the atrophic response and was associated with increased membrane PKC activity at both 3 (140%) and 7 (190%) days. Of the five PKC isoforms (alpha, epsilon, theta, zeta, and mu) detected in soleus muscle by Western immunoblotting, clenbuterol treatment affected only the PKC-alpha and PKC-theta forms. PKC-alpha was translocated to the membrane fraction upon denervation, and the presence of clenbuterol increased membrane-bound PKC-alpha and active PKC-alpha as assayed by Ser(657) phosphorylation. PKC-theta ...
The Ca2+-insensitive protein kinase C (PKC) isoforms ε, η, δ and ζ are possible direct downstream targets of phosphatidylinositol 3-kinase (PI3-K), and might therefore be involved in insulin signalling. Although isoform-specific changes in PKC expression have been reported for skeletal muscle and liver in insulin-resistant states, little is known about these isoforms in adipocytes. Therefore we studied (1) expression and subcellular localization of these isoforms in murine adipocytes, (2) translocation of specific isoforms to membranes in response to treatment with insulin and phorbol 12-myristate 13-acetate (PMA) and (3) regulation of expression in insulin-resistant states. The PKC isoforms ε, η, δ and ζ are expressed in adipocytes. Immunoreactivity for all isoforms is higher in the membranes than in the cytosol, but subcellular fractionation by differential centrifugation shows an isoform-specific distribution within the membrane fractions. PMA treatment of adipocytes induces ...
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The PKC family of serinethreonine kinases, including PRKCN (PKD3), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of
phdthesis{d275ee82-4648-4ce3-902e-0e2d63580bc3, abstract = {The human neuroblastoma cell line SH-SY5Y can be induced to differentiate into a neuronal sympathetic phenotype after treatment with 16 nM 12-O-tetradecanoyl phorbol 13-acetate (TPA) in serum, or by a combination of the growth factors basic fibroblast growth factor and insulin-like growth factor-I (bFGF/IGF-I). SH-SY5Y cells stably transfected with TrkA, the nerve growth factor (NGF) receptor, differentiate in response to NGF. The function of protein kinase C (PKC) isoforms in these processes was investigated. SH-SY5Y cells were shown to express PKC-alpha, PKC-epsilon and PKC-zeta protein. All three isoforms remained present during TPA- and bFGF/IGF-I-induced differentiation, while a higher TPA concentration (1.6 µM), that does not promote differentiation, down-regulated PKC-alpha completely. The use of the PKC inhibitor GF 109203X demonstrated that TPA-induced differentiation is completely, while growth factor induced differentiation ...
This study demonstrates that different PKC isoforms are differentially expressed in particular cellular components of ovarian follicles of pre-pubertal, pubertal and adult mouse ovaries.. Data obtained from H-Score evaluation of immunohistochemistry findings revealed that PKCα expression was more apparent in oocytes of all follicles in pre-pubertal, pubertal and adult ovaries, though it was also expressed in granulosa cells. Interestingly, in adult and pre-pubertal ovaries, intense immunostaining of PKCα in oocytes was statistically significant in primordial (PND60, PND7 and PND1), primary (PND60, PND7 and PND1) and secondary follicles (PND60 and PND7), whereas in PND21 ovaries only oocytes of primordial follicles had significantly higher immunostaining level of PKCα. These findings support the idea that PKCα expression in oocytes of larger follicles may have low significance due to granulosa-oocyte interactions during initiation of hormone dependent follicular growth [27],[28]. PKCα ...