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Academic literature on the topic 'PKC'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 July 2024

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Journal articles on the topic "PKC"

1

Muramatsu, M., K. Kaibuchi, and K. Arai. "A protein kinase C cDNA without the regulatory domain is active after transfection in vivo in the absence of phorbol ester." Molecular and Cellular Biology 9, no. 2 (February 1989): 831–36. http://dx.doi.org/10.1128/mcb.9.2.831-836.1989.

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We constructed mutant protein kinase C (PKC) cDNAs which expressed PKC activity in vivo in the absence of phorbol ester activation. A hybrid PKC gene, PKAC, was constructed by substituting the coding region for the N-terminal 253 amino acids of PKC alpha with the N-terminal 17 amino acids of the cyclic AMP-dependent protein kinase catalytic subunit (PKA). A truncated PKC gene, delta PKC beta, lacking the coding region for amino acid positions 6 to 159 of PKC beta was also constructed. These mutant kinase genes expressed under the control of the SR alpha promoter activated the c-fos gene enhancer in Jurkat cells and initiated maturation of Xenopus laevis oocytes. Phorbol ester binding activity was absent in both constructs but was preserved in another hybrid gene, PKCA, which was composed of the coding region for 1 to 253 amino acids of PKC alpha at the N-terminal side and the coding region for 18 to 350 amino acids of PKA at the C-terminal side. These results indicate that elimination of the regulatory domain of PKC produces constitutively active PKC that can bypass activation by the phorbol ester. delta PKC beta, in synergy with a calcium ionophore, was capable of activating the interleukin 2 promoter, indicating that cooperation of PKC-dependent and calcium-dependent pathways is necessary for activation of the interleukin 2 gene.

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2

Muramatsu, M., K. Kaibuchi, and K. Arai. "A protein kinase C cDNA without the regulatory domain is active after transfection in vivo in the absence of phorbol ester." Molecular and Cellular Biology 9, no. 2 (February 1989): 831–36. http://dx.doi.org/10.1128/mcb.9.2.831.

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We constructed mutant protein kinase C (PKC) cDNAs which expressed PKC activity in vivo in the absence of phorbol ester activation. A hybrid PKC gene, PKAC, was constructed by substituting the coding region for the N-terminal 253 amino acids of PKC alpha with the N-terminal 17 amino acids of the cyclic AMP-dependent protein kinase catalytic subunit (PKA). A truncated PKC gene, delta PKC beta, lacking the coding region for amino acid positions 6 to 159 of PKC beta was also constructed. These mutant kinase genes expressed under the control of the SR alpha promoter activated the c-fos gene enhancer in Jurkat cells and initiated maturation of Xenopus laevis oocytes. Phorbol ester binding activity was absent in both constructs but was preserved in another hybrid gene, PKCA, which was composed of the coding region for 1 to 253 amino acids of PKC alpha at the N-terminal side and the coding region for 18 to 350 amino acids of PKA at the C-terminal side. These results indicate that elimination of the regulatory domain of PKC produces constitutively active PKC that can bypass activation by the phorbol ester. delta PKC beta, in synergy with a calcium ionophore, was capable of activating the interleukin 2 promoter, indicating that cooperation of PKC-dependent and calcium-dependent pathways is necessary for activation of the interleukin 2 gene.

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Tremblay, Patricia G., and Marc-André Sirard. "Gene analysis of major signaling pathways regulated by gonadotropins in human ovarian granulosa tumor cells (KGN)†." Biology of Reproduction 103, no. 3 (May 19, 2020): 583–98. http://dx.doi.org/10.1093/biolre/ioaa079.

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Abstract The female reproductive function largely depends on timing and coordination between follicle-stimulating hormone (FSH) and luteinizing hormone. Even though it was suggested that these hormones act on granulosa cells via shared signaling pathways, mainly protein kinases A, B, and C (PKA, PKB, and PKC), there is still very little information available on how these signaling pathways are regulated by each hormone to provide such differences in gene expression throughout folliculogenesis. To obtain a global picture of the principal upstream factors involved in PKA, PKB, and PKC signaling in granulosa cells, human granulosa-like tumor cells (KGN) were treated with FSH or specific activators (forskolin, SC79, and phorbol 12-myristate 13-acetate) for each pathway to analyze gene expression with RNA-seq technology. Normalization and cutoffs (FC 1.5, P ≤ 0.05) revealed 3864 differentially expressed genes between treatments. Analysis of major upstream regulators showed that PKA is a master kinase of early cell differentiation as its activation resulted in the gene expression profile that accompanies granulosa cell differentiation. Our data also revealed that the activation of PKC in granulosa cells is also a strong differentiation signal that could control “advanced” differentiation in granulosa cells and the inflammatory cascade that occurs in the dominant follicle. According to our results, PKB activation provides support for PKA-stimulated gene expression and is also involved in granulosa cell survival throughout follicular development. Taken together, our results provide new information on PKA, PKB, and PKC signaling pathways and their roles in stimulating a follicle at the crossroad between maturation/ovulation and atresia.

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Blount, Mitsi A., Penelope Cipriani, Sara K. Redd, Ronald J. Ordas, Lauren N. Black, Diane L. Gumina, Carol A. Hoban, Janet D. Klein, and Jeff M. Sands. "Activation of protein kinase Cα increases phosphorylation of the UT-A1 urea transporter at serine 494 in the inner medullary collecting duct." American Journal of Physiology-Cell Physiology 309, no. 9 (November 1, 2015): C608—C615. http://dx.doi.org/10.1152/ajpcell.00171.2014.

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Hypertonicity increases urea transport, as well as the phosphorylation and membrane accumulation of UT-A1, the transporter responsible for urea permeability in the inner medullary collect duct (IMCD). Hypertonicity stimulates urea transport through PKC-mediated phosphorylation. To determine whether PKC phosphorylates UT-A1, eight potential PKC phosphorylation sites were individually replaced with alanine and subsequently transfected into LLC-PK1 cells. Of the single mutants, only ablation of the S494 site dampened induction of total UT-A1 phosphorylation by the PKC activator phorbol dibutyrate (PDBu). This result was confirmed using a newly generated antibody that specifically detected phosphorylation of UT-A1 at S494. Hypertonicity increased UT-A1 phosphorylation at S494. In contrast, activators of cAMP pathways (PKA and Epac) did not increase UT-A1 phosphorylation at S494. Activation of both PKC and PKA pathways increased plasma membrane accumulation of UT-A1, although activation of PKC alone did not do so. However, ablating the PKC site S494 decreased UT-A1 abundance in the plasma membrane. This suggests that the cAMP pathway promotes UT-A1 trafficking to the apical membrane where the PKC pathway can phosphorylate the transporter, resulting in increased UT-A1 retention at the apical membrane. In summary, activation of PKC increases the phosphorylation of UT-A1 at a specific residue, S494. Although there is no cross talk with the cAMP-signaling pathway, phosphorylation of S494 through PKC may enhance vasopressin-stimulated urea permeability by retaining UT-A1 in the plasma membrane.

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Lacroix, M., and A. Hontela. "Regulation of acute cortisol synthesis by cAMP-dependent protein kinase and protein kinase C in a teleost species, the rainbow trout (Oncorhynchus mykiss)." Journal of Endocrinology 169, no. 1 (April 1, 2001): 71–78. http://dx.doi.org/10.1677/joe.0.1690071.

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The effects of cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) on acute ACTH-stimulated cortisol secretion were assessed using a specific PKA inhibitor (H-89) and a PKC activator (phorbol 12-myristate 13-acetate, PMA) in dispersed head kidney cells of rainbow trout (Oncorhynchus mykiss). To investigate the sites of action of both PKA and PKC, pregnenolone (a cortisol precursor stemmed from the rate limiting step in cortisol synthesis) and 25-OH-cholesterol (an exogenous substrate that bypasses the rate limiting step) were used as substrates, with and without ACTH stimulation. Inhibition of PKA decreased ACTH-stimulated cortisol secretion while activation of PKC had the same effect, demonstrating that PKA stimulates and PKC inhibits cortisol synthesis. Inhibition of PKA and activation of PKC had no significant effect on pregnenolone-stimulated cortisol synthesis, indicating that both PKA and PKC act upstream from the pregnenolone step. Inhibition of PKA and activation of PKC had no significant effect on basal cortisol secretion in the presence of 25-OH-cholesterol, suggesting that PKA and PKC exert their effects on the mitochondrial cholesterol translocation step. This study provided evidence for the stimulatory role of PKA and the inhibitory role of PKC in the signalling pathways leading to cortisol synthesis in teleosts.

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Itoh, Hiroyuki, Shinji Yamamura, J. Anthony Ware, Shaobin Zhuang, Shinsuke Mii, Bo Liu, and K. Craig Kent. "Differential effects of protein kinase C on human vascular smooth muscle cell proliferation and migration." American Journal of Physiology-Heart and Circulatory Physiology 281, no. 1 (July 1, 2001): H359—H370. http://dx.doi.org/10.1152/ajpheart.2001.281.1.h359.

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Vascular smooth muscle cell (SMC) migration and proliferation contribute to intimal hyperplasia, and protein kinase C (PKC) may be required for both events. In this report, we investigated the role of PKC in proliferation and migration of SMC derived from the human saphenous vein. Activation of PKC by phorbol-12,13-dibutyrate (PDBu) or (−)-indolactam [(−)-ILV] increases SMC proliferation. Downregulation of PKC activity by prolonged incubation with phorbol ester or inhibition of PKC with chelerythrine in SMC diminished agonist-stimulated proliferation. In contrast, stimulation of PKC with PDBu or (−)-ILV inhibited basal and agonist-induced SMC chemotaxis. Moreover, downregulation of PKC or inhibition with chelerythrine accentuated migration. We postulated that the inhibitory effect of PKC on SMC chemotaxis was mediated through cAMP-dependent protein kinase (protein kinase A, PKA). In support of this hypothesis, we found that activation of PKC in SMC stimulated PKA activity. The cAMP agonist forskolin significantly inhibited SMC chemotaxis. Furthermore, the inhibitory effect of PKC on SMC chemotaxis was completely reversed by cAMP or PKA inhibitors. In search of the PKC isotype(s) underlying these differential effects of PKC in SMC, we identified eight isotypes expressed in human SMC. Only PKC-α, -βI, -δ, and -ε were eliminated by downregulation, suggesting that one or more of these four enzymes facilitate the observed phorbol ester-dependent effects of PKC in SMC. In summary, we found that PKC activation enhances proliferation but inhibits migration of human vascular SMC. These differential effect of PKC on vascular cells appears to be mediated through PKC-α, -βI, -δ, and/or -ε.

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Chen, Yongyue, Guillermo A. Altenberg, and Luis Reuss. "Mechanism of activation of Xenopus CFTR by stimulation of PKC." American Journal of Physiology-Cell Physiology 287, no. 5 (November 2004): C1256—C1263. http://dx.doi.org/10.1152/ajpcell.00229.2004.

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PKA-mediated phosphorylation of the regulatory (R) domain plays a major role in the activation of the human cystic fibrosis transmembrane conductance regulator (hCFTR). In contrast, the effect of PKC-mediated phosphorylation is controversial, smaller than that of PKA, and dependent on the cell type. In the present study, we expressed Xenopus CFTR ( XCFTR) and hCFTR in Xenopus oocytes and examined their responses (i.e., macroscopic membrane conductance) to maximal stimulation by PKC and PKA agonists. With XCFTR, the average response to PKC was approximately sixfold that of PKA stimulation. In contrast, with hCFTR, the response to PKC was ∼90% of the response to PKA stimulation. The reason for these differences was the small response of XCFTR to PKA stimulation. Using the substituted cysteine accessibility method, we found no evidence for insertion of functional CFTR channels in the plasma membrane in response to PKC stimulation. The increase in macroscopic conductance in response to PKC stimulation of XCFTR was due to an approximately fivefold increase in single-channel open probability, with a minor (∼30%) increase in single-channel conductance. The responses of XCFTR to PKC stimulation and of hCFTR to PKA stimulation were mediated by similar increases in Po. In both instances, there were no changes in the number of channels in the membrane. We speculate that in animals other than humans, PKC stimulation may be the dominant mechanism for activation of CFTR.

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Hou, Lili, Lei Zhu, Min Zhang, Xingyi Zhang, Guoqing Zhang, Zhenwei Liu, Qiang Li, and Xin Zhou. "Participation of Antidiuretic Hormone (ADH) in Asthma Exacerbations Induced by Psychological Stress via PKA/PKC Signal Pathway in Airway-Related Vagal Preganglionic Neurons (AVPNs)." Cellular Physiology and Biochemistry 41, no. 6 (2017): 2230–41. http://dx.doi.org/10.1159/000475638.

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Aims: Present study was performed to examine whether ADH was implicated in psychological stress asthma and to explore the underlying molecular mechanism. Methods: We not only examined ADH levels in the cerebrospinal fluid (CSF) via radioimmunoassay, but also measured ADH receptor (ADHR) expression in airway-related vagal preganglionic neurons (AVPNs) through real-time PCR in all experimental mice. Western blotting was performed to evaluate the relationship between ADH and PKA/PKC in psychological stress asthma. Finally, the role of PKA/PKC in psychological stress asthma was analyzed. Results: Marked asthma exacerbations were noted owing to significantly elevated levels of ADH and ADHR after psychological stress induction as compared to OVA alone (asthma group). ADHR antagonists (SR-49095 or SR-121463A) dramatically lowered higher protein levels of PKAα and PKCα induced by psychological stress as compared to OVA alone, suggesting the correlation between ADH and PKA/PKC in psychological stress asthma. KT-5720 (PKA inhibitor) and Go-7874 (PKC inhibitor) further directly revealed the involvement of PKA/PKC in psychological stress asthma. Some notable changes were also noted after employing PKA and PKC inhibitors in psychological stress asthma, including reduced asthmatic inflammation (lower eosinophil peroxidase (EPO) activity, myeloperoxidase (MPO) activity, immunoglobulin E (IgE) level, and histamine release), substantial decrements in inflammatory cell counts (eosinophils and lymphocytes), and decreased cytokine secretion (IL-6, IL-10, and IFN-γ), indicating the involvement of PKA/PKC in asthma exacerbations induced by psychological stress. Conclusion: Our results strongly suggested that ADH participated in psychological stress-induced asthma exacerbations via PKA/PKC signal pathway in AVPNs.

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Wartmann, M., D. A. Jans, P. J. Parker, Y. Nagamine, B. A. Hemmings, S. Jaken, U. Eppenberger, and D. Fabbro. "Overexpression of the alpha-type protein kinase (PK) C in LLC-PK1 cells does not lead to a proportional increase in the induction of two 12-O-tetradecanoylphorbol-13-acetate-inducible genes." Cell Regulation 2, no. 6 (June 1991): 491–502. http://dx.doi.org/10.1091/mbc.2.6.491.

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Phorbol esters, by activating protein kinase C (PKC), induce the expression of the urokinase-type plasminogen activator (uPA) gene and the proto-oncogene c-fos in LLC-PK1 (PK1) porcine kidney epithelial cells. To investigate the role of PKC in the regulation of these two 12-O-tetradecanoylphorbol-13-acetate (TPA)-inducible genes, the alpha-type PKC, the predominant subtype present in the PK1 cells, was overexpressed in this cell line. Two clonal PK1 derivatives overexpressing the alpha PKC 15- and 20-fold, respectively, were established. Compared with the parental and control cells, only a modest but substantially sustained (2- to 3-fold) increase in the accumulation of uPA as well as c-fos mRNAs were observed by TPA in these cells. These results indicate that the extent of induction of these genes mediated by TPA was not proportional to the amounts of alpha-type PKC stably overexpressed in these cells, suggesting that factor(s) downstream of the activation of the alpha PKC appear to be rate limiting for the induction of both TPA-inducible genes in PK1 cells.

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Wu, D., I. J. Clarke, and C. Chen. "The role of protein kinase C in GH secretion induced by GH-releasing factor and GH-releasing peptides in cultured ovine somatotrophs." Journal of Endocrinology 154, no. 2 (August 1997): 219–30. http://dx.doi.org/10.1677/joe.0.1540219.

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Abstract The involvement of protein kinase C (PKC) in the action of GH-releasing factor (GRF) and synthetic GH-releasing peptides (GHRP-2 and GHRP-6) was investigated in ovine somatotrophs in primary culture. In partially purified sheep somatotrophs, GRF and GHRP-2 caused translocation of PKC activity from the cytosol to the cell membranes and caused GH release in a dose- and time-dependent manner. GHRP-6 did not cause PKC translocation. The PKC inhibitors, calphostin C, staurosporine and chelerythrine, partially reduced GH release in response to GRF and GHRP-2 at doses which selectively inhibit PKC activity. These inhibitors totally abolished GH release caused by phorbol 12-myristate 13-acetate (PMA). Down-regulation of PKC by the treatment of cells with phorbol 12,13-dibutyrate for 16 h caused a significant (P<0·001) reduction in total PKC activity and totally abolished PKC translocation in response to a challenge with GRF, GHRP-2 or PMA. In addition, down-regulation abolished GH release in response to GRF, GHRP-2 or GHRP-6. Treatment of cells with H89, a selective PKA inhibitor, totally blocked GH release caused by either GRF or GHRP-2 and partially reduced PMA-induced GH release. H89 had no effect on PKC translocation caused by GRF, GHRP-2 or PMA and did not affect GH release caused by GHRP-6. These data suggest that GHRP-2 and GRF activate PKC in addition to stimulating adenylyl cyclase activity. Although the cAMP–protein kinase A (PKA) pathway is the major signalling pathway employed by GRF and GHRP-2, the activation of PKC may potentiate signalling via the cAMP–PKA pathway in ovine GH secretion. Importantly, the effect of PMA in increasing the secretion of GH from ovine somatotrophs is effected, in part, by up-regulation of the cAMP–PKA pathway. We conclude that there is cross-talk between the PKC pathway and the cAMP–PKA pathway in ovine somatotrophs during the action of GRF or GHRP. Journal of Endocrinology (1997) 154, 219–230

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Dissertations / Theses on the topic "PKC"

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Plammootil, Suma Mary. "Herstellung und Etablierung von 4-Hydroxytamoxifen aktivierbaren PKC[alpha]- [PKC alpha]-, PKC[beta]1- [PKC beta1] und PKCd--Fusionsproteinen [PKC delta-Fusionsproteinen]." [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=971703302.

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Snider, Adam K. "PKC gamma regulates connexin 57." Thesis, Manhattan, Kan. : Kansas State University, 2010. http://hdl.handle.net/2097/4128.

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Bahte, Svenja-Katharina Paula. "Identifikation neuer Bindungspartner von PKC- d [PKC-delta] mit Hilfe des Yeast-two-hybrid-Screens." [S.l.] : [s.n.], 2004. http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&doc_number=013081490&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA.

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Cheng, Sam Xian Jun. "Functional significance of phosphorylation of rat renal Na+,K+-ATPase by PKA and PKC /." Stockholm, 1998. http://diss.kib.ki.se/1998/91-628-2971-8.

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Quittau-Prévostel, Corinne. "Mutant D294G de la PKC[alpha] tumorigénèse humaine : la PKC[alpha], un nouveau suppresseur de tumeur." Montpellier 1, 1997. http://www.theses.fr/1997MON1T005.

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ZINI, SILVIA. "PKC: Paffard Keatinge-Clay architetto itinerante." Doctoral thesis, Università IUAV di Venezia, 2015. http://hdl.handle.net/11578/278352.

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Worthmann, Kirstin [Verfasser]. "Die Rolle der atypischen Protein Kinase C Isoformen PKC[lambda]/[iota] und PKC[zeta] in Podozyten / Kirstin Worthmann." Hannover : Technische Informationsbibliothek und Universitätsbibliothek Hannover, 2011. http://d-nb.info/1012625508/34.

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Cabrerizo, Benito Yolanda. "Studies on a PKC-PLD-MAPK pathway." Thesis, University College London (University of London), 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.399767.

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Kostelecky, B. D. "An investigation of PKC isoform functional specificity." Thesis, University College London (University of London), 2009. http://discovery.ucl.ac.uk/18705/.

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Protein kinase C (PKC) isozymes are vital signalling proteins in many intracellular processes including cell survival, proliferation and migration. As such, changes in their expression levels have been linked to many types of cancer. The various PKC family members provoke differential responses in cancer highlighting the need for study of individual isoforms. This investigation of PKC has aimed to determine how kinase domain structure, regulatory region interactions and binding partners confer functional specificity to individual PKC isoforms. X-ray crystallographic, biochemical and biophysical studies have been employed to explore the architecture of these PKC interactions. A panel of recombinant PKC kinase domains has been cloned, expressed and purified to characterise their maturation, activities and structures. Kinetic constants have been determined for several PKC kinase domains in various phosphorylation states. Additionally, inhibition by novel low molecular weight inhibitors provided by collaborators at Cancer Research Technologies (CRT) has been probed. The PKCζ kinase domain has been crystallised with one of the CRT inhibitors and the structure determined at 2.8Å resolution. A panel of PKC isoform regulatory regions has also been expressed and purified. The results presented here show it is possible to reconstitute an intact PKC holoenzyme complex after expression of the domains as individual polypeptides. The protocols and materials developed during this thesis project will be further used in the laboratory with the aim of crystallising a PKC holoenzyme complex. This thesis also presents the crystal structure of PKCε-binding partner 14-3-3 bound to an asymmetric PKCε di-phosphorylated peptide determined at 2.2Å resolution. The PKCε di-phosphorylated peptide in the crystal structure was derived from the PKCε V3 variable region containing one consensus 14-3-3-phospho-binding motif and one divergent 14-3-3-binding motif. A thermodynamic analysis of the interaction between 14-3-3 and the PKCεV3 di-phosphopeptide reveals an increased affinity more than two orders of magnitude greater than the singly phosphorylated species. Together, the results of this study provide a multifaceted examination of PKC functional specificity by isoform-specific low molecular weight inhibitors, regulatory domains and binding partner interactions and provide a solid platform for exploring further aspects of PKC regulation.

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Peel, N. R. "Dissecting compartmentalised atypical PKC controls in cell migration." Thesis, University College London (University of London), 2014. http://discovery.ucl.ac.uk/1419046/.

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Atypical Protein Kinase C (aPKC) isoforms are essential regulators of polarised cell behaviour and in migrating NRK cells translocate to the leading edge in a complex with the exocyst and KIBRA. Engineered delivery of upstream signals to the plasma membrane places leading edge ERK activation downstream of aPKC and demonstrates partial sufficiency in regulating cell migration and adhesion. This model system provides the opportunity to probe the leading edge to better understand events downstream of aPKC. Multiple screening approaches have identified cytoskeletal and translation processes as putative targets of this pathway. Based on in silico candidate screening it is shown that multi-site phosphorylation of Parvin alpha is important for focal adhesion maturation. These phosphorylation events are triggered following acute focal adhesion turnover, which can be blocked by aPKC and MEK inhibition. Based upon proteomic approaches, a novel role for the putative aPKC/ERK substrate Cdc42 effector protein 1 (Cdc42ep1) has been identified. siRNA knockdown of Cdc42ep1 phenocopies aPKC loss; focal adhesions enlarge and turnover less efficiently. This impacts on polarized cell motility as knockdown prevents cell orientation and efficient wound closure. Finally, a novel role for aPKC is reported in relation to leading edge translation. Active translation at the leading edge is reduced following aPKC and MEK inhibition and compartmentalised distribution of translation factors is modulated following pathway intervention. This includes the eukaryotic translation initiation factor 3A (eIF3A), one hit identified by proteomic screening. eIF3A interacts with the exocyst and localises to the leading edge in an aPKC-dependent fashion. In addition, eIF3A is shown to regulate polarised migration and adhesion maturation. The data presented in this thesis illustrate combined screening and validation to delineate compartmentalised signalling events. Localised aPKC/exocyst/ERK activity is necessary for cytoskeletal controls and the polarized delivery and activation of translation machinery at the leading edge.

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Books on the topic "PKC"

1

Garay, Juan A., ed. Public-Key Cryptography – PKC 2021. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-75245-3.

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Garay, Juan A., ed. Public-Key Cryptography – PKC 2021. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-75248-4.

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Hanaoka, Goichiro, Junji Shikata, and Yohei Watanabe, eds. Public-Key Cryptography – PKC 2022. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-97121-2.

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Hanaoka, Goichiro, Junji Shikata, and Yohei Watanabe, eds. Public-Key Cryptography – PKC 2022. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-97131-1.

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Yung, Moti, Yevgeniy Dodis, Aggelos Kiayias, and Tal Malkin, eds. Public Key Cryptography - PKC 2006. Berlin, Heidelberg: Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/11745853.

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Nguyen, Phong Q., and David Pointcheval, eds. Public Key Cryptography – PKC 2010. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-13013-7.

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Okamoto, Tatsuaki, and Xiaoyun Wang, eds. Public Key Cryptography – PKC 2007. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71677-8.

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Jarecki, Stanisław, and Gene Tsudik, eds. Public Key Cryptography – PKC 2009. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-00468-1.

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Lin, Dongdai, and Kazue Sako, eds. Public-Key Cryptography – PKC 2019. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-17253-4.

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Lin, Dongdai, and Kazue Sako, eds. Public-Key Cryptography – PKC 2019. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-17259-6.

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Book chapters on the topic "PKC"

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Wang, Q. Jane. "PKC–PKD Interplay in Cancer." In Protein Kinase C in Cancer Signaling and Therapy, 287–303. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-543-9_14.

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Sun, Zuoming. "PKC-θ." In Encyclopedia of Medical Immunology, 854–58. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-0-387-84828-0_45.

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Wolf, Christopher, An Braeken, and Bart Preneel. "Efficient Cryptanalysis of RSE(2)PKC and RSSE(2)PKC." In Security in Communication Networks, 294–309. Berlin, Heidelberg: Springer Berlin Heidelberg, 2005. http://dx.doi.org/10.1007/978-3-540-30598-9_21.

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Kazanietz, Marcelo G. "Introduction: PKC and Cancer." In Protein Kinase C in Cancer Signaling and Therapy, 247–51. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-543-9_11.

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Merajver, Sofia D., Devin T. Rosenthal, and Lauren Van Wassenhove. "PKC and Breast Cancer." In Protein Kinase C in Cancer Signaling and Therapy, 347–60. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-543-9_17.

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Kim, Jeewon, and Marcelo G. Kazanietz. "PKC and Prostate Cancer." In Protein Kinase C in Cancer Signaling and Therapy, 361–78. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-543-9_18.

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McNaughton, Peter A. "TRPV1 Modulation by PKC." In Encyclopedia of Pain, 4102–4. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-28753-4_4645.

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Denning, Mitchell F. "PKC Isozymes and Skin Cancer." In Protein Kinase C in Cancer Signaling and Therapy, 323–45. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-543-9_16.

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Baier, G. "PKC Isotype Functions in T Lymphocytes." In Sparking Signals, 29–41. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/2789_2007_061.

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Basu, Alakananda. "PKC and Resistance to Chemotherapeutic Agents." In Protein Kinase C in Cancer Signaling and Therapy, 409–29. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-543-9_21.

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Conference papers on the topic "PKC"

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Kiviharju, Mikko. "Fuzzy pairings-based CL-PKC." In Proceedings of the First SAGA Conference. WORLD SCIENTIFIC, 2008. http://dx.doi.org/10.1142/9789812793430_0009.

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Nasako, Takeshi, Yasuyuki Murakami, and Masao Kasahara. "Security of Double-Sequence Knapsack PKC and Single-Sequence Knapsack PKC against Low-Density Attack." In 2009 Fourth International Conference on Computer Sciences and Convergence Information Technology. IEEE, 2009. http://dx.doi.org/10.1109/iccit.2009.283.

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Martin, DW, J. Mazer, EO Harrington, and G. Choudhary. "PKC Isoforms in Right Ventricular Hypertrophy." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a4145.

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Apostolatos, Andre H., Wishrawana S. Ratnayake, Tracess Smalley, Anisul Islam, and Mildred Acevedo-Duncan. "Abstract 2369: Transcription activators that regulate PKC-iota expression and are downstream targets of PKC-iota." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-2369.

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Hopple, Sara, Mark Bushfield, Fiona Murdoch, and D. Euan MacIntyre. "REGULATION OF PLATELET cAMP FORMATION BY PROTEIN KINASE C." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644512.

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Exogenous synthetic 1,2-diacylglycerols (e.g. 1,2-dioctanoylglycerol, DiC8) and 4β Phorbol esters (e.g. phorbol myristate acetate, PMA) routinely are used to probe the effects of protein Kinase C (PKC) on cellular responsiveness. Such agents act either independently or synergistically with elevated [Ca2+]i to induce platelet activation, but also inhibit agonist-induced inositol lipid metabolism and Ca2+ flux. These findings led to the concept that activated PKC can function as a bi-directional regulator of platelet reactivity. Therefore, DiCg and PMA were utilized to examine the effects of activated PKC on receptor-mediated stimulation and inhibition of adenylate cyclase, as monitored by cAMP accumulation. All studies were performed using intact human platelets in a modified Tyrodes solution, and cAMP was quantified by radioimmunoassay. Pretreatment (2 min.; 37°C) of platelets with PMA (≤ 300 nM) but not DiCg (200 μM) attenuated the elevation of platelet cAMP content evoked by PGD2 300 nM) but not by PGE1 (≤300 nM), PGI2 (≤100 nM) or adenosine (≤ 100 μM).These effects of PMA were unaffected by ADP scavengers, by Flurbiprofen (10 μM) or by cAMP phosphodiesterase inhibitors (IBMX, 1 mM) but were abolished by the PKC inhibitor Staurosporine (STP, 100 nM). In contrast, DiC8 (200 μM), but not PMA ( ≤ 300 nM), reduced the inhibitory effect of adrenaline (5 μM) on PGE1 (300 nM)-induced cAMP formation. This effect of DiCg was unaltered by STP (100 nM). Selective inhibition of PGD2-induced cAMP formation by PMA most probably can be attributed to PKC catalysed phosphorylation of the DP receptor. Reduction of the inhibitory effect of adrenaline by DiC8 could occur via an action at the α2 adrenoreceptor or Ni. These differential effects of PMA and DiC8 may result from differences in their distribution or efficacy, or to heterogeneity of platelet PKC.

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Nasako, Takeshi, Yasuyuki Murakami, and Masao Kasahara. "A Note on Security of KMN PKC." In 2008 Third International Conference on Convergence and Hybrid Information Technology (ICCIT). IEEE, 2008. http://dx.doi.org/10.1109/iccit.2008.96.

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Cayrel, Pierre-Louis, and Pierre Dusart. "McEliece/Niederreiter PKC: Sensitivity to Fault Injection." In 2010 5th International Conference on Future Information Technology. IEEE, 2010. http://dx.doi.org/10.1109/futuretech.2010.5482663.

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Zuxi, Wang, and Yu Baimu. "A Probabilistic Encryption Way in Knapsack PKC." In 1st International Workshop on Cloud Computing and Information Security. Paris, France: Atlantis Press, 2013. http://dx.doi.org/10.2991/ccis-13.2013.33.

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Douzono, Tatsuo, Takeshi Nasako, and Yasuyuki Murakami. "Effectiveness of plaintext encoding in knapsack PKC." In 2008 International Symposium on Information Theory and Its Applications (ISITA). IEEE, 2008. http://dx.doi.org/10.1109/isita.2008.4895588.

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Kong, Xianwen, and Cle´ment M. Gosselin. "Mobility Analysis of Parallel Mechanisms Based on Screw Theory and the Concept of Equivalent Serial Kinematic Chain." In ASME 2005 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. ASMEDC, 2005. http://dx.doi.org/10.1115/detc2005-85337.

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This paper presents a systematic approach for the mobility analysis of parallel mechanisms. The method is based on screw theory and the concept of equivalent serial chain. An equivalent serial kinematic chain of a k-legged PKC (parallel kinematic chain) is defined as a serial kinematic chain which has the same twist system and the wrench system as the k-legged PKC. Using the proposed approach, the mobility analysis of a PKC is performed in two steps. The first step is the instantaneous mobility analysis, and the second step is the full-cycle mobility inspection. The first step is dealt with based on screw theory. The second step is performed with the aid of the concept of equivalent serial chain and the types of multi-DOF overconstrained single-loop kinematic chains. The proposed approach is illustrated with several examples.

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Reports on the topic "PKC"

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Gutmann, P., and C. Bonnell. Standard Public Key Cryptography (PKC) Test Keys. RFC Editor, December 2023. http://dx.doi.org/10.17487/rfc9500.

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Balaji, Kethandapatti C. MT 2A Phosphorylation by PKC Mu/PKD Influences Chemosensitivity to Cisplatin in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, November 2008. http://dx.doi.org/10.21236/ada495664.

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Garg, Rachana. PKC Epsilon: A Novel Oncogenic Player in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, September 2014. http://dx.doi.org/10.21236/ada612051.

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Garg, Rachana. PKC Epsilon: A Novel Oncogenic Player in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, September 2013. http://dx.doi.org/10.21236/ada592838.

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Cho, Yunhi, and David Talmage. The Role of PKC in Retinoic Acid Regulation of Human Mammary Cancer Cell Proliferation. Fort Belvoir, VA: Defense Technical Information Center, September 1997. http://dx.doi.org/10.21236/ada338674.

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Cho, Yunhi, and David A. Talmage. The Role of PKC in Retinoic Acid Regulation of Human Mammary Cancer Cell Proliferation. Fort Belvoir, VA: Defense Technical Information Center, September 1998. http://dx.doi.org/10.21236/ada357326.

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Kazanietz, Marcelo G. Role of the Chemokine MCP-1 in Sensitization of PKC-Mediated Apoptosis in Prostate Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, February 2009. http://dx.doi.org/10.21236/ada500950.

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Kazanietz, Marcelo G. Role of the Chemokine MCP-1 in Sensitization of PKC-Medicated Apoptosis in Prostate Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, February 2008. http://dx.doi.org/10.21236/ada482340.

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Dickman, Martin B., and Oded Yarden. Role of Phosphorylation in Fungal Spore Germination. United States Department of Agriculture, August 1993. http://dx.doi.org/10.32747/1993.7568761.bard.

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Spore germination is a common and fundamental event in fungal development and in many instances an essential phase of fungal infection and dissemination. Spore germination is also critical for hyperparasites to function as biocontrol agents as well as in fermentation proceses. Our common objective is to understand the mechanisms which regulated spore germination and identify factors involved in pathogenicity related prepenetration development. Our approach is to exploit the overall similarity among filamentous fungi using both a plant pathogen (Colletotricum trifolii) and a model system that is genetically sophisticated (Neurospora crassa). The simulataneous use of two organisms has the advantage of the available tools in Neurospora to rapidly advance the functional analysis of genes involved in spore germination and development of an economically important fungal phytopathogen. Towards this we have isolated a protein kinase gene from C. trifolii (TB3) that is maximally expressed during the first hour of conidial germination and prior to any visible gene tube formation. Based on sequence similarities with other organisms, this gene is likely to be involved in the proliferative response in the fungus. In addition, TB3 was able to functionally complement a N. crassa mutant (COT-1). Pharmacological studies indicated the importance of calmodulin in both germination and appressorium differentiation. Using an antisense vector from N. crassa, direct inhibition of calmodulin results in prevention of differentiation as well as pathogenicity. Both cAMP dependent protein kinase (PKA) and protein kinase C (PKC) like genes have been cloned from C. trifolii. Biochemical inhibition of PKA prevents germination; biochemical inhibitors of PKC prevents appressorium differentiation. In order to analyze reversible phosphorylation as a regulatory mechanism, some ser.thr dephosphorylative events have also been analyzed. Type 2A and Type 2B (calcineurin) phosphatases have been identified and structurally and functionally analyzed in N. crassa during this project. Both phosphatases are essential for hyphal growth and maintenance of proper hyphal architecture. In addition, a first novel-type (PPT/PP5-like) ser/thr phosphatase has been identified in a filamentous fungus. The highly collaborative project has improved our understanding of a fundamental process in fungi, and has identified targets which can be used to develop new approaches for control of fungal plant pathogens as well as improve the performance of beneficial fungi in the field and in industry. In addition, the feasibility of molecular technology transfer in comparative mycology has been demonstrated.

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Lee, Yong J., S. S. Galoforo, and C. M. Berns. Differential effect of 1{alpha},25-dihydroxyvitamin D{sub 3} on Hsp28 and PKC{beta} gene expression in the phorbol ester-resistant human myeloid HL-525 leukemic cells. Office of Scientific and Technical Information (OSTI), August 1997. http://dx.doi.org/10.2172/522765.

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