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Academic literature on the topic 'PKCe'

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Published: 9 March 2023

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Journal articles on the topic "PKCe"

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Amiri, Farhad, and Raul Garcia. "Regulation of angiotensin II receptors and PKC isoforms by glucose in rat mesangial cells." American Journal of Physiology-Renal Physiology 276, no. 5 (May 1, 1999): F691—F699. http://dx.doi.org/10.1152/ajprenal.1999.276.5.f691.

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It has been shown that glomerular angiotensin II (ANG II) receptors are downregulated and protein kinase C (PKC) is activated under diabetic conditions. We, therefore, investigated ANG II receptor and PKC isoform regulation in glomerular mesangial cells (MCs) under normal and elevated glucose concentrations. MCs were isolated from collagenase-treated rat glomeruli and cultured in medium containing normal or high glucose concentrations (5.5 and 25.0 mM, respectively). Competitive binding experiments were performed using the ANG II antagonists losartan and PD-123319, and PKC analysis was conducted by Western blotting. Competitive binding studies showed that the AT1 receptor was the only ANG II receptor detected on MCs grown to either subconfluence or confluence under either glucose concentration. AT1 receptor density was significantly downregulated in cells grown to confluence in high-glucose medium. Furthermore, elevated glucose concentration enhanced the presence of all MC PKC isoforms. In addition, PKCβ, PKCγ and PKCε were translocated only in cells cultured in elevated glucose concentrations following 1-min stimulation by ANG II, whereas PKCα, PKCθ, and PKCλ were translocated by ANG II only in cells grown in normal glucose. Moreover, no changes in the translocation of PKCδ, PKCι, PKCζ, and PKCμ were detected in response to ANG II stimulation under euglycemic conditions. We conclude that MCs grown in high glucose concentration show altered ANG II receptor regulation as well as PKC isoform translocation compared with cells grown in normal glucose concentration.
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Dobkin-Bekman, Masha, Liat Rahamim Ben-Navi, Boris Shterntal, Ludmila Sviridonov, Fiorenza Przedecki, Michal Naidich-Exler, Chaya Brodie, Rony Seger, and Zvi Naor. "Differential Role of PKC Isoforms in GnRH and Phorbol 12-Myristate 13-Acetate Activation of Extracellular Signal-Regulated Kinase and Jun N-Terminal Kinase." Endocrinology 151, no. 10 (September 1, 2010): 4894–907. http://dx.doi.org/10.1210/en.2010-0114.

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GnRH is the first key hormone of reproduction. The role of protein kinase C (PKC) isoforms in GnRH-stimulated MAPK [ERK and Jun N-terminal kinase (JNK)] was examined in the αT3-1 and LβT2 gonadotrope cells. Incubation of the cells with GnRH resulted in a protracted activation of ERK1/2 and a slower and more transient activation of JNK1/2. Gonadotropes express conventional PKCα and conventional PKCβII, novel PKCδ, novel PKCε, and novel PKCθ, and atypical PKC-ι/λ. The use of green fluorescent protein-PKC constructs revealed that GnRH induced rapid translocation of PKCα and PKCβII to the plasma membrane, followed by their redistribution to the cytosol. PKCδ and PKCε localized to the cytoplasm and Golgi, followed by the rapid redistribution by GnRH of PKCδ to the perinuclear zone and of PKCε to the plasma membrane. Interestingly, PKCα, PKCβII, and PKCε translocation to the plasma membrane was more pronounced and more prolonged in phorbol-12-myristate-13-acetate (PMA) than in GnRH-treated cells. The use of selective inhibitors and dominant-negative plasmids for the various PKCs has revealed that PKCβII, PKCδ, and PKCε mediate ERK2 activation by GnRH, whereas PKCα, PKCβII, PKCδ, and PKCε mediate ERK2 activation by PMA. Also, PKCα, PKCβII, PKCδ, and PKCε are involved in GnRH and PMA stimulation of JNK1 in a cell-context-dependent manner. We present preliminary evidence that persistent vs. transient redistribution of selected PKCs or redistribution of a given PKC to the perinuclear zone vs. the plasma membrane may dictate its selective role in ERK or JNK activation. Thus, we have described the contribution of selective PKCs to ERK and JNK activation by GnRH.
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Collazos, Alejandra, Barthélémy Diouf, Nathalie C. Guérineau, Corinne Quittau-Prévostel, Marion Peter, Fanny Coudane, Frédéric Hollande, and Dominique Joubert. "A Spatiotemporally Coordinated Cascade of Protein Kinase C Activation Controls Isoform-Selective Translocation." Molecular and Cellular Biology 26, no. 6 (March 15, 2006): 2247–61. http://dx.doi.org/10.1128/mcb.26.6.2247-2261.2006.

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ABSTRACT In pituitary GH3B6 cells, signaling involving the protein kinase C (PKC) multigene family can self-organize into a spatiotemporally coordinated cascade of isoform activation. Indeed, thyrotropin-releasing hormone (TRH) receptor activation sequentially activated green fluorescent protein (GFP)-tagged or endogenous PKCβ1, PKCα, PKCε, and PKCδ, resulting in their accumulation at the entire plasma membrane (PKCβ and -δ) or selectively at the cell-cell contacts (PKCα and -ε). The duration of activation ranged from 20 s for PKCα to 20 min for PKCε. PKCα and -ε selective localization was lost in the presence of Gö6976, suggesting that accumulation at cell-cell contacts is dependent on the activity of a conventional PKC. Constitutively active, dominant-negative PKCs and small interfering RNAs showed that PKCα localization is controlled by PKCβ1 activity and is calcium independent, while PKCε localization is dependent on PKCα activity. PKCδ was independent of the cascade linking PKCβ1, -α, and -ε. Furthermore, PKCα, but not PKCε, is involved in the TRH-induced β-catenin relocation at cell-cell contacts, suggesting that PKCε is not the unique functional effector of the cascade. Thus, TRH receptor activation results in PKCβ1 activation, which in turn initiates a calcium-independent but PKCβ1 activity-dependent sequential translocation of PKCα and -ε. These results challenge the current understanding of PKC signaling and raise the question of a functional dependence between isoforms.
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Bhavanasi, Dheeraj, Soochong Kim, Lawrence E. Goldfinger, and Satya P. Kunapuli. "Protein Kinase C Delta Mediates the Activation of Protein Kinase D In Platelets." Blood 116, no. 21 (November 19, 2010): 2021. http://dx.doi.org/10.1182/blood.v116.21.2021.2021.

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Abstract Abstract 2021 Protein kinase D (PKD) is a subfamily of serine/threonine specific family of kinases, comprised of PKD1, PKD2 and PKD3 (PKCm, PKD2 and PKCn in humans). They are part of alternate DAG receptors along with RasGRPs, Munc 13s, chimerins and DAG kinases. Members of the novel class of PKC isoforms such as PKCd, PKCh, and PKCe associate with PKD in smooth muscle cells and COS-7 cells. The mechanism of activation of PKD and the specific PKC isoforms required for its activation are not known to date. This study is aimed at investigating the pathways involved in the activation of PKD in platelets. We show that human as well as murine platelets express PKD. PKD could be activated with PAR4 agonist AYPGKF, PAR1 agonist SFLLRN and GPVI agonist convulxin. AYPGKF and SFLLRN induced PKD phosphorylation as early as 30 sec and convulxin induced PKD phosphorylation at 1 minute. PKD phosphorylation induced by AYPGKF and convulxin were sustained for 5 minutes but phosphorylation induced by SFLLRN was attenuated after 2 minutes of stimulation. AYPGKF-induced PKD phosphorylation was reduced with a calcium chelator, dimethyl BAPTA, indicating that calcium-mediated signals might play a role in activation of PKD. PKD phosphorylation in response to AYPGKF was abolished with a Gq inhibitor, YM-254890, but was not affected by Gi-coupled P2Y12 receptor antagonist ARC-69931MX, indicating that PKD phosphorylation is Gq-, but not Gi- or G 12/13-dependent. PKD phosphorylation was abolished with pan-PKC inhibitors, GF109203X and Ro31-8220, indicating that PKCs are required for PKD activation in platelets. PKD phosphorylation was significantly inhibited with a PKC delta inhibitor, rottlerin, but was not affected by the classical PKC inhibitor, Go6976, suggesting that novel PKC isoforms are important for PKD activation. In addition, 2MeSADP that fails to activate PKCd did not induce phosphorylation of PKD in platelets. Furthermore, phosphorylation of PKD induced by AYPGKF was significantly reduced in PKCd-deficient platelets compared to that of wild type platelets. Hence, we conclude that PKD is a common signaling target downstream of various agonist receptors in platelets, and Gq-mediated signals and novel PKC isoforms, in particular PKCd is required for activation of PKD. Disclosures: No relevant conflicts of interest to declare.
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Chaudhary, Divya, Diane Boschelli, Andrea Bree, Agnes Brennan, Joan Chen, Bijia Deng, Lori Fitz, et al. "Characterization of a selective Protein Kinase C theta (PKCθ) inhibitor for blocking T Cell responses (93.21)." Journal of Immunology 182, no. 1_Supplement (April 1, 2009): 93.21. http://dx.doi.org/10.4049/jimmunol.182.supp.93.21.

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Abstract PKC theta (PKCθ) regulates T cell activation in lung inflammation and airway hyperresponsiveness, and in mouse models of multiple sclerosis, arthritis, and inflammatory bowel disease. We investigated inhibition of PKCθ enzyme activity by a small molecule as a strategy for modulating T cell mediated responses. Screening and lead optimization identified Compound A, a potent PKCθ inhibitor in both enzymatic and cell based assays, with low nM inhibitory activities. Compound A was highly selective (>1000 fold) over 50 kinases including representative serine/threonine, tyrosine, and phosphoinositol kinases, and the conventional and atypical PKCs, PKCβ and PKCξ. Compound A was 10 fold selective against PKCε, and 60 to 100 fold selectivity against PKCδand PKCη, respectively. We found that compound A strongly inhibited IL-2 production in antiCD3/anti-CD28 activated whole blood, using both human and mouse blood, with submicromolar potency. Based on these findings, we evaluated compound A- mediated inhibition of anti-CD3 induced IL-2 production in vivo. The results show a dose dependent inhibitory effect of compound A in this 4 hour cytokine production model. Additional cytokines inhibited by compound A in this model are IFNγ, IL-4, and TNF. IL-5 production was not reduced. We propose that compound A is a selective PKCθ inhibitor for further evaluating blockade of T cell responses in inflammation.
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Lee, Angel W. "Atypical Protein Kinase Cs Promote CSF-1-Dependent Erk Activation and Proliferation in Myeloid Cells." Blood 108, no. 11 (November 16, 2006): 4227. http://dx.doi.org/10.1182/blood.v108.11.4227.4227.

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Abstract Macrophages are integral components of the innate immune system and essential players in inflammation. Enhanced macrophage numbers underlie these pathological states. Colony stimulating factor-1 (CSF-1) is the major physiological regulator of proliferation and survival of cells of the monocyte/macrophage lineage. CSF-1 binds to a receptor tyrosine kinase, the CSF-1 receptor (CSF-1R). CSF-1 and CSF-1R have emerged as drug targets in several diseases where inflammation is a critical component, e.g. breast cancer and rheumatoid arthritis. Multiple pathways are activated downstream of the CSF-1R; however, it is not clear which of these pathways regulate proliferation and survival. Atypical PKCs (aPKCs) are implicated in cell proliferation and survival. They include the isoforms PKCζ and PKCλ/ι. Unlike the classical and novel PKCs, aPKCs are insensitive to Ca2+ and phorbol esters. In this study, we investigated the role of aPKCs in CSF-1-mediated proliferation in myeloid cells. CSF-1 is a proliferation and survival factor for 32D.R cells, a myeloid progenitor cell line transfected with the CSF-1R. Western blotting shows that PKCα, PKCδ, PKCε and PKCζ/λ/I are expressed in 32D.R. Based on studies with PKC inhibitors that have different specificities towards aPKCs (GF109203X, Ro-31-8220, Go6983 and a Myr-PKCζ peptide), maximal CSF-1-dependent proliferation in 32D.R cells appears to depend on the activity of either aPKCs or PKCε. Using phospho-specific antibodies that detect the activation state of PKCζ as well as in vitro kinase assays, we showed that CSF-1 activates aPKCs in 32D.R and bone marrow derived macrophages. In contrast, CSF-1-induced activation of PKCε was not observed. We next asked how aPKC affects CSF-1 signaling. PKCζ promotes activation of the MEK-Erk pathway in different cell types (Corbit, K.C. et al. Mol. Cell. Biol. 20, 5392). In 32D.R cells, treatment with the MEK inhibitor, U0126, reduced CSF-1-provoked proliferation by 60–70%, consistent with the inhibition observed with PKC inhibitors. Previous work from our lab showed that CSF-1 activates the Erk pathway through A-Raf and not Raf-1 (Lee and States, Mol. Cell. Biol. 18, 6779). We found that aPKC inhibitors do not affect CSF-1 induced Ras and A-Raf activity but markedly reduce MEK and Erk activity, implying that aPKC inputs into the CSF-1 Erk pathway at the level of MEK. Transient transfections with dominant-negative and constitutively active (CA) PKCζ confirmed that aPKC promotes CSF-1-induced Erk activation. aPKC inhibition does not affect CSF-1-stimulated Akt activation. To investigate the role of PKCζ in CSF-1-dependent proliferation, we established stable 32D.R mass populations overexpressing wildtype (WT) or CA PKCζ at levels 2-fold above endogenous. Comparing cells expressing CA-PKCζ to WT-PKCζ, the EC50 for CSF-1-dependent proliferation and the cell doubling time at maximal CSF-1 concentration were both reduced, consistent with a role for PKCζ in CSF-1 dependent proliferation. We will use our stable cell lines to elucidate the pathways modulated by PKCζ. Altogether, our results identify atypical PKCs as new targets of CSF-1 signaling.
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RENDÓN-HUERTA, Erika, Guillermo MENDOZA-HERNÁNDEZ, and Martha ROBLES-FLORES. "Characterization of calreticulin as a protein interacting with protein kinase C." Biochemical Journal 344, no. 2 (November 24, 1999): 469–75. http://dx.doi.org/10.1042/bj3440469.

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A protein kinase C (PKC)-binding protein was purified to homogeneity from the Triton-insoluble fraction from rat hepatocytes homogenates. The protein was identified as the mature calreticulin chain by N-terminal amino acid sequencing and by its immunoreactivity with anti-calreticulin antibody raised against the C-terminal KDEL (single-letter code) sequence. The calculated molecular mass was 46.6 kDa but the protein migrates in SDS/PAGE as a doublet with apparent molecular masses of 60 and 55 kDa. Studies in vitro with purified calreticulin with the use of an overlay assay approach demonstrated that it binds to activated PKC isoenzymes expressed in rat hepatocytes. Phosphorylation of purified calreticulin with a PKC isoenzyme-specific immune complex kinase assay showed that it is also a very good substrate for all PKC isoforms in vitro. The treatment of intact cells with phorbol ester or with adrenaline (epinephrine) plus propranolol increased calreticulin phosphorylation, which was blocked by the pretreatment of cells with the PKC-specific inhibitor Ro 31-8220. The analysis of calreticulin immunoprecipitates from control or treated cells indicated that PKCα, PKCβ, PKCθ, PKCζ and PKCμ, but not PKCδ or PKCϵ, co-immunoprecipitated with calreticulin. Taken together, our results indicate that PKC interacts in vivo with calreticulin and suggest that they can operate in common signalling pathways.
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WEBB, Benjamin L. J., Mark A. LINDSAY, Peter J. BARNES, and Mark A. GIEMBYCZ. "Protein kinase C isoenzymes in airway smooth muscle." Biochemical Journal 324, no. 1 (May 15, 1997): 167–75. http://dx.doi.org/10.1042/bj3240167.

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The protein kinase C (PKC) isoenzymes expressed by bovine tracheal smooth muscle (BTSM) were identified at the protein and mRNA levels. Western immunoblot analyses reliably identified PKCα, PKCβI and PKCβII. In some experiments immunoreactive bands corresponding to PKCδ, PKCϵ and PKCθ were also labelled, whereas the γ, η and ζ isoforms of PKC were never detected. Reverse transcriptase PCR of RNA extracted from BTSM using oligonucleotide primer pairs designed to recognize unique sequences in the PKC genes for which protein was absent or not reproducibly identified by immunoblotting, amplified cDNA fragments that corresponded to the predicted sizes of PKCδ, PKCϵ and PKCζ, which was confirmed by Southern blotting. Anion-exchange chromatography of the soluble fraction of BTSM following homogenization in Ca2+-free buffer resolved two major peaks of activity. Using ϵ-peptide as the substrate, the first peak of activity was dependent upon Ca2+ and 4β-PDBu (PDBu = phorbol 12,13-dibutyrate), and represented a mixture of PKCs α, βI and βII. In contrast, the second peak of activity, which eluted at much higher ionic strength, also appeared to comprise a combination of conventional PKCs that were arbitrarily denoted PKCα′, PKCβI′ and PKCβII′. However, these novel enzymes were cofactor-independent and did not bind [3H]PDBu, but were equally sensitive to the PKC inhibitor GF 109203X compared with bona fide conventional PKCs, and migrated on SDS/polyacrylamide gels as 81 kDa polypeptides. Taken together, these data suggest that PKCs α′, βI′ and βII′ represent modified, but not proteolysed, forms of their respective native enzymes that retain antibody immunoreactivity and sensitivity to PKC inhibitors, but have lost their sensitivity to Ca2+ and PDBu when ϵ-peptide is used as the substrate.
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Liu, Hong, and Fan Dong. "Involvement of PKCe in the Negative Regulation of Akt Activation Stimulated by G-CSF." Blood 104, no. 11 (November 16, 2004): 2187. http://dx.doi.org/10.1182/blood.v104.11.2187.2187.

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Abstract Granulocyte colony-stimulating factor (G-CSF) supports the proliferation, differentiation and survival of myeloid cells by stimulating the activation of several signaling cascades including the serine/threonine kinase Akt pathway. Akt activation has been shown to be important for G-CSF-induced survival and granulocytic differentiation. Although significant progresses have been made in our understanding of the molecular mechanisms by which Akt is activated, much less is known about the signaling events that negatively regulate Akt activation. Interestingly, G-CSF-induced activation of Akt was completely inhibited when myeloid 32D cells transfected with the wild type G-CSF receptor were incubated with phorbol-12-myristate 13-acetate (PMA), a PKC activator. PMA-mediated inhibition of Akt activation occurred with 5 min and lasted at least 1 hour. Previously, it has been shown that a carboxyl terminally truncated G-CSF receptor (D715), whose expression is associated with the development of acute myeloid leukemia in patients with severe congenital neutropenia (SCN), mediates significantly prolonged Akt activation. Notably, Akt activation by G-CSF in 32D cells expressing the D715 receptor mutant was rapidly downregulated by PMA treatment. The inhibitory effect of PMA on Akt activation was abolished by pretreatment of cells with the specific PKC inhibitor GF109203X, suggesting that PKC-dependent pathway negatively regulates Akt activation. Ro-31-7549, a specific inhibitor of PKCe, also abrogated PMA-mediated inhibition of Akt activation whereas rottlerin and Go6976, inhibitors of PKCd and PKC a/bI,, respectively, displayed no effect. Together, these results identified PKCe as being critically involved in PMA-mediated inhibition of Akt activation. Experiments are currently under way to determine the mechanism by which PKCe downregulates Akt activation and the role of PKCe in the regulation of cell proliferation, differentiation and survival in response to G-CSF.
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Bhavanasi, Dheeraj, Carol T. Dangelmaier, Jin Jianguo, Soochong Kim, and Satya P. Kunapuli. "Classical PKCs Regulate ADP-Induced Thromboxane Generation by Modulating Tyrosine Phosphorylation On Novel PKC Isoform Delta Through Shptp-1." Blood 120, no. 21 (November 16, 2012): 1064. http://dx.doi.org/10.1182/blood.v120.21.1064.1064.

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Abstract Abstract 1064 Introduction: Adenosine Di-phosphate (ADP) is stored in dense granules of platelets and is released upon platelet activation acting as a feedback activator by binding to G-protein coupled P2Y1 and P2Y12 receptors. ADP stimulation causes platelets to change shape, aggregate, release dense and a-granule contents and synthesize thromboxane A2 that can further act as a feedback activator potentiating platelet responses by binding to thromboxane receptor (TP). Protein kinase C is a serine threonine specific kinase that regulates multiple platelet functional responses. Specific PKC isoforms regulating platelet responses downstream of ADP receptors are not completely known. Aim: The aim of the current study is to elucidate the role of PKC isoforms in regulating ADP-induced platelet functional responses in platelets. Methods: We sought to delineate the mechanism of ADP-induced platelet responses by performing platelet aggregation (aggregometry), ATP secretion (luciferin-luciferase reaction) and thromboxane generation (ELISA kit measuring TxB2) in human or murine platelets by pre-incubating the platelets with control (DMSO) or inhibitors wherever mentioned. We also evaluated the role of PKCd to ADP-induced platelet responses by using murine platelets lacking PKCd. Background and Results: Murugappan et al have shown that PKCd was not activated downstream of ADP receptors based on the inability of ADP to cause threonine 507 phosphorylation on PKCd in platelets. However, studies from other labs have shown that PKCd can be activated when it is phosphorylated on its tyrosine residues. In the current study we show that, upon stimulation with 2MeSADP, PKCd is phosphorylated on tyrosine residue 311 in a time-dependent manner in platelets (Fig A). Also, ADP-induced thromboxane generation (Fig B) and ADP-induced thromboxane-mediated dense granule secretion were significantly inhibited in PKCd knockout murine platelets compared to those of wild type platelets. Similarly, thromboxane generation downstream of ADP receptors in human platelets pre-incubated with a PKCd inhibitor is significantly inhibited compared to control indicating a role for PKCd in mediating ADP-induced responses in platelets. Bynagari et al have shown that ADP-induced thromboxane generation is potentiated in the presence of the pan-PKC inhibitor, GF 109203X and the isoform regulating this effect is PKCe. We observed that pre-incubation of PKCe knockout murine platelets with GF 109203X further potentiated ADP-induced thromboxane generation suggesting that there are other PKC isoforms negatively regulating ADP-induced thromboxane generation. We show that this potentiating effect of thromboxane generation with GF 109203X in WT or PKCe KO murine platelets correlate with an increase in the phosphorylation of Y311 on PKCd (Fig C) suggesting that ADP-induced thromboxane generation is regulated through PKCd Y311 phosphorylation. Tyrosine phosphorylation on PKCd is mediated by Src family kinases (SFKs) as the phosphorylation is abolished with PP2, a SFK inhibitor and is only partially inhibited in Fyn knockout murine platelets suggesting that other SFKs also mediate this tyrosine phosphorylation. Surprisingly, pre-incubation of platelets with LY-333531, a classical PKC isoform (a/b) inhibitor potentiated PKCd Y311 phosphorylation (Fig D) as well as thromboxane generation (Fig E) downstream of ADP receptors suggesting a role for classical PKCs. Also, platelets pre-incubated with LY-333531 showed a decrease in the phosphorylation of SHPTP-1 (Fig F), a tyrosine phosphatase, rendering it active. The active SHPTP-1 phosphatase may dephosphorylate and activate SFKs, which can now phosphorylate PKCd on Y311 in platelets. Conclusions: In the current study, we report for the first time that the novel PKC isoform d is tyrosine phosphorylated downstream of ADP receptors through which it mediates ADP-induced thromboxane generation. We also show a novel role for classical PKC isoforms a/b in regulating tyrosine phosphorylation on novel isoform, PKCd possibly through the tyrosine phosphatase SHPTP-1 and Src family kinases in platelets. Disclosures: No relevant conflicts of interest to declare.
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Dissertations / Theses on the topic "PKCe"

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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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Queirolo, Valeria <1981&gt. "Caratterizzazione e ruolo di PKCε e PKCδ in modelli di differenziamento megacariocitario normale e patologico." Doctoral thesis, Alma Mater Studiorum - Università di Bologna, 2015. http://amsdottorato.unibo.it/6757/1/Queirolo_Valeria_tesi.pdf.

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La PKCε e la PKCδ, chinasi ubiquitariamente distribuite e ad azione pleiotropica, sono implicate del differenziamento, sopravvivenza e proliferazione cellulare. Esse sono coinvolte nel processo differenziativo delle cellule staminali ematopoietiche e in fenomeni patologici associati al compartimento sanguigno. In questa tesi sono presentati i risultati riguardanti lo studio in vitro del ruolo di PKCε e PKCδ nel contesto del differenziamento megacariocitario, in particolare si caratterizza l’espressione e la funzione di queste chinasi nel modello umano e nel modello murino di Megacariocitopoiesi, normale e patologica. Confrontando le cinetiche dei due modelli presi in analisi nello studio è stato possibile osservare come in entrambi PKCε e PKCδ dimostrino avere una chiara e specifica modulazione nel progredire del processo differenziativo. Questi dati, se confrontati, permettono di affermare che PKCε e PKCδ presentano un pattern di espressione opposto e, nel modello umano rispetto a quello murino, reciproco: nell’uomo i livelli di PKCε devono essere down-modulati, mentre nel topo, al contrario, i livelli della chinasi risultano up-modulati durante lo stesso processo. Analogamente, le CD34+ in differenziazione presentano una costante e maggiore espressione di PKCδ durante la maturazione MK, mentre nel modello murino tale proteina risulta down-modulata nella fase più tardiva di formazione della piastrina. Le chinasi mostrano in oltre di agire, nei due modelli, attraverso pathways distinti e cioè RhoA nel topo e Bcl-xL nell’uomo. È stato inoltre verificato che l’aberrante differenziamento MK osservato nella mielofibrosi primaria (PMF), è associato a difetti di espressione di PKCε e di Bcl-xL e che una forzata down-modulazione di PKCε porta ad un ripristino di un normale livello di espressione di Bcl-xL così come della popolazione di megacariociti formanti propiastrine. I dati ottenuti indicano quindi che PKCε e PKCδ svolgono un ruolo importante nel corretto differenziamento MK e che PKCε potrebbe essere un potenziale nuovo target terapeutico nelle PMF.
Protein kinases C (PKC) are known to be ubiquitously distributed and to have pleiotropic effects. Isoforms epsilon (PKCε) and delta (PKCδ) are involved in the regulation of cell growth, survival and differentiation; in particular, they have been also investigated for their role in the hematopoiesis and in aberrant processes of differentiation along the erythroid and megakaryocytic lineages. In this PhD thesis, the results of an in vitro study about the role of these two kinases in models of megakaryocytic (MK) differentiation, both normal and pathological, are presented. The observations about PKCε and PKCδ kinetics show how these proteins have a specific modulation during the MK differentiation that results in an opposite pattern of expression and, in the murine model if compared with the human model, also a reciprocal one. In particular, in human megakaryocytopoiesis, PKCε results down-modulated, whereas in mouse its levels increase. Instead, PKCδ shows a high and steady expression in maturing CD34+ MK committed, but it is strongly down-modulated during the latest phases of platelet maturation in the murine model. The study also elucidates the different pathways PKCε and PKCδ work through, being an inhibitory action of PKCε on RhoA during proplatelets (ppt) formation in the mouse model while, in the human MK differentiation, platelets production is regulated by PKCδ through Bcl-xL. In this dissertation it is also demonstrated how in an aberrant megakaryocytopoiesis, as in the pathologic model of primary myeloproliferative neoplasm (PMF), PKCε is strongly deregulated and it results in an altered Bcl-xL expression. A forced down-modulation of this kinase restores a normal MK differentiation and ppt maturation. Therefore, the data presented show that PKCε and PKCδ play a key role in proper megakaryocyte maturation and that PKCε could be a potential new therapeutic target for PMF.
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Queirolo, Valeria <1981&gt. "Caratterizzazione e ruolo di PKCε e PKCδ in modelli di differenziamento megacariocitario normale e patologico." Doctoral thesis, Alma Mater Studiorum - Università di Bologna, 2015. http://amsdottorato.unibo.it/6757/.

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La PKCε e la PKCδ, chinasi ubiquitariamente distribuite e ad azione pleiotropica, sono implicate del differenziamento, sopravvivenza e proliferazione cellulare. Esse sono coinvolte nel processo differenziativo delle cellule staminali ematopoietiche e in fenomeni patologici associati al compartimento sanguigno. In questa tesi sono presentati i risultati riguardanti lo studio in vitro del ruolo di PKCε e PKCδ nel contesto del differenziamento megacariocitario, in particolare si caratterizza l’espressione e la funzione di queste chinasi nel modello umano e nel modello murino di Megacariocitopoiesi, normale e patologica. Confrontando le cinetiche dei due modelli presi in analisi nello studio è stato possibile osservare come in entrambi PKCε e PKCδ dimostrino avere una chiara e specifica modulazione nel progredire del processo differenziativo. Questi dati, se confrontati, permettono di affermare che PKCε e PKCδ presentano un pattern di espressione opposto e, nel modello umano rispetto a quello murino, reciproco: nell’uomo i livelli di PKCε devono essere down-modulati, mentre nel topo, al contrario, i livelli della chinasi risultano up-modulati durante lo stesso processo. Analogamente, le CD34+ in differenziazione presentano una costante e maggiore espressione di PKCδ durante la maturazione MK, mentre nel modello murino tale proteina risulta down-modulata nella fase più tardiva di formazione della piastrina. Le chinasi mostrano in oltre di agire, nei due modelli, attraverso pathways distinti e cioè RhoA nel topo e Bcl-xL nell’uomo. È stato inoltre verificato che l’aberrante differenziamento MK osservato nella mielofibrosi primaria (PMF), è associato a difetti di espressione di PKCε e di Bcl-xL e che una forzata down-modulazione di PKCε porta ad un ripristino di un normale livello di espressione di Bcl-xL così come della popolazione di megacariociti formanti propiastrine. I dati ottenuti indicano quindi che PKCε e PKCδ svolgono un ruolo importante nel corretto differenziamento MK e che PKCε potrebbe essere un potenziale nuovo target terapeutico nelle PMF.
Protein kinases C (PKC) are known to be ubiquitously distributed and to have pleiotropic effects. Isoforms epsilon (PKCε) and delta (PKCδ) are involved in the regulation of cell growth, survival and differentiation; in particular, they have been also investigated for their role in the hematopoiesis and in aberrant processes of differentiation along the erythroid and megakaryocytic lineages. In this PhD thesis, the results of an in vitro study about the role of these two kinases in models of megakaryocytic (MK) differentiation, both normal and pathological, are presented. The observations about PKCε and PKCδ kinetics show how these proteins have a specific modulation during the MK differentiation that results in an opposite pattern of expression and, in the murine model if compared with the human model, also a reciprocal one. In particular, in human megakaryocytopoiesis, PKCε results down-modulated, whereas in mouse its levels increase. Instead, PKCδ shows a high and steady expression in maturing CD34+ MK committed, but it is strongly down-modulated during the latest phases of platelet maturation in the murine model. The study also elucidates the different pathways PKCε and PKCδ work through, being an inhibitory action of PKCε on RhoA during proplatelets (ppt) formation in the mouse model while, in the human MK differentiation, platelets production is regulated by PKCδ through Bcl-xL. In this dissertation it is also demonstrated how in an aberrant megakaryocytopoiesis, as in the pathologic model of primary myeloproliferative neoplasm (PMF), PKCε is strongly deregulated and it results in an altered Bcl-xL expression. A forced down-modulation of this kinase restores a normal MK differentiation and ppt maturation. Therefore, the data presented show that PKCε and PKCδ play a key role in proper megakaryocyte maturation and that PKCε could be a potential new therapeutic target for PMF.
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BONALUME, VERONICA. "GABAA RECEPTOR AS A NOVEL REGULATOR OF PERIPHERAL PAIN SENSITIVITY AND LOCAL NEURON-GLIA INTERACTION." Doctoral thesis, Università degli Studi di Milano, 2020. http://hdl.handle.net/2434/699522.

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The pathogenesis of neuropathic pain and its chronicization process are still not fully elucidated. For this reason, therapies currently ongoing in the clinic are aimed to treat mostly the symptoms, considering poorly the target mechanisms causing those pathologies. The approach that we choose to investigate new pharmacological targets for the therapy of chronic pain, was to firstly investigate the mechanisms of nociception in physiological condition, finding new molecular pathways responsible for nociception modulation. Secondly, we were aimed to study the contribution of these targets in the pathological condition. In particular, in this PhD thesis, I focused on the characterization of the GABAergic system, primarily the GABAA receptors (GABAAR), along peripheral nociceptors axons (forming C-fibers), evaluating their putative role in the modulation of pain peripheral conduction, during different physio-pathological conditions. GABAAR mediate fast synaptic inhibition in the dendrites, soma and axons of mature neurons that maintain low intracellular Cl- concentrations. In immature neurons as well as mature somatosensory neurons, the intracellular Cl- concentration is physiologically elevated and this gives rise to depolarizing GABAAR currents. We here report that, in somatosensory unmyelinated C-fibre axons, GABAAR mediates depolarizing currents and that the magnitude and time course of GABAAR responses are determined by NKCC1 activity. GABA (1 µM-1 mM) depolarizing responses were mediated specifically by axonal GABAAR, indeed they were mimicked by muscimol (>1 µM) and gaboxadol (THIP; >1 µM) and blocked by bicuculline (50 µM). Depolarizing axonal responses to GABA were completely absent in mice lacking β3 GABAAR subunit (β3,fl/fl), in either all sensory neurons (AdvillinCRE) or in nociceptor neurons expressing NaV1.8 (snsCRE). qRT-PCR analyses suggested that the most common GABAAR composition in somatosensory DRG neurons was a2, b3 and g2. To examine the physiological role of axonal GABAAR, C-fibres were subjected to a sustained frequency challenge (3 min at 2.5 Hz) and three main effects were found. First, the amplitude of axonal GABA responses was increased, and this effect was deemed secondary to an NKCC1 mediated shift in E Cl-. Second, GABAAR activation increased the axonal conduction velocity of C-fibres. Third, axonal GABAAR was activated by endogenous ligands. Our results indicate that C-fibres sustained firing increases NKCC1 activity, shifting ECl- toward more positive values. In this condition, constitutive GABAAR currents maintain nociceptor conductance during sustained firing. Established the capability of peripheral GABAergic currents to stabilize nociceptor conductance during sustained activity, we investigated the GABAergic modulation in pathological conditions characterized by hypersensitivity of nociceptors. In this regard, we studied in vivo model of inflammatory pain on snsCRE;b3-/- mice. The outcomes indicated that GABAAR activity increment mechanical allodynia and prevent the insurgence of hyperalgesia. In addition, GABAAR activity prolonged the recovery time, maintaining the hypersensitive phenotype for a longer period of time (up to 4 weeks). This finding corroborated the hypothesis that GABAergic transmission within peripheral fibers is able to stabilize the physiological conduction of pain, although it appeared dangerous in pathological condition, promoting nociceptor hypersensitivity and chronicization. We found that ALLO, a neuroactive steroid able to activate GABAAR and endogenously synthesized in PNS, induces the release of the growth factor BDNF from SCs, which is able to target trkB receptors on axons, in turn inducing PKCe upregulation and activation. PKCe is a typical protein kinase known to be involved in the process of pain chronicization. Overall, these set of data suggested that GABAAR is involved in a complex paracrine mechanism mediated by SCs, which activate the GABAAR and subsequently modulate its hyperactivity by the BDNF release. In conclusion, the results presented in this PhD thesis highlight the novel role of peripheral GABAAR in the modulation of nociceptor conduction in different physio-pathological conditions affecting the peripheral nervous system. Moreover, our findings stressed the role of local neuron-glia interaction in such mechanisms. GABAAR is able to dynamically stabilize nociceptor conduction of action potential during sustained activity, preventing excessive C-fiber slowing. On the other hand, GABAAR promotes pain hypersensitive state after neuronal inflammation and prolong the symptoms, likely leading to the pain chronicization. SCs play a fundamental role in the regulation of GABAergic signalling along C-fibers, although further studies are needed to unveil this process. in this direction might leads to the individuation of new pharmacological targets, exploiting endogenous pathways to obtain selective peripheral treatments. Hopefully, the complete comprehension of all the mechanisms would lay the basis for future identification of novel, possibly local, therapeutic strategies for the treatment of peripheral neuropathies and associated chronic pain.
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Le, Good Jessie Ann. "Regulation of atypical PKCs." Thesis, University College London (University of London), 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.313738.

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Kerai, Preeti. "Structural and functional characterisation of PKCI." Thesis, University College London (University of London), 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.325029.

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Crossland, V. M. "Cell cycle specific recruitment of PKCε." Thesis, University College London (University of London), 2012. http://discovery.ucl.ac.uk/1352790/.

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Protein kinase C (PKC) comprises a family of serine/threonine kinases which play central roles in intracellular signal transduction typically triggered by recruitment to membraneous compartments. The epsilon isoform of PKC (PKCå) has been shown to localize to cell-cell contacts and to the cytokinetic furrow/midbody, indicative of a role in the cell cycle. Both recruitment patterns can be visualized under conditions of PKCå inhibition, which is selectively achieved using a gatekeeper mutant (PKCå-M486A) and the inhibitor NaPP1. Initial studies indicated that interphase and mitotic cells were not distinguished in their capacity for PKCå-M486A recruitment as evidenced by optical trapping experiments. I therefore assessed whether recruitment to the furrow/midbody is a general property reflecting the juxtaposition of two membranes and a cell-cell contact response. I have successfully used fluorescence recovery after photobleaching (FRAP) to distinguish between the localization at the furrow/midbody from that at cell-cell contacts by measuring PKCå-M486A turnover at these two compartments. It is demonstrated that PKCå-M486A has a slower turnover at the furrow/midbody. The distinct kinetic behaviour of PKCå M486A at the furrow/midbody is indicative of other factors contributing to recruitment and/or retention. Sites and domains within PKCå-M486A were therefore assessed for their involvement in this process using a combination of mutagenesis and confocal microscopy. Through these studies I have identified a short motif in the regulatory domain of PKCå-M486A, the inter C1 domain (IC1D), that is in part required for the accumulation of PKCå-M486A at the furrow/midbody. The deletion of this domain (PKCå-ÄIC1D-M486A) prevents the kinase being recruited to the furrow/midbody despite, the recruitment and furrow/midbody localization of the co-expressed PKCå-M486A. Given that the IC1D was previously identified as an actin-binding region, I have assessed the relationship between actin and PKCå-M486A recruitment by manipulating actin polymerization. Using latrunculinA, an inhibitor of F-actin assembly, I have shown that PKCå-M86A and RhoA colocalize and are stabilized in the same compartment in conditions where F-actin is depolymerized. Importantly, the behaviour is observed for both active and inactive PKCε-M486A. This condition may be analogous to a stage in midbody biogenesis and may be evidence of the requirement of F-actin for normal PKCε and RhoA behaviour in cytokinesis. These data show some progress towards understanding the unique behaviour of PKCε at the furrow/midbody and indicate a complex relationship between PKCε, actin and RhoA.
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Pena, Darlene Aparecida. "Anticorpos conformacionais para PKCs clássicas e suas aplicações." Universidade de São Paulo, 2016. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-17082016-074719/.

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A família proteína quinases C (PKC) é composta por dez isoenzimas, as quais são capazes de fosforilar resíduos de serina e treonina. A ativação dessas quinases envolve mudanças conformacionais, como a remoção do pseudo-substrato do sítio ativo e associação dessas enzimas com lipídeos em membranas biológicas. Além disso, três fosforilações são importantes para a maturação/ enovelamento da enzima e não estão associadas com o estado de ativação das cPKCs. Apesar dessas quinases estarem envolvidas em vários processos patológicos, como carcinogênese e doenças cardiovasculares, ainda não se estabeleceu a relação entre estado de ativação das PKCs com essas doenças. Isso se deve, em parte, à ausência de ferramentas que possibilitam a distinção das formas ativas e inativas das PKCs. Na presente tese, baseando-se em mudanças conformacionais sofridas pelas PKCs durante o processo de ativação, dois anticorpos contra cPKCs ativas foram racionalmente desenvolvidos, sendo um anticorpo policlonal (anti-C2Cat) e outro monoclonal (4.8E). O anticorpo anti-C2Cat foi desenvolvido a partir de imunização de coelhos com um peptídeo localizado na região de interação entre os domínios C2 e catalítico na PKC inativa. Já o anticorpo monoclonal 4.8E foi produzido após a imunização de camundongos Balb/ C com extrato de proteínas proveniente de células HEK293T superexpressando formas constitutivamente ativas da PKCβI. A seletividade de anti-C2Cat e 4.8E por cPKCs ativas foi demonstrada por ensaios de ELISA e de imunoprecipitação, sendo que os anticorpos sempre apresentaram maior afinidade por cPKCs ativas purificadas, superexpressas ou mesmo as endógenas. O anticorpo anti-C2Cat foi capaz de monitorar a dinâmica espaço-temporal da ativação das cPKCs em linhagens de neuroblastoma (Neuro-2A e SK-N-SH) estimuladas com PMA, morfina, ATP ou glutamato por diferentes tempos. Ainda, um maior conteúdo de cPKCs ativas foi detectado por anti-C2Cat na linhagem de câncer de mama MDA-MB-231 (triplo- negativa) do que em células MCF-7 (ER+). Em acordo com esses dados, anti-C2Cat identificou uma maior ativação de cPKCs em tumores mais agressivos de câncer de mama (subtipo triplo-negativo) do que em tumores menos agressivos (ER+, subtipo luminal). Os anticorpos conformacionais anti-C2Cat e 4.8E foram aplicados para elucidar vias de sinalização que levam à carcinogênese em células MDA-MB-231, por meio da realização de ensaios de co-imunoprecipitação, seguida pela identificação das proteínas por espectrometria de massas. Usando essa abordagem, os resultados sugerem que as cPKCs ativas possam estar envolvidas com a tradução de proteínas envolvidas na migração celular, como actina. Em conjunto, os resultado obtidos na presente tese demonstram duas formas racionais de desenvolver anticorpos contra cPKCs ativas, sendo que algumas aplicações para estas ferramentas foram demonstradas. Estratégias baseadas em mudanças conformacionais, similares às apresentadas aqui, poderão ser utilizadas para a produção racional de anticorpos contra outras quinases ou proteínas
The protein kinase C family (PKC) is composed of ten isoenzymes, which are capable of phosphorylating serine and threonine amino acid residues. PKC activation involves conformational changes, such as removing the pseudo-substrate from the active site and binding of the enzyme to lipids in biological membranes. In addition, PKC undergoes three phosphorylations that are important for the maturation/ folding of the enzyme and are not linked with activation status. Despite the fact that these kinases are involved in various pathological processes, such as carcinogenesis and cardiovascular disease, a relationship between PKC activation status with these diseases has not yet been established. This is partly due to the lack of tools to detect active PKC in tissue samples. In this thesis, based on conformational changes suffered by PKC during its activation, two antibodies against active cPKCs were rationally developed; a polyclonal antibody (anti-C2Cat) and a monoclonal (4.8E). Anti-C2Cat was produced after immunization of rabbits with a peptide located at the interface between the C2 and catalytic domains of cPKCs in an inactive PKC. The monoclonal antibody 4.8E was produced after immunization of Balb/C mice with total lysates from HEK293T cells overexpressing constitutively active forms of PKCβI. The anti-C2Cat and 4.8E specificity by active cPKCs was demonstrated by ELISA and immunoprecipitation assays, where the antibodies always showed higher affinity to active cPKCs. Anti-C2Cat was able to detect the temporal and spatial dynamics of cPKC activation upon receptor (morphine, ATP or glutamate) or phorbol ester stimulation in neuroblastoma lines (Neuro-2A and SK-N-SH). Futhermore, anti-C2Cat is able to detect active PKC in human tissues. Higher levels of active cPKC were observed in the more aggressive triple negative breast cancer tumors as compared to the less aggressive estrogen receptor positive tumors. Also, both antibodies were applied to study signaling pathways that lead to carcinogenesis in MDA-MB-231 cells by performing co-immunoprecipitation and mass spectrometry. Using this approach, the results suggest that active cPKCs may be involved in translation of proteins involved in cell migration, such as actin. Taken together, the results obtained in this thesis showed two rational ways to develop antibodies against active cPKCs and some applications for these tools were demonstrated. Strategies based on conformational changes, similar to those presented herein may be used for rational production of antibodies against other kinases and proteins.
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McCarthy, Joy. "PKCε and cardioprotection : an exploration of putative mechanisms." Doctoral thesis, University of Cape Town, 2006. http://hdl.handle.net/11427/3429.

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Includes bibliographical references.
Recent studies have investigated the underlying regulatory mechanisms that may explain the cardioprotective role of PKCε. Sub-proteome analysis has identified interactions between activated PKCε and various mitochondrial proteins, which orchestrate mitochondrial homeostasis, including proteins governing mitochondrial oxidative phosphorylation, electron transfer, ion transport and control of mitochondrial permeability transition (MPT). MPT disruption is regarded as a key step in the initiation of an apoptotic cascade. However, brief pore opening may be beneficial in triggering the generation of small amounts of protective reactive oxygen species (ROS) and restoring calcium homeostasis. PKCε also interacts with adenine nucleotide translocases (ANTs), inner mitochondrial membrane proteins essential for ATP production and an integral component of the permeability transition pore. An augmented capacity to generate ATP would fundamentally enhance resilience to ischemia.
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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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Books on the topic "PKCe"

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Kozarova, Anna. Structure-function studies between the regulatory domain of human PKCa [alpha] and the PKCa [alpha] catalytic domain. Sudbury, Ont: Laurentian University, School of Graduate Studies, 2004.

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

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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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Book chapters on the topic "PKCe"

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Petiti, Juan Pablo, and Alicia Inés Torres. "Pituitary Tumor Cells: Role of PKCα, PKCδ and PKCε Expression." In Tumors of the Central Nervous System, Volume 10, 151–59. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-5681-6_17.

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Donato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, M. P. Suresh Jayasekara, Zhan-Guo Gao, Francesca Deflorian, John Papaconstantinou, et al. "PKD (isoforms: PKD1/PKCμ, PKD2, PKD3/PKCν)." In Encyclopedia of Signaling Molecules, 1434. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101053.

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Landrock, Peter, and Danny De Cock. "PKCS." In Encyclopedia of Cryptography and Security, 934–35. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4419-5906-5_298.

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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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Neagu, Monica, and Carolina Constantin. "Signal Transduction in Immune Cells and Protein Kinases." In Advances in Experimental Medicine and Biology, 133–49. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-49844-3_5.

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AbstractImmune response relies upon several intracellular signaling events. Among the protein kinases involved in these pathways, members of the protein kinase C (PKC) family are prominent molecules because they have the capacity to acutely and reversibly modulate effector protein functions, controlling both spatial distribution and dynamic properties of the signals. Different PKC isoforms are involved in distinct signaling pathways, with selective functions in a cell-specific manner.In innate system, Toll-like receptor signaling is the main molecular event triggering effector functions. Various isoforms of PKC can be common to different TLRs, while some of them are specific for a certain type of TLR. Protein kinases involvement in innate immune cells are presented within the chapter emphasizing their coordination in many aspects of immune cell function and, as important players in immune regulation.In adaptive immunity T-cell receptor and B-cell receptor signaling are the main intracellular pathways involved in seminal immune specific cellular events. Activation through TCR and BCR can have common intracellular pathways while others can be specific for the type of receptor involved or for the specific function triggered. Various PKC isoforms involvement in TCR and BCR Intracellular signaling will be presented as positive and negative regulators of the immune response events triggered in adaptive immunity.
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Arestis, Philip. "PKE Theoretical Framework." In Money, Pricing, Distribution and Economic Integration, 9–33. London: Palgrave Macmillan UK, 1997. http://dx.doi.org/10.1057/9780230374485_2.

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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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Conference papers on the topic "PKCe"

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Kong, Xianwen, and Cle´ment M. Gosselin. "Type Synthesis of 3-DOF PPR Parallel Manipulators Based on Screw Theory and the Concept of Virtual Chain." In ASME 2004 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. ASMEDC, 2004. http://dx.doi.org/10.1115/detc2004-57472.

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PPR-PMs (parallel manipulators) are the parallel counterparts of the 3-DOF PPR serial robots, which are composed of two P (prismatic) joints and one R (revolute) joint. For a PPR-PM, the moving platform can rotate arbitrarily about an axis undergoing a planar translation. This paper deals with the type synthesis of 3-DOF PPR-PMs. At first, virtual chains are introduced to represent the motion patterns of 3-DOF motions and relevant results from screw theory are recalled. A method is then proposed for the type synthesis of 3-DOF PPR-PMs. Using the proposed approach, the type synthesis of 3-DOF PPR-PMs is performed in three steps, namely, the type synthesis of legs for PPR-PKCs (parallel kinematic chains), the type synthesis of PPR-PKCs, and the selection of actuated joints of PPR-PMs. The three steps are dealt with in detail consequently. The characteristics of the proposed approach is that the type synthesis of legs for PPR-PKCs is reduced to the type synthesis of 3-DOF overconstrained single-loop kinematic chains and thus easy to perform. In addition to all the 3-DOF PPR-PKCs and 3-DOF PPR-PMs proposed in the literature, a number of new 3-DOF PPR-PKCs and 3-DOF PPR-PMs are identified. It is also found that there are no PPR-PMs with identical types of legs.
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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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Giri, Ritwik, Arvindh Krishnaswamy, and Karim Helwani. "Robust Non-negative Block Sparse Coding for Acoustic Novelty Detection." In 4th Workshop on Detection and Classification of Acoustic Scenes and Events (DCASE 2019). New York University, 2019. http://dx.doi.org/10.33682/pkcj-5s72.

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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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Abstract:
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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Berardi, Damian E., María Inés Díaz Bessone, Paola B. Campodónico, Andrea Motter, Elisa D. Bal de Kier Joffé, Alejandro J. Urtreger, and Laura B. Todaro. "Abstract 1199: Implications of protein kinase C (PKC)α and PKCΔ on murine mammary tumor growth and metastatic dissemination; effect of retinoids." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-1199.

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Mouri, Israt Jahan, Muhammad Ridowan, and Muhammad Abdullah Adnan. "RS-PKE." In CODASPY '22: Twelveth ACM Conference on Data and Application Security and Privacy. New York, NY, USA: ACM, 2022. http://dx.doi.org/10.1145/3508398.3511518.

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Delaune, Stéphanie, Steve Kremer, and Graham Steel. "Formal Analysis of PKCS#11." In 2008 21st IEEE Computer Security Foundations Symposium. IEEE, 2008. http://dx.doi.org/10.1109/csf.2008.16.

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Bortolozzo, Matteo, Matteo Centenaro, Riccardo Focardi, and Graham Steel. "Attacking and fixing PKCS#11 security tokens." In the 17th ACM conference. New York, New York, USA: ACM Press, 2010. http://dx.doi.org/10.1145/1866307.1866337.

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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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Li, Zhi-Chun, and Chunxiao Zhang. "Digital Rights Management System Based on PKCS#12." In 2013 Ninth International Conference on Intelligent Information Hiding and Multimedia Signal Processing (IIH-MSP). IEEE, 2013. http://dx.doi.org/10.1109/iih-msp.2013.163.

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Reports on the topic "PKCe"

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Pechanec, J., and D. Moffat. The PKCS #11 URI Scheme. RFC Editor, April 2015. http://dx.doi.org/10.17487/rfc7512.

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Kaliski, B. PKCS #1: RSA Encryption Version 1.5. RFC Editor, March 1998. http://dx.doi.org/10.17487/rfc2313.

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Leonard, S. The PKCS #8 EncryptedPrivateKeyInfo Media Type. RFC Editor, June 2018. http://dx.doi.org/10.17487/rfc8351.

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Mavrogiannopoulos, N. Storing Validation Parameters in PKCS#8. RFC Editor, September 2018. http://dx.doi.org/10.17487/rfc8479.

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Kaliski, B. PKCS #10: Certification Request Syntax Version 1.5. RFC Editor, March 1998. http://dx.doi.org/10.17487/rfc2314.

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Kaliski, B. PKCS #7: Cryptographic Message Syntax Version 1.5. RFC Editor, March 1998. http://dx.doi.org/10.17487/rfc2315.

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Kaliski, B., and J. Staddon. PKCS #1: RSA Cryptography Specifications Version 2.0. RFC Editor, October 1998. http://dx.doi.org/10.17487/rfc2437.

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Nystrom, M., S. Parkinson, A. Rusch, and M. Scott. PKCS #12: Personal Information Exchange Syntax v1.1. Edited by K. Moriarty. RFC Editor, July 2014. http://dx.doi.org/10.17487/rfc7292.

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Kaliski, B., J. Jonsson, and A. Rusch. PKCS #1: RSA Cryptography Specifications Version 2.2. Edited by K. Moriarty. RFC Editor, November 2016. http://dx.doi.org/10.17487/rfc8017.

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Kaliski, B. PKCS #5: Password-Based Cryptography Specification Version 2.0. RFC Editor, September 2000. http://dx.doi.org/10.17487/rfc2898.

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