Relevant bibliographies by topics / PKC activator

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'PKC activator'

Author: Grafiati
Published: 4 June 2021
Last updated: 13 February 2022

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Journal articles on the topic "PKC activator"

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Blount, Mitsi A., Penelope Cipriani, Sara K. Redd та ін. "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, № 9 (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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Rashid, Gloria, Eleanora Plotkin, Osnat Klein, Janice Green, Jacques Bernheim, and Sydney Benchetrit. "Parathyroid hormone decreases endothelial osteoprotegerin secretion: role of protein kinase A and C." American Journal of Physiology-Renal Physiology 296, no. 1 (2009): F60—F66. http://dx.doi.org/10.1152/ajprenal.00622.2007.

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Parathyroid hormone (PTH), which is elevated in patients with chronic renal failure, has been shown to participate in the development of vascular calcification. Previous studies have demonstrated that PTH may promote endothelial expressions of proinflammatory parameters. On the basis of these data, we evaluated whether PTH may have an impact on endothelial osteoprotegerin (OPG), a vascular-protective factor which may control vascular calcification. Endothelial cells were stimulated with 10−12 to 10−10 mol/l PTH. PKC and PKA are the main cellular pathways of PTH. Inhibitors and activators of PKC or PKA were used to determine whether these signaling pathways are involved in the control of endothelial OPG. PTH induced a decrease in OPG secretion and mRNA expression. Treatment of PTH-stimulated cells by calphostin C (PKC inhibitor) induced a further decrease in OPG secretion, while Rp-cAMP (PKA inhibitor) had no additional effect. In nonstimulated cells, a PKC activator significantly stimulated OPG secretion, while a PKA activator was associated with a decline. These effects were blunted in the presence of calphostin C and Rp-cAMP, respectively. An increase in OPG secretion induced by a PKC activator indicates that the basal OPG secretion is mediated through PKC. The decrease induced by a PKA activator, which is similar to the decrease observed with PTH, suggests that the action of PTH on OPG secretion and mRNA expression may be due to the PKA pathway.
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VAN DIJK, Marc C. M., Henk HILKMANN та Wim J. VAN BLITTERSWIJK. "Platelet-derived growth factor activation of mitogen-activated protein kinase depends on the sequential activation of phosphatidylcholine-specific phospholipase C, protein kinase C-ζ and Raf-1". Biochemical Journal 325, № 2 (1997): 303–7. http://dx.doi.org/10.1042/bj3250303.

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The mechanism of Raf-1 activation by platelet-derived growth factor (PDGF) is poorly defined. We previously reported that, in Rat-1 fibroblasts, PDGF activates a phosphatidylcholine-specific phospholipase C (PC-PLC) and that the product, diacylglycerol, somehow activates protein kinase C-ζ (PKC-ζ). Both PC-PLC and PKC-ζ activities were required for PDGF activation of mitogen-activated protein kinase (MAPK). Now we report that MAPK activation by exogenous PC-PLC depends on Raf-1 activation. PKC-ζ co-immunoprecipitates with, phoshorylates and activates Raf-1, suggesting that in the PDGF- and PC-PLC-activated MAPK pathway, PKC-ζ operates in a signalling complex as a direct activator of Raf-1.
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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 (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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Cai, H., U. Smola, V. Wixler, et al. "Role of diacylglycerol-regulated protein kinase C isotypes in growth factor activation of the Raf-1 protein kinase." Molecular and Cellular Biology 17, no. 2 (1997): 732–41. http://dx.doi.org/10.1128/mcb.17.2.732.

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The Raf protein kinases function downstream of Ras guanine nucleotide-binding proteins to transduce intracellular signals from growth factor receptors. Interaction with Ras recruits Raf to the plasma membrane, but the subsequent mechanism of Raf activation has not been established. Previous studies implicated hydrolysis of phosphatidylcholine (PC) in Raf activation; therefore, we investigated the role of the epsilon isotype of protein kinase C (PKC), which is stimulated by PC-derived diacylglycerol, as a Raf activator. A dominant negative mutant of PKC epsilon inhibited both proliferation of NIH 3T3 cells and activation of Raf in COS cells. Conversely, overexpression of active PKC epsilon stimulated Raf kinase activity in COS cells and overcame the inhibitory effects of dominant negative Ras in NIH 3T3 cells. PKC epsilon also stimulated Raf kinase in baculovirus-infected Spodoptera frugiperda Sf9 cells and was able to directly activate Raf in vitro. Consistent with its previously reported activity as a Raf activator in vitro, PKC alpha functioned similarly to PKC epsilon in both NIH 3T3 and COS cell assays. In addition, constitutively active mutants of both PKC alpha and PKC epsilon overcame the inhibitory effects of dominant negative mutants of the other PKC isotype, indicating that these diacylglycerol-regulated PKCs function as redundant activators of Raf-1 in vivo.
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Limatola, C., D. Schaap, W. H. Moolenaar та W. J. van Blitterswijk. "Phosphatidic acid activation of protein kinase C-ζ overexpressed in COS cells: comparison with other protein kinase C isotypes and other acidic lipids". Biochemical Journal 304, № 3 (1994): 1001–8. http://dx.doi.org/10.1042/bj3041001.

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Phosphatidic acid (PA) is produced rapidly in agonist-stimulated cells, but the physiological function of this PA is unknown. We have examined the effects of PA on distinct isoforms of protein kinase C (PKC) using a new cell-free assay system. Addition of PA to cytosol from COS cells overexpressing PKC-alpha, -epsilon or -zeta differentially-activated all three isotypes, as shown by PKC autophosphorylation, and prominent phosphorylation of multiple endogenous substrates. In the absence of Ca2+, the diacylglycerol-insensitive zeta-isotype of PKC was most strongly activated by both PA and bisPA, a newly identified product of activated phospholipase D, with each lipid inducing its own profile of protein phosphorylation. BisPA was also a strong activator of PKC-epsilon, but a weak activator of PKC-alpha. Ca2+, at > or = 0.1 microM, inhibited PA and bisPA activation of PKC-zeta, but did not affect PKC-epsilon activation. In contrast, PKC-alpha was strongly activated by PA only in the presence of Ca2+. BisPA-induced phosphorylations mediated by PKC-zeta could be mimicked in part by other acidic phospholipids and unsaturated fatty acids. PA activation of PKC-zeta was unique in that PA not only stimulated PKC-zeta-mediated phosphorylation of distinctive substrates, but also caused an upward shift in electrophoretic mobility of PKC-zeta, which was not observed with other acidic lipids or with PKC-alpha or -epsilon. We have presented evidence that this mobility shift is not caused by PKC-zeta autophosphorylation, but it coincides with physical binding of PA to PKC-zeta. These results suggest that in cells stimulated under conditions where intracellular Ca2+ is at (or has returned to) basal level, PA may be a physiological activator of PKC-zeta.
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Golard, A., L. W. Role, and S. A. Siegelbaum. "Protein kinase C blocks somatostatin-induced modulation of calcium current in chick sympathetic neurons." Journal of Neurophysiology 70, no. 4 (1993): 1639–43. http://dx.doi.org/10.1152/jn.1993.70.4.1639.

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1. Somatostatin produces a voltage-dependent inhibition of N-type Ca2+ current in chick sympathetic neurons. Pretreatment of chick sympathetic ganglion neurons with protein kinase C (PKC) activators has no effect on calcium current (ICa) but reduces the inhibition of ICa by somatostatin. 2. The effects of the alkaloid PKC activator (-)-indolactam V were indistinguishable from those of 4 beta-phorbol-12-myristate-13-acetate (4 beta-PMA). The inactive isomers (+)-indolactam V and 4 alpha-PMA did not alter the modulation of ICa by somatostatin. 3. Modulation of ICa by somatostatin desensitizes, with a time for half desensitization of approximately 3 min. PKC activation mimics the normal desensitization process in that responses to 30 nM somatostatin are inhibited to a greater extent than are responses to 1 microM somatostatin. 4. PKC appears to act at the level of the somatostatin receptor or receptor-G protein interaction because PKC activation does not alter Ca2+ current inhibition in response to a nonhydrolyzable analog of GTP, GTP-gamma-S, which directly activates G proteins. 5. The specific PKC inhibitor calphostin C largely reverses the effects of phorbol esters, but does not slow the normal rate of desensitization of somatostatin responses. This indicates that PKC is not involved in the homologous desensitization of the somatostatin receptor. 6. Neither substance P, which activates PKC in these cells, nor arachidonic acid, another PKC activator, altered the action of somatostatin on ICa.
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Matsumoto, Shigeji, Shinki Yoshida, Mizuho Ikeda, Chikako Saiki, and Mamoru Takeda. "Effects of PKC and PKA Inhibitors on the cAMP-Stimulant-Induced Enhancement of Tetrodotoxin-Resistant Na+ (Nav1.8) Currents." Open Pharmacology Journal 2, no. 1 (2008): 17–19. http://dx.doi.org/10.2174/1874143600802010017.

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The protein kinase C (PKC) inhibitor bisindolymaleimide Ro-31-8425 (Ro-31-8425) decreases the peak tetrodotoxin- resistant (TTX-R) Na+ (Nav1.8) current in nodose ganglion (NG) neurons, and this decrease is not altered by simultaneous application of 8-bromo-cAMP (8-Br-cAMP), phorbol 12-myristate 13-acetate (PMA, a PKC activator) or forskolin (a cAMP analogue). Intracellular application of the endogenous protein kinase A (PKA) inhibitor, protein kinase inhibitor (PKI) abolishes the increase in the peak Nav1.8 current that occurs in response to the applications of 8-BrcAMP, PMA, forskolin, or prostaglandin E2 (PGE2, an adenyl cyclase activator). At a higher concentration (0.5 mM) compared with a sufficient concentration (0.01 mM) to block the cAMP-stimulant Nav1.8 current, PKI still attenuated the Ro-31-8425-induced decrease in peak Nav1.8 current. When we considered these results together, cAMP-stimulantinduced modification of Nav1.8 currents is mediated by the activation of both PKA and PKC, and PKC may be located upstream of PKA.
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Barman, Scott A., Shu Zhu, and Richard E. White. "Protein kinase C inhibits BKCa channel activity in pulmonary arterial smooth muscle." American Journal of Physiology-Lung Cellular and Molecular Physiology 286, no. 1 (2004): L149—L155. http://dx.doi.org/10.1152/ajplung.00207.2003.

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Signaling mechanisms that elevate cyclic AMP (cAMP) activate large-conductance, calcium- and voltage-activated potassium (BKCa) channels in pulmonary vascular smooth muscle and cause pulmonary vasodilatation. BKCa channel modulation is important in the regulation of pulmonary arterial pressure, and inhibition (closing) of the BKCa channel has been implicated in the development of pulmonary vasoconstriction. Protein kinase C (PKC) causes pulmonary vasoconstriction, but little is known about the effect of PKC on BKCa channel activity. Accordingly, studies were done to determine the effect of PKC activation on cAMP-induced BKCa channel activity using patch-clamp studies in pulmonary arterial smooth muscle cells (PASMC) of the fawn-hooded rat (FHR), a recognized animal model of pulmonary hypertension. Forskolin (10 μM), a stimulator of adenylate cyclase and an activator of cAMP, opened BKCa channels in single FHR PASMC, which were blocked by the PKC activators phorbol 12-myristate 13-acetate (100 nM) and thymeleatoxin (100 nM). The inhibitory response by thymeleatoxin on forskolin-induced BKCa channel activity was blocked by Gö-6983, which selectively blocks the α, β, δ, γ, and ζ PKC isozymes, and Gö-6976, which selectively inhibits PKC-α, PKC-β, and PKC-μ, but not by rottlerin, which selectively inhibits PKC-δ. Collectively, these results indicate that activation of specific PKC isozymes inhibits cAMP-induced activation of the BKCa channel in pulmonary arterial smooth muscle, which suggests a unique signaling pathway to modulate BKCa channels and subsequently cAMP-induced pulmonary vasodilatation.
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Ren, Chongyu, Jin Zhang, Kenneth D. Philipson, Michael I. Kotlikoff, Mordecai P. Blaustein, and Donald R. Matteson. "Activation of L-type Ca2+ channels by protein kinase C is reduced in smooth muscle-specific Na+/Ca2+ exchanger knockout mice." American Journal of Physiology-Heart and Circulatory Physiology 298, no. 5 (2010): H1484—H1491. http://dx.doi.org/10.1152/ajpheart.00965.2009.

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L-type voltage-gated Ca2+ channels (LVGCs) are functionally downregulated in arterial smooth muscle (SM) cells (ASMCs) of mice with SM-specific knockout of Na+/Ca2+ exchanger type-1 (NCX1SM−/−) ( 32 ). Here, using activators and inhibitors of protein kinase C (PKC), we explore the regulation of these channels by a PKC-dependent mechanism. In both wild-type (WT) and NCX1SM−/− myocytes, the PKC activator phorbol 12,13-dibutyrate (PDBu) increases LVGC conductance, decreases channel closing rate, and shifts the voltage dependence of channel opening to more negative potentials. Three different PKC inhibitors, bisindolylmaleimide, Ro-31-8220, and PKC 19-31, all decrease LVGC currents in WT myocytes and prevent the PDBu-induced increase in LVGC current. Dialysis of WT ASMCs with activated PKC increases LVGC current and decreases channel closing rate. These results demonstrate that PKC activates LVGCs in ASMCs. The phosphatase inhibitor calyculin A increases LVGC conductance by over 50%, indicating that the level of LVGC activation is a balance between phosphatase and PKC activities. PDBu causes a larger increase in LVGC conductance and a larger shift in voltage dependence in NCX1SM−/− myocytes than in WT myocytes. The inhibition of PKC with PKC 19-31 decreased LVGC conductance by 65% in WT myocytes but by only 37% in NCX1SM−/− myocytes. These results suggest that LVGCs are in a state of low PKC-induced phosphorylation in NCX1SM−/− myocytes. We conclude that in NCX1SM−/− myocytes, reduced Ca2+ entry via NCX1 lowers cytosolic [Ca2+], thereby reducing PKC activation that lowers LVGC activation.
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Dissertations / Theses on the topic "PKC activator"

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Douceau, Sara. "Implication du tPA cérébral dans la régulation des comportements et le remodelage des perineuronal nets Tissue-type plasminogen activator expressed in PKC-δ positive GABAergic neurons within the central amygdala modulates motor and emotional responses tPA originating from parvalbumin interneurons controls the remodeling of perineuronal nets". Thesis, Normandie, 2020. http://www.theses.fr/2020NORMC423.

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L’activateur tissulaire du plasminogène (tPA) est une sérine protéase initialement décrite dans le compartiment vasculaire pour son rôle dans les processus de fibrinolyse. Le tPA est également retrouvé dans le parenchyme cérébral où il est exprimé par différents types cellulaires et notamment par les neurones. Cette protéase est impliquée dans de nombreuses fonctions cérébrales telles que la plasticité synaptique, la modulation de la neurotransmission glutamatergique et régule également les processus cognitifs et émotionnels. L’implication du tPA dans ces différentes fonctions est dépendante de sa capacité à convertir le plasminogène en plasmine ou à interagir avec différents récepteurs. L’étude des fonctions du tPA a été essentiellement réalisée dans des modèles d’invalidation constitutive du gène codant le tPA (Plat) et ne permettent pas de rendre compte de son expression au sein de différents types cellulaires et régions cérébrales.Lors d’une première étude nous avons utilisé une souris transgénique, tPA Flox permettant la délétion conditionnelle du tPA dans les régions cérébrales, grâce au système Cre-lox, ainsi qu’une souris tPA Null, déficiente en tPA de manière constitutive. Chez les souris tPA Null, nous avons mis en évidence une diminution de l’anxiété-trait, une hyperactivité locomotrice ainsi que des déficits de la mémoire spatiale. De manière intéressante la délétion conditionnelle du tPA dans le gyrus denté de l’hippocampe a révélé une augmentation de l’activité locomotrice chez les souris tPA Flox. Parallèlement nous avons montré que la délétion du tPA dans le noyau central de l’amygdale augmente l’activité locomotrice et diminue l’anxiété des animaux. Nous avons également montré que le tPA est exprimé dans les interneurones PKCδ dans l’amygdale centrale.La seconde partie de ces travaux visait à étudier l’implication du système tPA/plasmine dans le remodelage des réseaux périneuronaux (PNNs), une structure spécifique de la matrice extracellulaire entourant les interneurones à parvalbumine (PV). L’utilisation d’un outil rapporteur de l’activité du gène Plat couplée à des analyses électrophysiologiques et par single-cell RT-PCR nous a permis de mettre en évidence l’expression du tPA par les interneurones PV. Nous montrons que la délétion conditionnelle du tPA dans les interneurones PV augmente la densité des PNNs, suggérant un rôle de cette protéase dans leurs modulations. In vitro, nous mettons en évidence que le tPA influence le remodelage des PNNs par un mécanisme dépendant de l’activation du plasminogène en plasmine, elle-même responsable du clivage de l’aggrécan, un composant majeur de ces structures.Ces résultats sont novateurs et permettent une meilleure compréhension du rôle du tPA et de la plasmine dans les réponses comportementales et dans le remodelage de la matrice extracellulaire<br>Tissue-type plasminogen activator is a serine protease, initially describe in the vascular compartment for its role in fibrinolysis processes. tPA is also found in the cerebral parenchyma where it is expressed by different cell types, being notably expressed by neurons. This protease displays different roles including synaptic plasticity, modulation of glutamatergic neurotransmission and also regulates cognitive and emotional processes. tPA’s involvement in these different functions depends on its ability to convert plasminogen into plasmin or to interact with different receptors. The study of tPA’s functions has been mainly performed in models constitutively deficient for tPA gene (Plat) and does not allow to account for its expression within different cell types and brain regions.In a first study we used a transgenic mouse, tPA Flox, which allows the conditional deletion of tPA in brain regions, thanks to the Cre-lox system, as well as a tPA Null mouse, constitutively deficient in tPA. In tPA Null mice, we have demonstrated a decreased anxiety, a locomotor hyperactivity and spatial memory deficits. Interestingly, the conditional deletion of tPA in the dentate gyrus of the hippocampus revealed an increase in locomotor activity in tPA Flox mice. At the same time we showed that tPA deletion in the central nucleus of the amygdala increases locomotor activity and decreases anxiety of mice. We also showed that tPA is expressed in PKCδ-positive interneurons in the central amygdala.The second part of my work aimed at studying the involvement of the tPA/plasmin system in the remodeling of perineuronal nets (PNNs), a specific structure of the extracellular matrix surrounding parvalbumin (PV) interneurons. Using a reporter construct of the Plat gene activity coupled with electrophysiological and single-cell RT-PCR analyses, we were able to highlight the expression of tPA by PV interneurons. We show that the conditional deletion of tPA in PV interneurons increases the density of PNNs, suggesting a role of this protease in their modulations. In vitro, we show that tPA influences the remodeling of PNNs by a mechanism dependent of the activation of plasminogen into plasmin, which is responsible for the cleavage of aggrecan, a major component of these structures.These results are novel and allow a better understanding of the role of tPA and plasmin in behavioral responses and extracellular matrix remodeling
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Ettinger, Susan Lorraine. "Cytokine-induced activation of PKC isoenzymes in hemopoietic cells." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp03/NQ27139.pdf.

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Cozzi, Sarah-Jane. "Molecular targets of anticancer PKC activators in the treatment of melanoma /." [St. Lucia, Qld.], 2005. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe19185.pdf.

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Rourke, Bryan. "Characterization of the activation of PKC Apl II in Aplysia californica." Thesis, McGill University, 2014. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=121492.

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PKC Apl II, a novel PKC in Aplysia californica, is required for reversal of depression, the cellular analog of behavioral dishabituation. The neurotransmitter 5HT activates PKC Apl II in sensory neurons and can induce the reversal of depression. Here we investigated the ability of 5HT to activate PKC Apl II and the molecular pathway involved. Reversal of depression can occur at concentrations as low as 1.6 μM. We observed that activation of PKC Apl II, as measured by membrane enrichment, can occur at similar concentrations (1 μM). Furthermore we observed differences in membrane enrichment in the processes compared to the cell bodies when sensory neurons had formed a synapse with a motor neuron but not in isolated sensory neurons. The receptor activated by 5HT upstream of PKC Apl II is currently unknown. We tested the ability of the Aplysia 5HT4Apl, B2 and B4 receptors to measure the activation of PKC Apl II in a heterologous cell system. The B receptors are unique to Aplysia and are related to the biogenic amine receptors. Neither receptor was able to activate PKC Apl II as measured by translocation. The ligand or purpose of the Aplysia B receptors remains unclear. Despite not being present in sensory neurons 5HT4Apl was able to activate PKC Apl II. Previous work has shown that genistein blocks PKC Apl II activation and reversal of depression. However was not clear which target of genistein was responsible. Using pharmacological inhibitors we confirm that genistein as acting on a tyrosine kinase. Furthermore we provided evidence that the receptor tyrosine kinase FGFR is involved in PKC Apl II activation. This suggests that the 5HT receptor responsible for PKC Apl II activation transactivates FGFR in Aplysia sensory neurons.<br>Chez l'Aplysie de californie, la nouvelle PKC Apl II est importante pour inverser la dépression synaptique qui est sous-jacente à la déshabituation chez l'animal. Nos études précédentes avaient démontré que la sérotonine (5HT) activait la PKC Apl II dans les neurones sensoriels. De plus, des concentrations de 5HT aussi faibles que 1 μM pouvaient inverser la dépression synaptique. Dans la présente thèse, nous avons investigué la translocation de la PKC Apl II en réponse à la 5HT. En premier lieu, nous avons démontré que l'activation de la PKC Apl II, tel que mesurée par la translocation à la membrane plasmique, avait aussi lieu à des concentrations de 1 μM 5HT. De plus, nous avons observé des différences dans la translocation de la PKC Apl II à la membrane dans les prolongements par rapport aux corps cellulaires lorsque les neurones sensoriels formaient une synapse avec le neurone moteur. Le récepteur activé par la 5HT en amont de la PKC Apl II demeure inconnu. Nous avons donc cloné les récepteurs B2 et B4 de l'Aplysie et testé leur capacité à activer la PKC Apl II dans une lignée cellulaire soit les cellules Sf9. Les récepteurs B sont uniques à l'Aplysie et ressemblent aux récepteurs d'amines biogènes. Tel que mesuré par la translocation, les récepteurs B2 et B4 n'ont pas activé la PKC Apl II en réponse à la 5HT. Des travaux antérieurs ont montré que la génistéine bloquait l'activation de PKC Apl II et l'inversion de la dépression synaptique. Cependant, le récepteur précis ciblé par la génistéine n'était pas connu. En utilisant des inhibiteurs pharmacologiques, nous avons confirmé que la génistéine bloquait une tyrosine kinase. De plus, nous avons démontré que le récepteur tyrosine kinase de la famille des récepteurs de facteur de croissance des fibroblastes (FGFR) était impliqué dans l'activation PKC Apl II suggérant que la 5HT pouvait transactiver le récepteur FGFR dans les neurones sensoriels de l'Aplysie pour inverser la dépression synaptique.
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Janoshazi, Agnès. "Study of activation process of protein kinase C (PKC) in living cells." Université Louis Pasteur (Strasbourg) (1971-2008), 2008. http://www.theses.fr/2008STR13064.

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Walker, Valerie Glynis. "Pl3-kinase mediates cSrc activation and podosome formation through the adaptor protein, AFAP-110, in response to PKC[alpha] activation." Morgantown, W. Va. : [West Virginia University Libraries], 2007. https://eidr.wvu.edu/etd/documentdata.eTD?documentid=5191.

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Thesis (Ph. D.)--West Virginia University, 2007.<br>Title from document title page. Document formatted into pages; contains viii, 306 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references.
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Da, Lotti Dagan Ginette. "Détermination des pKa de la dézocine." Paris 5, 1995. http://www.theses.fr/1995PA05P024.

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Mazzucotelli, Anne. "Activation du métabolisme énergétique par le co-activateur PGC-1Alpha et implication du récepteur nucléaire PPAR Alpha dans l’adipocyte blanc humain." Toulouse 3, 2007. http://thesesups.ups-tlse.fr/40/.

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L’accumulation de tissu adipeux prédispose au développement d’un certain nombre de désordres métaboliques parmi lesquels l’insulino-résistance et le syndrome métabolique. Une des stratégies envisagées est de convertir les adipocytes blancs en adipocytes présentant un phénotype oxydatif similaire à celui des adipocytes bruns. L’activation de la béta-oxydation et de la thermogenèse permettrait d’augmenter la dépense énergétique tout en utilisant les acides gras libérés par la lipolyse. Récemment, l’équipe a montré que la sur-expression de PGC1alpha dans des cultures primaires d’adipocytes blancs humains différenciés augmente l’expression de la protéine découplante UCP1 ainsi qu’une augmentation de l’oxydation. Afin d’avoir une vision plus large des gènes régulés par PGC1alpha dans l’adipocyte humain des expériences des puces à ADN ont été réalisées. Nous avons démontré que la sur-expression de PGC1alpha dans l’adipocyte humain induit l’expression de nombreux gènes impliqués dans le métabolisme énergétique et ceci indépendamment du récepteur nucléaire PPARgamma. Parallèlement, une augmentation de l’expression du récepteur nucléaire PPARalpha a été observée. PGC1alpha et PPARalpha ont été montré comme impliqués dans la régulation du gène de la glycérol kinase. Ainsi, la sur-expression de PGC1alpha dans l’adipocyte blanc permet la mise en place d’un cycle futile induit par la glycérol kinase ainsi qu’une augmentation de l’oxydation des acides gras ce qui pourrait limiter le relargage des acides gras dans la circulation. Ce résultat révèle une implication possible de PPARalpha dans la régulation de l’expression génique au niveau des adipocytes humains sur exprimant PGC1alpha. <br>Plasma free fatty acids released from white adipose tissue may contribute to the metabolic abnormalities found in obese subjects. Expression of the transcriptional coactivator peroxisome proliferator-activated receptor gamma (PPARgamma) coactivator 1alpha (PGC-1alpha) in human adipocytes leads to a PPARgamma-dependent induction of the uncoupling protein UCP1 and promotes fat oxidation. The aim of the study was to get an exhaustive view of genes regulated by PGC-1alpha. We performed gene expression profiling using pangenomic microarrays. The identified 6 groups of genes: genes down regulated by Rosiglitazone, PGC1alpha or both and genes up regulated by Rosiglitazone, PGC1alpha or both. Among the large number of genes regulated by PGC-1alpha independently of PPARgamma, many genes were involved in mitochondrial metabolism. PGC-1alphaoverexpression induced mRNA expression of the glycerol kinase (GyK) as well as enzymatic activity. PPARalpha was also one of the PGC-1alphatargets. Its activation increased GyK expression and activity. PPARalpha was shown to bind and activate the GyK promoter in PGC-1alpha expressing human adipocytes. In vivo data in various mouse models confirmed the role of PGC-1alpha and PPARalpha in the regulation of GyK. The induction of GyK by PGC-1alpha and PPARalpha offers a new strategy to promote fat utilization in fat cells through the generation of a futile cycle between triglyceride hydrolysis and fatty acid reesterification. Moreover, this work reveals that PPARalpha controls gene expression in human white adipocytes
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Cheng, Cecilia Yuen-Man. "Dissecting the allosteric regulation of PKA-I alpha activation." Diss., [La Jolla] : University of California, San Diego, 2009. http://wwwlib.umi.com/cr/ucsd/fullcit?p3355645.

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Thesis (Ph. D.)--University of California, San Diego, 2009.<br>Title from first page of PDF file (viewed June 23, 2009). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references (p. 200-214).
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Fillmore, Natasha. "Chronic AMP-Activated Protein Kinase Activation and a High-Fat Diet Have an Additive Effect on Mitochondria in Rat Skeletal Muscle." BYU ScholarsArchive, 2010. https://scholarsarchive.byu.edu/etd/2548.

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Factors that stimulate mitochondrial biogenesis in skeletal muscle include AMPK, calcium, and circulating FFAs. Chronic treatment with either AICAR, a chemical activator of AMPK, or increasing circulating FFAs with a high fat diet increases mitochondria in rat skeletal muscle. The purpose of this study was to determine whether the combination of chronic chemical activation of AMPK and high fat feeding would have an additive effect on skeletal muscle mitochondria levels. We treated Wistar male rats with a high fat diet (HF), AICAR injections (AICAR), or a high fat diet and AICAR injections (HF+AICAR) for six weeks. At the end of the treatment period, markers of mitochondrial content were examined in white quadriceps, red quadriceps, and soleus muscles, predominantly composed of unique muscle-fiber types. In white quadriceps, there was a cumulative effect of treatments on LCAD, cytochrome c, and PGC-α protein, as well as on citrate synthase and β-HAD activity. In contrast, no additive effect was noted in the soleus and in the red quadriceps only β-HAD activity increased additively. The additive increase of mitochondrial markers observed in the white quadriceps may be explained by a combined effect of two separate mechanisms: high fat diet-induced post transcriptional increase in PGC-α protein and AMPK mediated increase in PGC-α protein via a transcriptional mechanism. These data show that chronic chemical activation of AMPK and a high fat diet have a muscle type specific additive effect on markers of fatty acid oxidation, the citric acid cycle, the electron transport chain, and transcriptional regulation.
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Books on the topic "PKC activator"

1

J, Weber Walter. Toxic substance removal in activated sludge and PAC treatment systems. U.S. Environmental Protection Agency, Water Engineering Research Laboratory, 1986.

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Griffiths, Gareth Joseph. The selective activation of PKC[delta] by Bistratene A and its role in apoptosis. University of Birmingham, 1998.

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Siderovski, David Peter. Human immunodeficiency virus type-1 trans-activator of transcription (HIV-1 Tat): Random mutagenesis and interaction with PKR. National Library of Canada = Bibliothèque nationale du Canada, 1997.

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Tom, Badgett, ed. Official Sega Genesis and Game Gear strategies, 2ND Edition. Bantam Books, 1991.

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Sandler, Corey. Official Sega Genesis and Game Gear strategies, 3RD Edition. Bantam Books, 1992.

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Official Sega Genesis and Game Gear Strategies, '94 Edition. Random House, Electronic Publishing, 1993.

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Book chapters on the topic "PKC activator"

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Young, Lindon H., Aisha Phillipson, Didi Omiyi, et al. "Protein Kinase C Isoform (PKC) Peptide Activator/Inhibitors Exert Cardioprotective Effects in Polymorphonuclear Leukocyte (PMN)-induced Ischemia/Reperfusion (I/R) Injury." In Understanding Biology Using Peptides. Springer New York, 2006. http://dx.doi.org/10.1007/978-0-387-26575-9_194.

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Okuno, Kenji, Keisuke Taya, Christina R. Marmarou, et al. "The modulation of aquaporin-4 by using PKC-activator (phorbol myristate acetate) and V1a receptor antagonist (SR49059) following middle cerebral artery occlusion/reperfusion in the rat." In Acta Neurochirurgica Supplements. Springer Vienna, 2008. http://dx.doi.org/10.1007/978-3-211-85578-2_84.

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Blumberg, Peter M., Noemi Kedei, Nancy E. Lewin, et al. "Phorbol Esters and Diacylglycerol: The PKC Activators." In Protein Kinase C in Cancer Signaling and Therapy. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-543-9_3.

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Donato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, et al. "Protein Kinase RNA-Activated (PKR)." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101100.

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De Barry, J., H. Shinagawa, A. Janoshazi, M. Ikeda, J. L. Dupont, and T. Yoshioka. "Receptor Activation Studies by Ca2+, Thermal, and PKC Imaging." In Slow Synaptic Responses and Modulation. Springer Japan, 2000. http://dx.doi.org/10.1007/978-4-431-66973-9_24.

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Neagu, Monica, and Carolina Constantin. "Signal Transduction in Immune Cells and Protein Kinases." In Advances in Experimental Medicine and Biology. 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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Chang, Ji Suk, and Thomas W. Gettys. "Analyzing Phosphorylation-Dependent Regulation of Subcellular Localization and Transcriptional Activity of Transcriptional Coactivator NT-PGC-1α." In Peroxisome Proliferator-Activated Receptors (PPARs). Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-155-4_11.

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Brito, Marina, Elvire Guiot, and Pierre Vincent. "Imaging PKA Activation Inside Neurons in Brain Slice Preparations." In Protein Kinase Technologies. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-824-5_13.

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Osol, George. "Protein Kinase C (PKC) Activation Lowers the Calcium Requirement for Cerebral Artery Myogenic Tone." In The Resistance Arteries. Humana Press, 1994. http://dx.doi.org/10.1007/978-1-4757-2296-3_1.

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de Medeiros, Ana Santos, Grace Kwak, Jordan Vanderhooft, Sam Rivera, Rachel Gottlieb, and Charles S. Hoffman. "Fission Yeast-Based High-Throughput Screens for PKA Pathway Inhibitors and Activators." In Methods in Molecular Biology. Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-2269-7_6.

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Conference papers on the topic "PKC activator"

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Qiao, Lixin, Rene Etcheberrigaray, Alan Kozikowski, and Bryan Roth. "LQ12, A Novel PKC Activator, Enhances sAPP Secretion in PC-12 Cells." In The 3rd International Electronic Conference on Synthetic Organic Chemistry. MDPI, 1999. http://dx.doi.org/10.3390/ecsoc-3-01764.

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Kedei, Noemi, Andrea Telek, Gabriella Czifra, et al. "Abstract 4500: What distinguishes a PKC activator like phorbol ester from a PKC functional antagonist like bryostatin 1? Bryologues permit mechanistic insight." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-4500.

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Simizu, Siro, and Wataru Matsuki. "Abstract B045: Structure-activity relationship study of a novel PKC activator, vibsanin A, for induction of differentiation in leukemia cells." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics; October 26-30, 2017; Philadelphia, PA. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1535-7163.targ-17-b045.

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Binnema, D. J., and G. Dooijewaard. "INVOLVEMENT OF FACTOR XII (F XII) AND PREKALLIKREIN (PKK) IN THE ACTIVATION OF UROKINASE (UK)-RELATED PROTEINS IN HUMAN PLASMA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643297.

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Recently it has been shown that in human plasma two types of UK-related proteins occur: Type I, plasma UK, with UK-related antigenic determinants directly accessible to anti-UK antibodies and Type II with UK-related antigenic determinants which become accessible only after SDS treatment and separation of polypeptides on PAGE. In this study we compared the molecular and enzymic properties of the two types in: 1. plasma activated by dextran sulphate (DXS) euglobulin precipitation, 2. plasma that was not activated and 3. plasma deficient in F XII, depleted in PKK and subsequently activated by DXS. ACA 34 gel chromatography, SDS PAGE, fibrin underlay zymography and immunoblotting were used. Results:Conclusions: 1. The UK-related subunits of T1 and TII are active when cleaved, but relatively inactive in the single-chain form. 2. The presence of F XII and PKK is indispensable for activation of TII, but not for that of TI; TII contributes to the F Xll-de-pendent plasminogen activator activity reported earlier, TI to the F Xll-independent part. 3. Activation of TI by DXS with no F XII and PKK present impairs the formation of the 150,000 form. 4. The specific activity of TII is rather low, but its concentration in plasma (not shown) is at least ten times that of TI.
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Lambers, J. W. J., M. Cammenga, B. Konig, H. Pannekoek, and J. A. van Mourik. "ACTIVATION OF HUMAN ENDOTHELIAL TYPE PLASMINOGEN ACTIVATOR INHIBITOR (PAI-1) BY NEGATIVELY CHARGED PHOSPHOLIPIDS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642807.

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The endothelial cell type plasminogen activator inhibitor (PAI-1) may exist in an active, latent form that can be converted into an active form upon exposure to denaturants such as sodium dodecyl sulphate (SDS), guanidine-HCl or urea. Here we show that latent PAI-1 can be activated with lipid vesicles, consisting of the negatively charged phospholipids phosphatidylserine (PS) or phosphatidylinositol (PI). The presence of a net negative charge on the phospholipid headgroup is essential for activation. Incubation with lipid vesicles, consisting of the zwitterionic phospholipids phosphatidylcholine (PC) and phosphatidylethanol-amine (PE), does not result in activation of the inhibitor. In the presence of PS vesicles, the capacity of PAI-1 to inhibit tissue type plasminogen activator (t-PA) is 50-fold higher than that of the untreated protein. For comparison, the activity of PAI-1 was enhanced 25-fold by treatment of the protein with SDS. PS induces activation of the inhibitor at much lower concentrations than SDS. For example, to achieve 50% inhibition of t-PA with a more than 100-fold excess of PAI-1, 0.25 nmoles of PS are required, whereas L.60 nmoles of SDS are necessary to reach half maximal inactivation of t-PA. Activation of PAI-1 by PS can be reversed by the addition of Ca2+-ions, suggesting that Ca2+-ions interfere with the interaction of PAI-1 with the negatively charged lipid surface, thus preventing its activation. The lipid-induced activation of PAI-1 points to a possibly important role of phospholipids in fibrinolysis; regulation of the fibrinolytic activity in blood plasma may ultimately be determined by the extent to which these phospholipids activate the inhibitor of t-PA.This study was supported by the Netherlands Thrombosis Foundation.
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Dooi jewaard, G., D. J. Binnema, and C. Kluft. "CONTACT ACTIVATION AND SINGLE-CHAIN UROKINASE-TYPE PLASMINOGEN ACTIVATOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642958.

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For many years it is known that activation of the factor XII (FXII) -prekallikrein (PKK)- kininogen system of coagulation (contact activation) also may be involved in activation of fibrinolysis. Despite the numerous efforts over the past two decades to clarify this process, our current insights in this matter are far from complete. Also the physiological meaning of this possible interlinkage of coagulation and fibrinolysis is still uncertain; clearcut clinical manifestations in patients deficient in FXII or PKK are not found.No doubt, activation of fibrinolysis is a much more complicated process than it originally was thought to be, and it is only recently that the importance of urokinase for fibrinolysis in the circulation became clear. Two pathways of plasminogen (Pig) activation may be distinguished: 1. the extrinsic system, catalysed by t-PA, which upon stimulus is increasingly released from the endothelial cells of the vessel wall and 2. the intrinsic system, catalysed via Pig proactivators which circulate in the blood at a fairly constant level of concentration. The discovery that the virgin 55 kD urokinase molecule in fact is a single-chain proenzym (now denoted by scu-PA, single-chain urokinase-type PA), the notion that 55 kD scu-PA occurs in the blood and that its concentration even among individuals is fairly constant (2.1+/-0.4 ng/ml, n=52), and the observation that the efficacy of scu-PA is fibrin selective, all are recent findings pointing to the involvement of scu-PA in the intrinsic system.Still the relation between contact activation and the activation of scu-PA is obscure. Active KK, for instance, is an effective activator of 55 kD scu-PA, but proteolytic cleavage of scu-PA resulting in an active molecule, is readily achieved in plasma’s deficient in FXII or PKK. In addition, a portion of Pig activator activity which is dependent for its activation on FXII and PKK, is fully recovered in plasma’s artificially depleted in 55 kD scu-PA. Yet, both portions are activated by negatively charged surfaces or dextransulphate (DXS) as a substitute! These observations have led to the concept of two co-ordinative pathways of Pig activation for the intrinsic system: one containing scu-PA, the other containing FXII, PKK and a postulated Pig proactivator (note that the Pig activator activities of FXIIa and KK per se do not account for the latter portion of activity). Until recently in both pathways was a missing link: in the former it was the step between the negatively charged surface and scu-PA, in the latter it was the postulated Pig proactivator between active KK and Pig. This year, however, it became clear that in plasma artificially depleted in u-PA, still a substantial amount of protein immunochemically related to u-PA, can be detected (at least 35 ng/ml), but only after SDS PAGE. Part of this protein is a single-chain 110 kD molecule which in plasma can be converted to a cleaved molecule with Pig activator activity provided the plasma contains FXII and PKK. Although the relation with the 55 kD scu-PA remained unclear, the discovery of this 110 kD PA with latent urokinase antigen, undoubtedly, explains the missing link between KK and Pig. The other missing link still remains unexplained. It could be an in vitro artefact by DXS causing scu-PA catalysed activation of Pig as fibrin clots do. Since subsequently generated plasmin is capable of activation of both scu-PA and FXII, the two intrinsic pathways are thus interlinked via feed-back activation and consequently may be co-operative in function.
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Mosca, A., S. Viganò D'Angelo, and A. D'Angelo. "ACTIVATION OF PROTEIN C INDUCES CHANGES IN ITS INTRINSIC FLUORESCENCE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644302.

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Upon activation with either thrombin (T) or thrombin-thrombo modulin complex (T-TM), the zymogen protein C (PC) is transformed into a serine-protease, activated protein C(APC), by release of a small activation peptide. The rate of PC activation changes dramatically with T or with T-TM as a function of the Ca++ concentration in the activation medium, suggesting a configurational change of the zymogen in the presence of Ca++ . It has been shown that Ca++ binding to one single high-affinity binding site of gla-domainless PC is accompanied by a significant decrease of the intrinsic fluo rescence emission intensity of the protein and that the high-affinity binding site is retained following activation of gla-domain-less PC (J. Biol. Chem: 258; 5554, 1983). In the present work we have investigated the fluorescence properties of PC in order to answer the following questions: 1) is there a difference in the fluorescence properties of PC as compared to APC? 2) is there a difference between the conformational changes of PC activated with T or T-TM? From our experimental data we conclude that : a) the fluorescence emission intensity of fully activated PC is about 54% of the PC zymogen fluorescence intensity (λexc 280 nm, λ em 345 nm, 0.6 μuM PC or APC in 20 mMTris-HCl, 0.1 M NaCl, pH 7.8 at 25°C) ; b) during activation of PC (2 μM) with T-TM (150 nM) in the presence of 2 mM Ca++ , there is a good correlation (r=0.959) between fluorescence quenching and degree of PC activation, as measured by the rate of cleavage of the chromogenic substrate S-2238; c) the maximal fluorescence quench of PC activated with T or T-TM are virtually identical. Preliminary data suggest that Ca++ affects differently the fluorescence emission properties of PC and APC. These results suggest that evaluation of the fluorescence properties of PC might represent a valuable tool for the characterization of abnormal PC molecules.
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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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Kirschstein, W., U. Hoffmann, S. Simianer, E. Dempfle, C. Kortsik, and D. Heene. "INCREASED THROMBOTIC TENDENCY IN A FAMILY WITH HEREDITARY ANGIONEUROTIC EDEMA ( HANE )." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643048.

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Biochemical hallmark of HANE is a reduction of C1-inhibitor. We observed a family with type II disease ( non-functional protein ), in which 3 of 6 affected members had arterial thromboembolic events at young ages. For evaluation of alterations in the hemostatic system analysis included: fibrinogen, FVII, FVIII, FIX, FXI, FXII, prekallikrein PK, antithrombin III ATIII, protein C PC, α2 antiplasmin α2AP, cl α2 macroglobulin α2 MG, plasminogen activator inhibitor PAI, plasminogen PG, euglobulin clot lysis time ECLT and tissue plasminogen activator tPA at baseline and after venous occlusion. The results are shown in part in the table:There is evidence of nearly no response to venous occlusion in 2 and a diminished response in 1 out of 4 patients.We conclude, that the increased thrombotic tendency in this family is related to the increased potential of prephase coagulation factors and impaired fibrinolytic response to venous occlusion concomitantly with the reduction of the main inhibitor of the contact activation system.
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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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Reports on the topic "PKC activator"

1

Anderson, C. W., M. A. Connelly, H. Zhang, et al. The human DNA-activated protein kinase, DNA-PK: Substrate specificity. Office of Scientific and Technical Information (OSTI), 1994. http://dx.doi.org/10.2172/113929.

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Liang, Jiyong. Activation of P13K/PKB Signaling in Breast Cancer may Inhibit TGFB-Induced G1 Arrest through Changes in p27 Function. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada438990.

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