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Artigos de revistas sobre o tema "PKC"

Autor: Grafiati

Publicado: 4 de junho de 2021

Última modificação: 25 de julho de 2025

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1

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

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We constructed mutant protein kinase C (PKC) cDNAs which expressed PKC activity in vivo in the absence of phorbol ester activation. A hybrid PKC gene, PKAC, was constructed by substituting the coding region for the N-terminal 253 amino acids of PKC alpha with the N-terminal 17 amino acids of the cyclic AMP-dependent protein kinase catalytic subunit (PKA). A truncated PKC gene, delta PKC beta, lacking the coding region for amino acid positions 6 to 159 of PKC beta was also constructed. These mutant kinase genes expressed under the control of the SR alpha promoter activated the c-fos gene enhanc

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2

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

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We constructed mutant protein kinase C (PKC) cDNAs which expressed PKC activity in vivo in the absence of phorbol ester activation. A hybrid PKC gene, PKAC, was constructed by substituting the coding region for the N-terminal 253 amino acids of PKC alpha with the N-terminal 17 amino acids of the cyclic AMP-dependent protein kinase catalytic subunit (PKA). A truncated PKC gene, delta PKC beta, lacking the coding region for amino acid positions 6 to 159 of PKC beta was also constructed. These mutant kinase genes expressed under the control of the SR alpha promoter activated the c-fos gene enhanc

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3

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

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Abstract The female reproductive function largely depends on timing and coordination between follicle-stimulating hormone (FSH) and luteinizing hormone. Even though it was suggested that these hormones act on granulosa cells via shared signaling pathways, mainly protein kinases A, B, and C (PKA, PKB, and PKC), there is still very little information available on how these signaling pathways are regulated by each hormone to provide such differences in gene expression throughout folliculogenesis. To obtain a global picture of the principal upstream factors involved in PKA, PKB, and PKC signaling

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4

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

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5

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. In

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6

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

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Vascular smooth muscle cell (SMC) migration and proliferation contribute to intimal hyperplasia, and protein kinase C (PKC) may be required for both events. In this report, we investigated the role of PKC in proliferation and migration of SMC derived from the human saphenous vein. Activation of PKC by phorbol-12,13-dibutyrate (PDBu) or (−)-indolactam [(−)-ILV] increases SMC proliferation. Downregulation of PKC activity by prolonged incubation with phorbol ester or inhibition of PKC with chelerythrine in SMC diminished agonist-stimulated proliferation. In contrast, stimulation of PKC with PDBu

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7

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

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PKA-mediated phosphorylation of the regulatory (R) domain plays a major role in the activation of the human cystic fibrosis transmembrane conductance regulator (hCFTR). In contrast, the effect of PKC-mediated phosphorylation is controversial, smaller than that of PKA, and dependent on the cell type. In the present study, we expressed Xenopus CFTR ( XCFTR) and hCFTR in Xenopus oocytes and examined their responses (i.e., macroscopic membrane conductance) to maximal stimulation by PKC and PKA agonists. With XCFTR, the average response to PKC was approximately sixfold that of PKA stimulation. In c

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8

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

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Aims: Present study was performed to examine whether ADH was implicated in psychological stress asthma and to explore the underlying molecular mechanism. Methods: We not only examined ADH levels in the cerebrospinal fluid (CSF) via radioimmunoassay, but also measured ADH receptor (ADHR) expression in airway-related vagal preganglionic neurons (AVPNs) through real-time PCR in all experimental mice. Western blotting was performed to evaluate the relationship between ADH and PKA/PKC in psychological stress asthma. Finally, the role of PKA/PKC in psychological stress asthma was analyzed. Results:

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9

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

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Phorbol esters, by activating protein kinase C (PKC), induce the expression of the urokinase-type plasminogen activator (uPA) gene and the proto-oncogene c-fos in LLC-PK1 (PK1) porcine kidney epithelial cells. To investigate the role of PKC in the regulation of these two 12-O-tetradecanoylphorbol-13-acetate (TPA)-inducible genes, the alpha-type PKC, the predominant subtype present in the PK1 cells, was overexpressed in this cell line. Two clonal PK1 derivatives overexpressing the alpha PKC 15- and 20-fold, respectively, were established. Compared with the parental and control cells, only a mod

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10

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

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Abstract The involvement of protein kinase C (PKC) in the action of GH-releasing factor (GRF) and synthetic GH-releasing peptides (GHRP-2 and GHRP-6) was investigated in ovine somatotrophs in primary culture. In partially purified sheep somatotrophs, GRF and GHRP-2 caused translocation of PKC activity from the cytosol to the cell membranes and caused GH release in a dose- and time-dependent manner. GHRP-6 did not cause PKC translocation. The PKC inhibitors, calphostin C, staurosporine and chelerythrine, partially reduced GH release in response to GRF and GHRP-2 at doses which selectively inhib

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11

Dai, Yue, Larry M. Jordan, and Brent Fedirchuk. "Modulation of Transient and Persistent Inward Currents by Activation of Protein Kinase C in Spinal Ventral Neurons of the Neonatal Rat." Journal of Neurophysiology 101, no. 1 (2009): 112–28. http://dx.doi.org/10.1152/jn.01373.2007.

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Neuronal excitability can be regulated through modulation of voltage threshold ( Vth). Previous studies suggested that this modulation could be mediated by modulation of transient sodium currents ( IT) and/or persistent inward current (PIC). Modulation of IT and PIC through activation of protein kinase C (PKC) has previously been described as a mechanism controlling neuronal excitability. We investigated modulation of IT and PIC by PKC in neonatal rat spinal ventral neurons. In whole cell voltage clamp, activation of PKC by application of 1-oleoyl-2-acetyl-sn-glycerol (OAG, 10–30 μM) resulted

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12

Wrede, CE, LM Dickson, MK Lingohr, I. Briaud, and CJ Rhodes. "Fatty acid and phorbol ester-mediated interference of mitogenic signaling via novel protein kinase C isoforms in pancreatic beta-cells (INS-1)." Journal of Molecular Endocrinology 30, no. 3 (2003): 271–86. http://dx.doi.org/10.1677/jme.0.0300271.

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It is possible that activation of protein kinase C (PKC) isoforms by free fatty acids (FFA) plays a role in the failure of pancreatic beta-cell mass expansion to compensate for peripheral insulin resistance in the pathogenesis of type-2 diabetes. The effect of lipid moieties on activation of conventional (PKC-alpha and -beta1), novel (PKC-delta) and atypical (PKC-zeta) PKC isoforms was evaluated in an in vitro assay, using biotinylated neurogranin as a substrate. Oleoyl-Coenzyme A (CoA) and palmitoyl-CoA, but not unesterified FFA, significantly increased the activity of all PKC isoforms (P<

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13

Garcia, Balañà, Lanuza та ін. "Opposed Actions of PKA Isozymes (RI and RII) and PKC Isoforms (cPKCβI and nPKCε) in Neuromuscular Developmental Synapse Elimination". Cells 8, № 11 (2019): 1304. http://dx.doi.org/10.3390/cells8111304.

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Background: During neuromuscular junction (NMJ) development, synapses are produced in excess. By sensing the activity-dependent release of ACh, adenosine, and neurotrophins, presynaptic receptors prompt axonal competition and loss of the unnecessary axons. The receptor action is mediated by synergistic and antagonistic relations when they couple to downstream kinases (mainly protein kinases A and C (PKA and PKC)), which phosphorylate targets involved in axonal disconnection. Here, we directly investigated the involvement of PKA subunits and PKC isoforms in synapse elimination. Methods: Selecti

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14

Beguin, P., A. Beggah, S. Cotecchia, and K. Geering. "Adrenergic, dopaminergic, and muscarinic receptor stimulation leads to PKA phosphorylation of Na-K-ATPase." American Journal of Physiology-Cell Physiology 270, no. 1 (1996): C131—C137. http://dx.doi.org/10.1152/ajpcell.1996.270.1.c131.

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Na-K-adenosinetriphosphatase (Na-K-ATPase) is a potential target for phosphorylation by protein kinase A (PKA) and C (PKC). We have investigated whether the Na-K-ATPase alpha-subunit becomes phosphorylated at its PKA or PKC phosphorylation sites upon stimulation of G protein-coupled receptors primarily linked either to the PKA or the PKC pathway. COS-7 cells, transiently or stably expressing Bufo marinus Na-K-ATPase wild-type alpha- or mutant alpha-subunits affected in its PKA or PKC phosphorylation site, were transfected with recombinant DNA encoding beta 2- or alpha 1-adrenergic (AR), dopami

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15

Hu, Hui-Juan, Kathi S. Glauner, and Robert W. Gereau. "ERK Integrates PKA and PKC Signaling in Superficial Dorsal Horn Neurons. I. Modulation of A-Type K+ Currents." Journal of Neurophysiology 90, no. 3 (2003): 1671–79. http://dx.doi.org/10.1152/jn.00340.2003.

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The transient outward potassium currents (also known as A-type currents or IA) are important determinants of neuronal excitability. In the brain, IA is modulated by protein kinase C (PKC), protein kinase A (PKA), and extracellular signal-related kinase (ERK), three kinases that have been shown to be critical modulators of nociception. We wanted to determine the effects of these kinases on IA in superficial dorsal horn neurons. Using whole cell recordings from cultured mouse spinal cord superficial dorsal horn neurons, we found that PKC and PKA both inhibit IA in these cells, and that PKC has a

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16

Klein, Janet D., Christopher F. Martin, Kimilia J. Kent та Jeff M. Sands. "Protein kinase C-α mediates hypertonicity-stimulated increase in urea transporter phosphorylation in the inner medullary collecting duct". American Journal of Physiology-Renal Physiology 302, № 9 (2012): F1098—F1103. http://dx.doi.org/10.1152/ajprenal.00664.2011.

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The UT-A1 urea transporter plays a critical role in the production of concentrated urine. Both vasopressin and hypertonicity increase urea permeability in rat terminal inner medullary collecting ducts (IMCD). Each agonist independently increases UT-A1 phosphorylation and apical plasma membrane accumulation. Vasopressin activates PKA and phosphorylates UT-A1 at serines 486 and 499. Hypertonicity stimulates urea permeability through protein kinase C (PKC) and intracellular calcium. To determine whether the hypertonic stimulation of urea permeability results from a PKC-mediated phosphorylation of

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17

Erclik, Mary S., та Jane Mitchell. "The role of protein kinase C-δ in PTH stimulation of IGF-binding protein-5 mRNA in UMR-106–01 cells". American Journal of Physiology-Endocrinology and Metabolism 282, № 3 (2002): E534—E541. http://dx.doi.org/10.1152/ajpendo.00417.2001.

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We have investigated the role of protein kinase C (PKC) signal transduction pathways in parathyroid hormone (PTH) regulation of insulin-like growth factor-binding protein-5 (IGFBP-5) gene expression in the rat osteoblast-like cell line UMR-106–01. Involvement of the PKC pathway was determined by the findings that bisindolylmaleimide I inhibited 40% of the PTH effect, and 1 μM bovine PTH-(3–34) stimulated a 10-fold induction of IGFBP-5 mRNA. PTH-(1–34) and PTH-(3–34) (100 nM) both stimulated PKC-δ translocation from the membrane to the nuclear fraction. Rottlerin, a PKC-δ-specific inhibitor, an

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18

Hu, Hui-Juan, and Robert W. Gereau. "ERK Integrates PKA and PKC Signaling in Superficial Dorsal Horn Neurons. II. Modulation of Neuronal Excitability." Journal of Neurophysiology 90, no. 3 (2003): 1680–88. http://dx.doi.org/10.1152/jn.00341.2003.

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Protein kinases belonging to the protein kinase A (PKA), protein kinase C (PKC), and extracellular signal-related kinase (ERK) families have been identified as key players in modulating nociception at the level of the spinal cord dorsal horn, yet little is known about the effects of these kinases on membrane properties of the dorsal horn neurons. PKA, PKC, and ERK exert inhibitory effects on transient potassium currents (A-type currents or IA) in mouse superficial dorsal horn neurons ( Hu et al. 2003 ). Here we aimed to determine the effects of these kinases on action potential firing and memb

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19

Button, Brian, Luis Reuss, and Guillermo A. Altenberg. "Pkc-Mediated Stimulation of Amphibian Cftr Depends on a Single Phosphorylation Consensus Site. Insertion of This Site Confers Pkc Sensitivity to Human Cftr." Journal of General Physiology 117, no. 5 (2001): 457–68. http://dx.doi.org/10.1085/jgp.117.5.457.

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Mutations of the CFTR, a phosphorylation-regulated Cl− channel, cause cystic fibrosis. Activation of CFTR by PKA stimulation appears to be mediated by a complex interaction between several consensus phosphorylation sites in the regulatory domain (R domain). None of these sites has a critical role in this process. Here, we show that although endogenous phosphorylation by PKC is required for the effect of PKA on CFTR, stimulation of PKC by itself has only a minor effect on human CFTR. In contrast, CFTR from the amphibians Necturus maculosus and Xenopus laevis (XCFTR) can be activated to similar

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20

Yano, Kenji, Jeanette R. Bauchat, Marya B. Liimatta, David R. Clemmons, and Cunming Duan. "Down-Regulation of Protein Kinase C Inhibits Insulin-Like Growth Factor I-Induced Vascular Smooth Muscle Cell Proliferation, Migration, and Gene Expression1." Endocrinology 140, no. 10 (1999): 4622–32. http://dx.doi.org/10.1210/endo.140.10.7035.

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Abstract Insulin-like growth factor-I (IGF-I) plays an important role in regulating vascular smooth muscle cell (VSMC) proliferation, directed migration, differentiation, and apoptosis. The signaling mechanisms used by IGF-I to elicit these actions, however, are not well defined. In this study, we examined the role(s) of protein kinase C (PKC) in mediating the IGF-I actions in cultured porcine VSMCs. Out of the eleven known members of PKC family, PKC-α, -βI, -ε, -η, -λ,θ , and -ζ, were detectable by Western immunoblot analysis in these cells. Further analysis indicated that the subcellular dis

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21

Vanoye, Carlos G., Ariel F. Castro, Thierry Pourcher, Luis Reuss, and Guillermo A. Altenberg. "Phosphorylation of P-glycoprotein by PKA and PKC modulates swelling-activated Cl− currents." American Journal of Physiology-Cell Physiology 276, no. 2 (1999): C370—C378. http://dx.doi.org/10.1152/ajpcell.1999.276.2.c370.

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Several proteins belonging to the ATP-binding cassette superfamily can affect ion channel function. These include the cystic fibrosis transmembrane conductance regulator, the sulfonylurea receptor, and the multidrug resistance protein P-glycoprotein (MDR1). We measured whole cell swelling-activated Cl− currents ( I Cl,swell) in parental cells and cells expressing wild-type MDR1 or a phosphorylation-defective mutant (Ser-661, Ser-667, and Ser-671 replaced by Ala). Stimulation of protein kinase C (PKC) with a phorbol ester reduced the rate of increase in I Cl,swell only in cells that express MDR

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22

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 PK

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23

Sugden, D., and S. J. Rowe. "Protein kinase C activation antagonizes melatonin-induced pigment aggregation in Xenopus laevis melanophores." Journal of Cell Biology 119, no. 6 (1992): 1515–21. http://dx.doi.org/10.1083/jcb.119.6.1515.

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The pineal hormone, melatonin (5-methoxy N-acetyltryptamine) induces a rapid aggregation of melanin-containing pigment granules in isolated melanophores of Xenopus laevis. Treatment of melanophores with activators of protein kinase C (PKC), including phorbol esters, mezerein and a synthetic diacylglycerol, did not affect pigment granule distribution but did prevent and reverse melatonin-induced pigment aggregation. This effect was blocked by an inhibitor of PKC, Ro 31-8220. The inhibitory effect was not a direct effect on melatonin receptors, per se, as the slow aggregation induced by a high c

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Hayabuchi, Y., N. B. Standen, and N. W. Davies. "Angiotensin II inhibits and alters kinetics of voltage-gated K+ channels of rat arterial smooth muscle." American Journal of Physiology-Heart and Circulatory Physiology 281, no. 6 (2001): H2480—H2489. http://dx.doi.org/10.1152/ajpheart.2001.281.6.h2480.

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The vasoconstrictor angiotensin II (ANG II) inhibits several types of K+ channels. We examined the inhibitory mechanism of ANG II on voltage-gated K+ (KV) currents ( I KV ) recorded from isolated rat arterial smooth muscle using patch-clamp techniques. Application of 100 nM ANG II accelerated the activation of I KV but also caused inactivation. These effects were abolished by the AT1 receptor antagonist losartan. The protein kinase A (PKA) inhibitor Rp-cyclic 3′,5′-hydrogen phosphothioate adenosine (100 μM) and an analog of diacylglycerol, 1,2-dioctanyoyl-rac-glycerol (2 μM), caused a signific

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Xie, Guofeng, and Jean-Pierre Raufman. "Association of protein kinase A with AKAP150 facilitates pepsinogen secretion from gastric chief cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 281, no. 4 (2001): G1051—G1058. http://dx.doi.org/10.1152/ajpgi.2001.281.4.g1051.

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Cross talk between signal transduction pathways augments pepsinogen secretion from gastric chief cells. A-kinase anchoring proteins (AKAPs) associate with regulatory subunits of protein kinase A (PKA), protein kinase C (PKC), and protein phosphatase 2B (PP2B) and localize this protein complex to specific cell compartments. We determined whether an AKAP-signaling protein complex exists in chief cells and whether this modulates secretion. In Western blots, we identified AKAP150, a rodent homologue of human AKAP79 that coimmunoprecipitates with PKA, PKC, and actin. The association of PKA and PP2B

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Mullin, James M., Jennifer A. Kampherstein, Kathleen V. Laughlin та ін. "Overexpression of protein kinase C-δ increases tight junction permeability in LLC-PK1epithelia". American Journal of Physiology-Cell Physiology 275, № 2 (1998): C544—C554. http://dx.doi.org/10.1152/ajpcell.1998.275.2.c544.

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The Ca2+-independent δ-isoform of protein kinase C (PKC-δ) was overexpressed in LLC-PK1 epithelia and placed under control of a tetracycline-responsive expression system. In the absence of tetracycline, the exogenous PKC-δ is expressed. Western immunoblots show that the overexpressed PKC-δ is found in the cytosolic, membrane-associated, and Triton-insoluble fractions. Overexpression of PKC-δ produced subconfluent and confluent epithelial morphologies similar to that observed on exposure of wild-type cells to the phorbol ester 12- O-tetradecanoylphorbol-13-acetate. Transepithelial electrical re

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Nakamura, Yuya, Masahiro Inagaki, Mayumi Tsuji, et al. "Linagliptin Has Wide-Ranging Anti-Inflammatory Points of Action in Human Umbilical Vein Endothelial Cells." Japanese Clinical Medicine 7 (January 2016): JCM.S39317. http://dx.doi.org/10.4137/jcm.s39317.

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Background Because of the potential anti-inflammatory effects, linagliptin, a therapeutic dipeptidyl peptidase-4 inhibitor, is used as an effective drug for diabetic patients for whom inflammation is a prognosis-related factor. We investigated the anti-inflammatory mechanism of linagliptin using seven markers. Methods We pretreated human umbilical vein endothelial cells (HUVECs), with linagliptin and lipopolysaccharide (LPS). The cytosolic fractions were evaluated for protein kinase A (PKA), protein kinase B (PKB), protein kinase C (PKC), ratio of reactive oxygen species (ROS) and Cu/Zn supero

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Middleton, Lisa M., and Robert D. Harvey. "PKC regulation of cardiac CFTR Cl− channel function in guinea pig ventricular myocytes." American Journal of Physiology-Cell Physiology 275, no. 1 (1998): C293—C302. http://dx.doi.org/10.1152/ajpcell.1998.275.1.c293.

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The role of protein kinase C (PKC) in regulating the protein kinase A (PKA)-activated Cl− current conducted by the cardiac isoform of the cystic fibrosis transmembrane conductance regulator (cCFTR) was studied in guinea pig ventricular myocytes using the whole cell patch-clamp technique. Although stimulation of endogenous PKC with phorbol 12,13-dibutyrate (PDBu) alone did not activate this Cl− current, even when intracellular dialysis was limited with the perforated patch-clamp technique, activation of PKC did elicit a significant response in the presence of PKA-dependent activation of the cur

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Jiang, Quan, Mulan He, Xinyan Wang та Anderson O. L. Wong. "Grass carp somatolactin: II. Pharmacological study on postreceptor signaling mechanisms for PACAP-induced somatolactin-α and -β gene expression". American Journal of Physiology-Endocrinology and Metabolism 295, № 2 (2008): E477—E490. http://dx.doi.org/10.1152/ajpendo.90386.2008.

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Somatolactin (SL), the latest member of the growth hormone/prolactin family, is a novel pituitary hormone with diverse functions. However, the signal transduction mechanisms responsible for SL expression are still largely unknown. Using grass carp as an animal model, we examined the direct effects of pituitary adenylate cyclase-activating polypeptide (PACAP) on SL gene expression at the pituitary level. In primary cultures of grass carp pituitary cells, SLα and SLβ mRNA levels could be elevated by PACAP via activation of PAC-I receptors. With the use of a pharmacological approach, the AC/cAMP/

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Fuller, William, Jacqueline Howie, Linda M. McLatchie, et al. "FXYD1 phosphorylation in vitro and in adult rat cardiac myocytes: threonine 69 is a novel substrate for protein kinase C." American Journal of Physiology-Cell Physiology 296, no. 6 (2009): C1346—C1355. http://dx.doi.org/10.1152/ajpcell.00523.2008.

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FXYD1 (phospholemman), the primary sarcolemmal kinase substrate in the heart, is a regulator of the cardiac sodium pump. We investigated phosphorylation of FXYD1 peptides by purified kinases using HPLC, mass spectrometry, and Edman sequencing, and FXYD1 phosphorylation in cultured adult rat ventricular myocytes treated with PKA and PKC agonists by phosphospecific immunoblotting. PKA phosphorylates serines 63 and 68 (S63 and S68) and PKC phosphorylates S63, S68, and a new site, threonine 69 (T69). In unstimulated myocytes, FXYD1 is ∼30% phosphorylated at S63 and S68, but barely phosphorylated a

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Vijayaragavan, Kausalia, Mohamed Boutjdir, and Mohamed Chahine. "Modulation of Nav1.7 and Nav1.8 Peripheral Nerve Sodium Channels by Protein Kinase A and Protein Kinase C." Journal of Neurophysiology 91, no. 4 (2004): 1556–69. http://dx.doi.org/10.1152/jn.00676.2003.

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Voltage-gated Na+ channels (VGSC) are transmembrane proteins that are essential for the initiation and propagation of action potentials in neuronal excitability. Because neurons express a mixture of Na+ channel isoforms and protein kinase C (PKC) isozymes, the nature of which channel is being regulated by which PKC isozyme is not known. We showed that DRG VGSC Nav1.7 (TTX-sensitive) and Nav1.8 (TTX-resistant), expressed in Xenopus oocytes were differentially regulated by protein kinase A (PKA) and PKC isozymes using the two-electrode voltage-clamp method. PKA activation resulted in a dose-depe

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Rubiś, Błazej, Sylwia Grodecka-Gazdecka, Remigiusz Lecybył, Marta Ociepa, Zygmunt Krozowski, and Wiesław H. Trzeciak. "Contribution of protein kinase A and protein kinase C signalling pathways to the regulation of HSD11B2 expression and proliferation of MCF-7 cells." Acta Biochimica Polonica 51, no. 4 (2004): 919–24. https://doi.org/10.18388/abp.2004_3524.

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Contribution of the protein kinase A (PKA) and protein kinase C (PKC) signalling pathways to the regulation of 11beta-hydroxysteroid dehydrogenase type II (HSD11B2) gene expression was investigated in human breast cancer cell line MCF-7. Treatment of the cells with an adenylyl cyclase activator, forskolin, known to stimulate the PKA pathway, resulted in an increase in HSD11B2 mRNA content. Semi-quantitative RT-PCR revealed attenuation of the effect of forskolin by phorbol ester, tetradecanoyl phorbol acetate (TPA), an activator of the PKC pathway. It was also demonstrated that specific inhibit

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Greco, S., C. Storelli та S. Marsigliante. "Protein kinase C (PKC)-δ/-ε mediate the PKC/Akt-dependent phosphorylation of extracellular signal-regulated kinases 1 and 2 in MCF-7 cells stimulated by bradykinin". Journal of Endocrinology 188, № 1 (2006): 79–89. http://dx.doi.org/10.1677/joe.1.06433.

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In this paper the signal transduction pathways evoked by bradykinin (BK) in MCF-7 breast cancer cells were investigated. BK activation of the B2 receptor provoked: (a) the phosphorylation of the extracellular signal-regulated kinases 1 and 2 (ERK1/2); (b) the translocation from the cytosol to the membrane of the conventional protein kinase C-α (PKC-α) and novel PKC-δ and PKC-ε; (c) the phosphorylation of protein kinase B (PKB/ Akt); (d) the proliferation of MCF-7 cells. The BK-induced ERK1/2 phosphorylation was completely blocked by PD98059 (an inhibitor of the mitogen-activated protein kinase

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Zhang, Q. Y., C. Hammerberg, J. J. Baldassare, et al. "Retinoic acid and phorbol ester synergistically up-regulate IL-8 expression and specifically modulate protein kinase C-epsilon in human skin fibroblasts." Journal of Immunology 149, no. 4 (1992): 1402–8. http://dx.doi.org/10.4049/jimmunol.149.4.1402.

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Abstract Phorbol ester (TPA) and retinoic acid (RA) are two potent immunomodulatory agents whose actions are mediated through distinct signal transduction pathways involving protein kinase C (PKC) and nuclear RA receptors, respectively. We have investigated the interactions between these two pathways in the regulation of expression of the inflammatory cytokine IL-8 in human skin fibroblasts. TPA (as previously reported) and RA both induced IL-8 mRNA and protein in a time- and dose-dependent manner. IL-8 mRNA induction by TPA (10 nM) was maximal (15-fold) within 6 h, and returned to baseline wi

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Dobado-Berrios, Pablo, Rosa Ros, Antonio Torres, et al. "Signal Transduction Pathways Underlying the Expression of Tissue Factor and Thrombomodulin in Promyelocytic Cells Induced to Differentiate by Retinoid Acid and Dibutyryl cAMP." Thrombosis and Haemostasis 85, no. 06 (2001): 1031–36. http://dx.doi.org/10.1055/s-0037-1615959.

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SummaryAcute promyelocytic leukaemia (APL) may be associated with disseminated intravascular coagulation, as a result of increased tissue factor (TF) expression and reduced thrombomodulin (TM) expression by APL blast cells. During retinoid acid (RA)- and dibutyryl cAMP (dbcAMP)-induced differentiation of the APL cells, there is a marked up-modulation of both the protein kinase A (PKA) and C (PKC) activities. In order to further assess whether these kinases are intimately associated with both the differentiation process and the regulation of TF and TM expression, we have correlated the modulati

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Rotfeld, H., P. Hillman, D. Ickowicz, and H. Breitbart. "PKA and CaMKII mediate PI3K activation in bovine sperm by inhibition of the PKC/PP1 cascade." REPRODUCTION 147, no. 3 (2014): 347–56. http://dx.doi.org/10.1530/rep-13-0560.

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To enable fertilization, spermatozoa must undergo several biochemical processes in the female reproductive tract, collectively called capacitation. These processes involve protein kinase A (PKA)-dependent protein tyrosine phosphorylation including phosphatidylinositol-3-kinase (PI3K). It is not known how PKA, a serine/threonine (S/T) kinase, mediates tyrosine phosphorylation of proteins. We recently showed that inhibition of S/T phosphatase 1 (PP1) causes a significant increase in phospho-PI3K. In this study, we propose a mechanism by which PKA and PP1 mediate an increase in PI3K tyrosine phos

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KAPADIA, RINA, PETER D. YURCHENCO, and KURT AMSLER. "Binding of the Renal Epithelial Cell Line LLC-PK1 to Laminin Is Regulated by Protein Kinase C." Journal of the American Society of Nephrology 10, no. 6 (1999): 1214–23. http://dx.doi.org/10.1681/asn.v1061214.

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Abstract. The α6β1 integrin heterodimer has been implicated in the mediation of renal epithelial cell binding to laminin, and it has been suggested that this binding is important for renal morphogenesis and development. Studies of nonrenal cells have suggested that the functional activity of α6β1 integrin is regulated by protein kinase C (PKC) activity. In this study, the binding of a renal epithelial cell line, LLC-PK1, to laminin was characterized and the role of PKC activity in the modulation of binding was investigated. LLC-PK1 cells bound to laminin-coated surfaces in a time- and laminin

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Shaw, Erynn E., Philip Wood, Justyna Kulpa, Feng Hua Yang, Alastair J. Summerlee, and W. Glen Pyle. "Relaxin alters cardiac myofilament function through a PKC-dependent pathway." American Journal of Physiology-Heart and Circulatory Physiology 297, no. 1 (2009): H29—H36. http://dx.doi.org/10.1152/ajpheart.00482.2008.

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The pregnancy hormone relaxin (RLX) is a powerful cardiostimulatory peptide. Despite its well-characterized effects on the heart, the intracellular mechanisms responsible for RLX's positive inotropic effects are unknown. Cardiac myofilaments are the central contractile elements of the heart, and changes in the phosphorylation status of myofilament proteins are known to mediate changes in function. The first objective of this study was to determine whether RLX stimulates myofilament activation and alters the phosphorylation of one or more myofilament proteins. RLX works through a variety of int

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Ragolia, Louis, Thomas Palaia, Enesa Paric, and John K. Maesaka. "Elevated L-PGDS activity contributes to PMA-induced apoptosis concomitant with downregulation of PI3-K." American Journal of Physiology-Cell Physiology 284, no. 1 (2003): C119—C126. http://dx.doi.org/10.1152/ajpcell.00247.2002.

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Recently we demonstrated the induction of apoptosis by the addition of recombinant lipocalin-type prostaglandin D2 synthase (L-PGDS) to the culture medium of LLC-PK1 cells. Because protein kinase C (PKC) has been shown to be involved in the apoptotic process of various cell types, we examined the potential role of L-PGDS in phorbol 12-myristate 13-acetate (PMA)-induced apoptosis. We report here the enzymatic activation and phosphorylation of L-PGDS in response to phorbol ester in cell culture and the direct phosphorylation of recombinant L-PGDS by PKC in vitro. Treatment of cells with PMA or L

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Zhou, Lian, Douglas A. Baxter, and John H. Byrne. "Contribution of PKC to the maintenance of 5-HT-induced short-term facilitation at sensorimotor synapses of Aplysia." Journal of Neurophysiology 112, no. 8 (2014): 1936–49. http://dx.doi.org/10.1152/jn.00577.2013.

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Aplysia sensorimotor synapses provide a useful model system for analyzing molecular processes that contribute to heterosynaptic plasticity. For example, previous studies demonstrated that multiple kinase cascades contribute to serotonin (5-HT)-induced short-term synaptic facilitation (STF), including protein kinase A (PKA) and protein kinase C (PKC). Moreover, the contribution of each kinase is believed to depend on the state of the synapse (e.g., depressed or nondepressed) and the time after application of 5-HT. Here, a previously unappreciated role for PKC-dependent processes was revealed to

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Kirton, C. Adam, and Rodger Loutzenhiser. "Alterations in basal protein kinase C activity modulate renal afferent arteriolar myogenic reactivity." American Journal of Physiology-Heart and Circulatory Physiology 275, no. 2 (1998): H467—H475. http://dx.doi.org/10.1152/ajpheart.1998.275.2.h467.

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Myogenic vasoconstriction of the renal afferent arteriole contributes to the autoregulation of renal blood flow, glomerular filtration rate, and glomerular capillary pressure (PGC). The reactivity of the afferent arteriole to pressure and the efficiency of PGC control are subject to physiological and pathophysiological alterations, but the determinants of the myogenic response of this vessel are largely unknown. We used the in vitro perfused hydronephrotic rat kidney to investigate the role of protein kinase C (PKC) in the control of this response. Inhibition of PKC by 1 μM chelerythrine atten

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Rider, M. H., J. Vandamme, E. Lebeau, et al. "The two forms of bovine heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase result from alternative splicing." Biochemical Journal 285, no. 2 (1992): 405–11. http://dx.doi.org/10.1042/bj2850405.

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Purified bovine heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2) showed two bands with subunit M(r) of 58,000 and 54,000 when analysed by SDS/PAGE. Both the 58,000- and 54,000-M(r) forms were phosphorylated by cyclic AMP-dependent protein kinase (PKA) and by protein kinase C (PKC) in vitro. Phosphorylation by PKA decreased the apparent Km of PFK-2 for one of its substrates, fructose 6-phosphate, while phosphorylation by PKC did not correlate with any change in PFK-2 activity. The differences between the 58,000- and 54,000-M(r) forms were studied by electroblotting, p

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Chen, Yongyue, Brian Button, Guillermo A. Altenberg, and Luis Reuss. "Potentiation of effect of PKA stimulation of Xenopus CFTR by activation of PKC: role of NBD2." American Journal of Physiology-Cell Physiology 287, no. 5 (2004): C1436—C1444. http://dx.doi.org/10.1152/ajpcell.00045.2004.

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Activity of the human (h) cystic fibrosis transmembrane conductance regulator (CFTR) channel is predominantly regulated by PKA-mediated phosphorylation. In contrast, Xenopus ( X)CFTR is more responsive to PKC than PKA stimulation. We investigated the interaction between the two kinases in XCFTR. We expressed XCFTR in Xenopus oocytes and maximally stimulated it with PKA agonists. The magnitude of activation after PKC stimulation was about eightfold that without pretreatment with PKC agonist. hCFTR, expressed in the same system, lacked this response. We name this phenomenon XCFTR-specific PKC po

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Garcia, Neus, Maria A. Lanuza, Marta Tomàs, et al. "PKA and PKC Balance in Synapse Elimination during Neuromuscular Junction Development." Cells 10, no. 6 (2021): 1384. http://dx.doi.org/10.3390/cells10061384.

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During the development of the nervous system, synaptogenesis occurs in excess though only the appropriate connections consolidate. At the neuromuscular junction, competition between several motor nerve terminals results in the maturation of a single axon and the elimination of the others. The activity-dependent release of transmitter, cotransmitters, and neurotrophic factors allows the direct mutual influence between motor axon terminals through receptors such as presynaptic muscarinic ACh autoreceptors and the tropomyosin-related kinase B neurotrophin receptor. In previous studies, we investi

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Karihaloo, A., K. Kato, D. A. Greene, and T. P. Thomas. "Protein kinase and Ca2+ modulation of myo-inositol transport in cultured retinal pigment epithelial cells." American Journal of Physiology-Cell Physiology 273, no. 2 (1997): C671—C678. http://dx.doi.org/10.1152/ajpcell.1997.273.2.c671.

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The acute regulation of inwardly directed Na(+)-myo-inositol (MI) cotransporter activity and basal and volume-sensitive MI efflux by protein kinases C (PKC) and A (PKA), cytosolic Ca2+, and phosphoinositide (PI) turnover were characterized in cultured human retinal pigment epithelial cells using 2-[3H]MI and liquid scintillation spectrometry. Kinetic analysis revealed two distinct Na(+)-MI cotransporter components differing in apparent Michaelis constant and maximal velocity. Composite Na(+)-MI cotransport activity was stimulated by PKA activation, the muscarinic agonist carbachol, and the Ca2

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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 pro

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Zheng, Yunhe, Chen Yang, Xiu’e Zheng, Qiangdong Guan, and Sufang Yu. "Acrylamide treatment alters the level of Ca2+ and Ca2+-related protein kinase in spinal cords of rats." Toxicology and Industrial Health 37, no. 3 (2021): 113–23. http://dx.doi.org/10.1177/0748233720971879.

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This study aimed to analyze the neurological changes induced by acrylamide (ACR) poisoning and their underlying mechanisms within the spinal cords of male adult Wistar rats. The rats were randomly divided into three groups ( n = 9 rats per group). ACR was intraperitoneally injected to produce axonopathy according to the daily dosing schedules of 20 or 40 mg/kg/day of ACR for eight continuous weeks (three times per week). During the exposure period, body weights and gait scores were assessed, and the concentration of Ca2+ was calculated in 27 mice. Protein kinase A (PKA), protein kinase C (PKC)

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Takimura, Tetsuo, Kenji Kamata, Kazuhiro Fukasawa та ін. "Structures of the PKC-ι kinase domain in its ATP-bound and apo forms reveal defined structures of residues 533–551 in the C-terminal tail and their roles in ATP binding". Acta Crystallographica Section D Biological Crystallography 66, № 5 (2010): 577–83. http://dx.doi.org/10.1107/s0907444910005639.

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Protein kinase C (PKC) plays an essential role in a wide range of cellular functions. Although crystal structures of the PKC-θ, PKC-ι and PKC-βII kinase domains have previously been determined in complexes with small-molecule inhibitors, no structure of a PKC–substrate complex has been determined. In the previously determined PKC-ι complex, residues 533–551 in the C-terminal tail were disordered. In the present study, crystal structures of the PKC-ι kinase domain in its ATP-bound and apo forms were determined at 2.1 and 2.0 Å resolution, respectively. In the ATP complex, the electron density o

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Wetsel, WC, WA Khan, I. Merchenthaler, et al. "Tissue and cellular distribution of the extended family of protein kinase C isoenzymes." Journal of Cell Biology 117, no. 1 (1992): 121–33. http://dx.doi.org/10.1083/jcb.117.1.121.

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Polyclonal isoenzyme-specific antisera were developed against four calcium-independent protein kinase C (PKC) isoenzymes (delta, epsilon, epsilon', and zeta) as well as the calcium-dependent isoforms (alpha, beta I, beta II, and gamma). These antisera showed high specificities, high titers, and high binding affinities (3-370 nM) for the peptide antigens to which they were raised. Each antiserum detected a species of the predicted molecular weight by Western blot that could be blocked with the immunizing peptide. PKC was sequentially purified from rat brain, and the calcium-dependent forms were

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Hermann-Kleiter, Natascha, Nikolaus Thuille, Christa Pfeifhofer та ін. "PKCθ and PKA are antagonistic partners in the NF-AT transactivation pathway of primary mouse CD3+ T lymphocytes". Blood 107, № 12 (2006): 4841–48. http://dx.doi.org/10.1182/blood-2005-10-4044.

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AbstractWe here investigate the crosstalk of PKC and PKA signaling during primary CD3+ T-lymphocyte activation using pharmacologic inhibitors and activators in combination with our established panel of PKC isotype–deficient mouse T cells in vitro. PKCθ and PKA inversely affect the CD3/CD28-induced IL-2 expression, whereas other PKC isotypes are dispensable in this signaling pathway. Gene ablation of PKCθ selectively results in a profound reduction of IL-2 production; however, complete abrogation of IL-2 production in these PKCθ–/– T cells was achieved only by simultaneous coactivation of the c

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