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Volumn 66, Issue 6, 1996, Pages 2381-2389

Phorbol ester-enhanced noradrenaline secretion correlates with the presence and activity of protein kinase C-α in human SH-SY5Y neuroblastoma cells

Author keywords

Bryostatin; Down regulation; Noradrenaline release; Phorbol ester; Protein kinase C; SH SY5Y neuroblastoma cells

Indexed keywords

3 [1 (3 AMINOPROPYL) 3 INDOLYL] 4 (1 METHYL 3 INDOLYL) 1H PYRROLE 2,5 DIONE; BRYOSTATIN; CARBACHOL; NORADRENALIN; PHORBOL 13 ACETATE 12 MYRISTATE; PHORBOL DIBUTYRATE; PHORBOL ESTER; POTASSIUM ION; PROTEIN KINASE C; PROTEIN KINASE C INHIBITOR;

EID: 0029975424     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.66062381.x     Document Type: Article
Times cited : (21)

References (38)
  • 1
    • 0025989384 scopus 로고
    • Preferential release of catecholamine from permeabilized PC12 cells by α- and β-type protein kinase C subspecies
    • Ben-Shlomo H., Sigmund O., Stabel S., Reiss N., and Naor Z. (1991) Preferential release of catecholamine from permeabilized PC12 cells by α- and β-type protein kinase C subspecies. Biochem. J. 280, 65-69.
    • (1991) Biochem. J. , vol.280 , pp. 65-69
    • Ben-Shlomo, H.1    Sigmund, O.2    Stabel, S.3    Reiss, N.4    Naor, Z.5
  • 2
    • 0023681462 scopus 로고
    • A major role for protein kinase C in calcium-activated exocytosis in permeabilised adrenal chromaffin cells
    • Burgoyne R. D., Morgan A., and O'Sullivan A. J. (1988) A major role for protein kinase C in calcium-activated exocytosis in permeabilised adrenal chromaffin cells. FEBS Lett. 238, 151-155.
    • (1988) FEBS Lett. , vol.238 , pp. 151-155
    • Burgoyne, R.D.1    Morgan, A.2    O'Sullivan, A.J.3
  • 3
    • 0020326790 scopus 로고
    • Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumour-promoting phorbol esters
    • Castagna M., Takai Y., Kaibuchi K., Sano K., Kikkawa U., and Nishizuka Y. (1982) Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumour-promoting phorbol esters. J. Biol. Chem. 257, 7847-7851.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7847-7851
    • Castagna, M.1    Takai, Y.2    Kaibuchi, K.3    Sano, K.4    Kikkawa, U.5    Nishizuka, Y.6
  • 4
    • 0027382816 scopus 로고
    • Protein kinase C and the regulation of glutamate exocytosis from cerebrocortical synaptosomes
    • Coffey E. T., Sihra T. S., and Nicholls D. G. (1993) Protein kinase C and the regulation of glutamate exocytosis from cerebrocortical synaptosomes. J. Biol. Chem. 268, 21060-21065.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21060-21065
    • Coffey, E.T.1    Sihra, T.S.2    Nicholls, D.G.3
  • 5
    • 0024324487 scopus 로고
    • Comparison of effects of bryostatins 1 and 2 and 12-O-tetradecanoylphorbol-13-acetate on protein kinase C activity in A549 human lung carcinoma cells
    • Dale I. L., Bradshaw T. D., Gescher A., and Pettit G. R. (1989) Comparison of effects of bryostatins 1 and 2 and 12-O-tetradecanoylphorbol-13-acetate on protein kinase C activity in A549 human lung carcinoma cells. Cancer Res. 49, 3242-3245.
    • (1989) Cancer Res. , vol.49 , pp. 3242-3245
    • Dale, I.L.1    Bradshaw, T.D.2    Gescher, A.3    Pettit, G.R.4
  • 7
    • 0026347085 scopus 로고
    • Transmitter release: Target of regulation by protein kinase C
    • (Gispen W. H. and Routtenberg A., eds), Elsevier Science Publishers, Amsterdam
    • Dekker L. V., De Graan P. N. E., and Gispen W. H. (1991) Transmitter release: target of regulation by protein kinase C, in Progress in Brain Research, Vol. 89 (Gispen W. H. and Routtenberg A., eds), pp. 209-233. Elsevier Science Publishers, Amsterdam.
    • (1991) Progress in Brain Research , vol.89 , pp. 209-233
    • Dekker, L.V.1    De Graan, P.N.E.2    Gispen, W.H.3
  • 8
    • 0025955689 scopus 로고
    • Role of protein kinase C in catecholamine secretion from digitonin-permeabilized bovine adrenal medullary cells
    • Isosaki M., Nakashima T., and Kurogochi Y. (1991) Role of protein kinase C in catecholamine secretion from digitonin-permeabilized bovine adrenal medullary cells. J. Biol. Chem. 266, 16703-16707.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16703-16707
    • Isosaki, M.1    Nakashima, T.2    Kurogochi, Y.3
  • 9
    • 0025314944 scopus 로고
    • Effects of bryostatins 1 and 2 on morphological and functional differentiation of SH-SY5Y human neuroblastoma cells
    • Jalava A. M., Heikkilä J., Åkerlind G., Pettit G. R., and Åkerman K. E. O. (1990) Effects of bryostatins 1 and 2 on morphological and functional differentiation of SH-SY5Y human neuroblastoma cells. Cancer Res. 50, 3422-3428.
    • (1990) Cancer Res. , vol.50 , pp. 3422-3428
    • Jalava, A.M.1    Heikkilä, J.2    Åkerlind, G.3    Pettit, G.R.4    Åkerman, K.E.O.5
  • 10
    • 0027304836 scopus 로고
    • Protein kinase C-α but not protein kinase C-ε is differentially down-regulated by bryostatin 1 and tetradecanoyl phorbol-13-acetate in SH-SY5Y human neuroblastoma cells
    • Jalava A., Lintunen M., and Heikkilä J. (1993) Protein kinase C-α but not protein kinase C-ε is differentially down-regulated by bryostatin 1 and tetradecanoyl phorbol-13-acetate in SH-SY5Y human neuroblastoma cells. Biochem. Biophys. Res. Commun. 191, 472-478.
    • (1993) Biochem. Biophys. Res. Commun. , vol.191 , pp. 472-478
    • Jalava, A.1    Lintunen, M.2    Heikkilä, J.3
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0025060264 scopus 로고
    • 2+ and inositol 1,4,5-trisphosphate mass in a human neuroblastoma cell line, SH-SY5Y
    • 2+ and inositol 1,4,5-trisphosphate mass in a human neuroblastoma cell line, SH-SY5Y. Biochem. J. 265, 555-562.
    • (1990) Biochem. J. , vol.265 , pp. 555-562
    • Lambert, D.G.1    Nahorski, S.R.2
  • 14
    • 0028358814 scopus 로고
    • Inhibition of intercellular communication of rat hepatocytes by nafenopin: Involvement of protein kinase C
    • Leibold E., Greim H., and Schwarz L. R. (1994) Inhibition of intercellular communication of rat hepatocytes by nafenopin: involvement of protein kinase C. Carcinogenesis 15, 1265-1269.
    • (1994) Carcinogenesis , vol.15 , pp. 1265-1269
    • Leibold, E.1    Greim, H.2    Schwarz, L.R.3
  • 16
    • 0023091203 scopus 로고
    • Down regulation of protein kinase C in neuronal cells: Effects on neurotransmitter release
    • Matthies H. J. G., Palfrey H. C., Hirning L. D., and Miller R. J. (1987) Down regulation of protein kinase C in neuronal cells: effects on neurotransmitter release. J. Neurosci. 7, 1198-1206.
    • (1987) J. Neurosci. , vol.7 , pp. 1198-1206
    • Matthies, H.J.G.1    Palfrey, H.C.2    Hirning, L.D.3    Miller, R.J.4
  • 17
    • 0027953598 scopus 로고
    • Staurosporine-induced reduction in secretory function in cultured bovine adrenal chromaffin cells
    • Maurer J. A. and McKay D. B. (1994) Staurosporine-induced reduction in secretory function in cultured bovine adrenal chromaffin cells. Eur. J. Pharmacol. 253, 115-124.
    • (1994) Eur. J. Pharmacol. , vol.253 , pp. 115-124
    • Maurer, J.A.1    McKay, D.B.2
  • 19
    • 0027208282 scopus 로고
    • Inhibition by Ro 31-8220 of acid secretory activity induced by carbachol indicates a stimulatory role for protein kinase C in the action of muscarinic agonists on isolated rat parietal cells
    • McKenna J. P. and Hanson P. J. (1993) Inhibition by Ro 31-8220 of acid secretory activity induced by carbachol indicates a stimulatory role for protein kinase C in the action of muscarinic agonists on isolated rat parietal cells. Biochem. Pharmacol. 46, 583-588.
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 583-588
    • McKenna, J.P.1    Hanson, P.J.2
  • 21
    • 0025880843 scopus 로고
    • The cholinergic regulation of intracellular calcium in the human neuroblastoma, SH-SY5Y
    • Murphy N. P., Vaughan P. F. T., Ball S. G., and McCormack J. G. (1991b) The cholinergic regulation of intracellular calcium in the human neuroblastoma, SH-SY5Y. J. Neurochem. 57, 2116-2123.
    • (1991) J. Neurochem. , vol.57 , pp. 2116-2123
    • Murphy, N.P.1    Vaughan, P.F.T.2    Ball, S.G.3    McCormack, J.G.4
  • 23
    • 0344245863 scopus 로고
    • Induction of exocytosis in permeabilized pituitary cells by α- and β-type protein kinase C
    • Naor Z., Dan-Cohen H., Hermon J., and Limor R. (1989) Induction of exocytosis in permeabilized pituitary cells by α- and β-type protein kinase C. Proc. Natl. Acad. Sci. USA 86, 4501-4504.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4501-4504
    • Naor, Z.1    Dan-Cohen, H.2    Hermon, J.3    Limor, R.4
  • 24
    • 0023139527 scopus 로고
    • Phorbol ester enhancement of neurotransmitter release from rat brain synaptosomes
    • Nichols R. A., Haycock J. W., Wang J. K. T., and Greengard P. (1987) Phorbol ester enhancement of neurotransmitter release from rat brain synaptosomes. J. Neurochem. 48, 615-621.
    • (1987) J. Neurochem. , vol.48 , pp. 615-621
    • Nichols, R.A.1    Haycock, J.W.2    Wang, J.K.T.3    Greengard, P.4
  • 25
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y. (1992) Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 258, 607-614.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 26
    • 0025963046 scopus 로고
    • Synaptosomal protein kinase C subspecies: B. Down-regulation promoted by phorbol ester and its effect on evoked norepinephrine release
    • Oda T., Shearman M. S., and Nishizuka Y. (1991) Synaptosomal protein kinase C subspecies: B. Down-regulation promoted by phorbol ester and its effect on evoked norepinephrine release. J. Neurochem. 56, 1263-1269.
    • (1991) J. Neurochem. , vol.56 , pp. 1263-1269
    • Oda, T.1    Shearman, M.S.2    Nishizuka, Y.3
  • 28
    • 0028986467 scopus 로고
    • 2+ channel currents in human neuroblastoma (SH-SY5Y) cells by phorbol esters with and without activation of protein kinase C
    • 2+ channel currents in human neuroblastoma (SH-SY5Y) cells by phorbol esters with and without activation of protein kinase C. Pflugers Arch. 429, 729-737.
    • (1995) Pflugers Arch. , vol.429 , pp. 729-737
    • Reeve, H.L.1    Vaughan, P.F.T.2    Peers, C.3
  • 29
    • 0026291394 scopus 로고
    • The role of protein kinase C and its neuronal substrates dephosphin, B-50, and MARCKS in neurotransmitter release
    • Robinson P. J. (1991) The role of protein kinase C and its neuronal substrates dephosphin, B-50, and MARCKS in neurotransmitter release. Mol. Neurobiol. 5, 87-130.
    • (1991) Mol. Neurobiol. , vol.5 , pp. 87-130
    • Robinson, P.J.1
  • 30
    • 0027431089 scopus 로고
    • Molecular cloning and characterization of PKCι, an atypical isoform of protein kinase C derived from insulin-secreting cells
    • Selbie L. A., Schmitz-Peiffer C., Sheng Y., and Biden T. J. (1993) Molecular cloning and characterization of PKCι, an atypical isoform of protein kinase C derived from insulin-secreting cells. J. Biol. Chem. 268, 24296-24302.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24296-24302
    • Selbie, L.A.1    Schmitz-Peiffer, C.2    Sheng, Y.3    Biden, T.J.4
  • 31
    • 0025610723 scopus 로고
    • Activation of protein kinase C is not required for exocytosis from bovine adrenal chromaffin cells
    • Terbush D. R. and Holz R. W. (1990) Activation of protein kinase C is not required for exocytosis from bovine adrenal chromaffin cells. J. Biol. Chem. 265, 21179-21184.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21179-21184
    • Terbush, D.R.1    Holz, R.W.2
  • 33
    • 0027191102 scopus 로고
    • Nicotinic receptor-mediated release of noradrenaline in the human neuroblastoma SH-SY5Y
    • Vaughan P. F. T., Kaye D. F., Reeve H. L., Ball S. G., and Peers C. (1993) Nicotinic receptor-mediated release of noradrenaline in the human neuroblastoma SH-SY5Y. J. Neurochem. 60, 2159-2166.
    • (1993) J. Neurochem. , vol.60 , pp. 2159-2166
    • Vaughan, P.F.T.1    Kaye, D.F.2    Reeve, H.L.3    Ball, S.G.4    Peers, C.5
  • 34
    • 0026539999 scopus 로고
    • Protein kinase C activation by phorbol esters induces chromaffin cell cortical filamentous actin disassembly and increases the initial rate of exocytosis in response to nicotinic receptor stimulation
    • Vitale M. L., Rodríguez Del Castillo A., and Trifaró J.-M (1992) Protein kinase C activation by phorbol esters induces chromaffin cell cortical filamentous actin disassembly and increases the initial rate of exocytosis in response to nicotinic receptor stimulation. Neuroscience 51, 463-474.
    • (1992) Neuroscience , vol.51 , pp. 463-474
    • Vitale, M.L.1    Rodríguez Del Castillo, A.2    Trifaró, J.-M.3
  • 35
    • 0028840159 scopus 로고
    • Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis
    • Vitale M. L., Seward E. P., and Trifaró J.-M. (1995) Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis. Neuron 14, 353-363.
    • (1995) Neuron , vol.14 , pp. 353-363
    • Vitale, M.L.1    Seward, E.P.2    Trifaró, J.-M.3
  • 36
    • 0026702507 scopus 로고
    • Effect of phorbol esters on protein kinase C-ζ
    • Ways D. K., Cook P. P., Webster C., and Parker P. J. (1992) Effect of phorbol esters on protein kinase C-ζ. J. Biol. Chem. 267, 4799-4805.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4799-4805
    • Ways, D.K.1    Cook, P.P.2    Webster, C.3    Parker, P.J.4
  • 37
    • 0027248964 scopus 로고
    • Isoenzyme specificity of bisindolylmaleimides, selective inhibitors of protein kinase C
    • Wilkinson S. E., Parker P. J., and Nixon J. S. (1993) Isoenzyme specificity of bisindolylmaleimides, selective inhibitors of protein kinase C. Biochem. J. 294, 335-337.
    • (1993) Biochem. J. , vol.294 , pp. 335-337
    • Wilkinson, S.E.1    Parker, P.J.2    Nixon, J.S.3
  • 38
    • 0023655187 scopus 로고
    • Down-regulation of protein kinase C is due to an increased rate of degradation
    • Young S., Parker P. J., Ullrich A., and Stabel S. (1987) Down-regulation of protein kinase C is due to an increased rate of degradation. Biochem. J. 244, 775-779.
    • (1987) Biochem. J. , vol.244 , pp. 775-779
    • Young, S.1    Parker, P.J.2    Ullrich, A.3    Stabel, S.4


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