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Volumn 95, Issue 3, 2000, Pages 894-902

Platelet secretion induced by phorbol esters stimulation is mediated through phosphorylation of MARCKS: A MARCKS-derived peptide blocks MARCKS phosphorylation and serotonin release without affecting pleckstrin phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

MARCKS PROTEIN; PHORBOL ESTER; PLECKSTRIN; PROTEIN KINASE C; SEROTONIN;

EID: 0034141835     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v95.3.894.003k15_894_902     Document Type: Article
Times cited : (68)

References (46)
  • 1
    • 0024532116 scopus 로고
    • Molecular mechanisms of platelet activation
    • Siess W. Molecular mechanisms of platelet activation. Physiol Rev. 1989;69:58.
    • (1989) Physiol Rev , vol.69 , pp. 58
    • Siess, W.1
  • 2
    • 0028292046 scopus 로고
    • Platelet activation and inhibition. Novel signal transduction mechanisms
    • Peterson SN, Lapetina EG. Platelet activation and inhibition. Novel signal transduction mechanisms. Ann N Y Acad Sci. 1994;714:53.
    • (1994) Ann N Y Acad Sci , vol.714 , pp. 53
    • Peterson, S.N.1    Lapetina, E.G.2
  • 4
    • 0020184672 scopus 로고
    • Separable assembly of platelet pseudopodal and contractile cytoskeletons
    • Carroll RC, Bitler RC, Morris PA. Separable assembly of platelet pseudopodal and contractile cytoskeletons. Cell. 1982;30:385.
    • (1982) Cell , vol.30 , pp. 385
    • Carroll, R.C.1    Bitler, R.C.2    Morris, P.A.3
  • 5
    • 0019870606 scopus 로고
    • The cytoskeleton of blood platelets viewed by immunofluorescence microscopy
    • Debus I, Weber K, Osborn M. The cytoskeleton of blood platelets viewed by immunofluorescence microscopy. Eur J Cell Biol. 1981;24:45.
    • (1981) Eur J Cell Biol , vol.24 , pp. 45
    • Debus, I.1    Weber, K.2    Osborn, M.3
  • 6
    • 0021366581 scopus 로고
    • Recycling of platelet phosphorylation and cytoskeletal assembly
    • Cox AC, Carroll RC, White JG, Rao GHR. Recycling of platelet phosphorylation and cytoskeletal assembly. J Cell Biol. 1984;98:8.
    • (1984) J Cell Biol , vol.98 , pp. 8
    • Cox, A.C.1    Carroll, R.C.2    White, J.G.3    Rao, G.H.R.4
  • 7
    • 0028237313 scopus 로고
    • Regulated membrane cytoskeleton linkages in platelets
    • Bertagnolli ME, Beckerle MC. Regulated membrane cytoskeleton linkages in platelets. Ann N Y Acad Sci. 1994;714:88.
    • (1994) Ann N Y Acad Sci , vol.714 , pp. 88
    • Bertagnolli, M.E.1    Beckerle, M.C.2
  • 8
    • 0019945873 scopus 로고
    • Association of coagulation factor V with the platelet cytoskeleton
    • Tuszynski GP, Walsh PN, Piperno JR, Kosshy A. Association of coagulation factor V with the platelet cytoskeleton. J Biol Chem. 1982;257:4557.
    • (1982) J Biol Chem , vol.257 , pp. 4557
    • Tuszynski, G.P.1    Walsh, P.N.2    Piperno, J.R.3    Kosshy, A.4
  • 9
    • 0023666065 scopus 로고
    • Integrins: A family of cell surface receptors
    • Hynes RO. Integrins: a family of cell surface receptors. Cell. 1987;48:549.
    • (1987) Cell , vol.48 , pp. 549
    • Hynes, R.O.1
  • 10
    • 0019978065 scopus 로고
    • Human platelets contain gelsolin: A regulator of actin filament length
    • Lind SE, Yin HL, Stossel TP. Human platelets contain gelsolin: a regulator of actin filament length. J Clin Invest. 1982;69:1384.
    • (1982) J Clin Invest , vol.69 , pp. 1384
    • Lind, S.E.1    Yin, H.L.2    Stossel, T.P.3
  • 13
    • 0030029849 scopus 로고    scopus 로고
    • Recombinant scinderin, an F-actin severing protein, increases calcium-induced release of serotonin from permeabilized platelets, an effect blocked by two scinderin-derived actin-binding peptides and phosphatidylinositol 4,5-bisphosphate
    • Marcu MG, Zhang L, Nau-Staudt K, Trifaró J-M. Recombinant scinderin, an F-actin severing protein, increases calcium-induced release of serotonin from permeabilized platelets, an effect blocked by two scinderin-derived actin-binding peptides and phosphatidylinositol 4,5-bisphosphate. Blood. 1996;87:20.
    • (1996) Blood , vol.87 , pp. 20
    • Marcu, M.G.1    Zhang, L.2    Nau-Staudt, K.3    Trifaró, J.-M.4
  • 14
    • 0025840196 scopus 로고
    • Cortical filamentous actin disassembly and scinderin redistribution during chromaffin cell stimulation precede exocytosis, a phenomenon not exhibited by gelsolin
    • Vitale ML, Rodríguez Del Castillo A, Tchakarov L, Trifaró J-M. Cortical filamentous actin disassembly and scinderin redistribution during chromaffin cell stimulation precede exocytosis, a phenomenon not exhibited by gelsolin. J Cell Biol. 1991; 113:1057.
    • (1991) J Cell Biol , vol.113 , pp. 1057
    • Vitale, M.L.1    Rodríguez Del Castillo, A.2    Tchakarov, L.3    Trifaró, J.-M.4
  • 15
    • 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 ML, Seward EP, Trifaró J-M. Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis. Neuron. 1995;14:353.
    • (1995) Neuron , vol.14 , pp. 353
    • Vitale, M.L.1    Seward, E.P.2    Trifaró, J.-M.3
  • 16
    • 0025238866 scopus 로고
    • Platelet protein phosphorylation and protein kinase C activation by phorbol esters with different biological activity and a novel synergistic response with Ca2+ ionophore
    • Brooks SF, Gordge PC, Toker A, Evans AT, Evans FJ, Aitken A. Platelet protein phosphorylation and protein kinase C activation by phorbol esters with different biological activity and a novel synergistic response with Ca2+ ionophore. Eur J Biochem. 1990;188:431.
    • (1990) Eur J Biochem , vol.188 , pp. 431
    • Brooks, S.F.1    Gordge, P.C.2    Toker, A.3    Evans, A.T.4    Evans, F.J.5    Aitken, A.6
  • 17
    • 0029657940 scopus 로고    scopus 로고
    • Correlation between cytosolic Ca2+ concentration, protein phosphorylation and platelet secretion
    • Dalla Via L, Stimamiglio M, Scapin M, Cesaro L, Deana R. Correlation between cytosolic Ca2+ concentration, protein phosphorylation and platelet secretion. Cell Calcium. 1996;20:431.
    • (1996) Cell Calcium , vol.20 , pp. 431
    • Dalla Via, L.1    Stimamiglio, M.2    Scapin, M.3    Cesaro, L.4    Deana, R.5
  • 18
    • 0001673324 scopus 로고    scopus 로고
    • Collagen-induced secretion-dependent phase of platelet aggregation is inhibited by the snake venom metalloproteinase jararhagin
    • Kamiguti AS, Moura-da-Silva AM, Laing GD, et al. Collagen-induced secretion-dependent phase of platelet aggregation is inhibited by the snake venom metalloproteinase jararhagin. Biochim Biophys Acta. 1997;1335:209.
    • (1997) Biochim Biophys Acta , vol.1335 , pp. 209
    • Kamiguti, A.S.1    Moura-da-Silva, A.M.2    Laing, G.D.3
  • 19
    • 0030819938 scopus 로고    scopus 로고
    • Different requirement of intracellular calcium and protein kinase C for arachidonic acid release and serotonin secretion in cathepsin G-activated platelets
    • Rotondo S, Evangelista V, Manarini S, de Gaetano G, Cerletti C. Different requirement of intracellular calcium and protein kinase C for arachidonic acid release and serotonin secretion in cathepsin G-activated platelets. Thromb Haemost. 1997;78:919.
    • (1997) Thromb Haemost , vol.78 , pp. 919
    • Rotondo, S.1    Evangelista, V.2    Manarini, S.3    De Gaetano, G.4    Cerletti, C.5
  • 20
    • 0030699914 scopus 로고    scopus 로고
    • Protein kinase C-dependent and Ca2+-dependent mechanisms of secretion from streptolysin O-permeabilized platelets: Effects of leakage of cytosolic proteins
    • Sloan DA, Haslam RJ. Protein kinase C-dependent and Ca2+-dependent mechanisms of secretion from streptolysin O-permeabilized platelets: effects of leakage of cytosolic proteins. Biochem J. 1997;328:13.
    • (1997) Biochem J , vol.328 , pp. 13
    • Sloan, D.A.1    Haslam, R.J.2
  • 21
    • 0021149043 scopus 로고
    • Potentiation by thrombin of the secretion of serotonin from permeabilized platelets equilibrated with Ca2+ buffers: Relationship to protein phosphorylalion and diacylglycerol formation
    • Haslam RJ, Davidson ML. Potentiation by thrombin of the secretion of serotonin from permeabilized platelets equilibrated with Ca2+ buffers: relationship to protein phosphorylalion and diacylglycerol formation. Biochem J. 1984;222: 351.
    • (1984) Biochem J , vol.222 , pp. 351
    • Haslam, R.J.1    Davidson, M.L.2
  • 22
    • 0028788181 scopus 로고
    • Phosphorylation of the platelet p47 phosphoprotein is mediated by the lipid products of phosphoinositide 3-kinase
    • Toker A, Bachelot C, Chen C-S, et al. Phosphorylation of the platelet p47 phosphoprotein is mediated by the lipid products of phosphoinositide 3-kinase. J Biol Chem. 1995;270:29,525.
    • (1995) J Biol Chem , vol.270
    • Toker, A.1    Bachelot, C.2    Chen, C.-S.3
  • 23
    • 0028232694 scopus 로고
    • Protein kinase C-dependent and -independent mechanisms of dense granule exocytosis by human platelets
    • Hashimoto Y, Togo M, Tsukamoto K, Horie Y, Watanabe T, Kurokawa K. Protein kinase C-dependent and -independent mechanisms of dense granule exocytosis by human platelets. Biochim Biophys Acta. 1994;1222:56.
    • (1994) Biochim Biophys Acta , vol.1222 , pp. 56
    • Hashimoto, Y.1    Togo, M.2    Tsukamoto, K.3    Horie, Y.4    Watanabe, T.5    Kurokawa, K.6
  • 24
    • 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 ML, Rodríguez Del Castillo A, Trifaró J-M. 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. 1992;51:463.
    • (1992) Neuroscience , vol.51 , pp. 463
    • Vitale, M.L.1    Rodríguez Del Castillo, A.2    Trifaró, J.-M.3
  • 25
    • 0026513601 scopus 로고
    • MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin
    • Hartwig JH, Thelen M, Rosen A, Janmey PA, Nairn AC, Aderem A. MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin. Nature. 1992; 356:618.
    • (1992) Nature , vol.356 , pp. 618
    • Hartwig, J.H.1    Thelen, M.2    Rosen, A.3    Janmey, P.A.4    Nairn, A.C.5    Aderem, A.6
  • 26
    • 0026639826 scopus 로고
    • Signal transduction and the actin cytoskeleton: The roles of MARCKS and profilin
    • Aderem A. Signal transduction and the actin cytoskeleton: the roles of MARCKS and profilin. Trends Biochem Sci. 1992;17:438.
    • (1992) Trends Biochem Sci , vol.17 , pp. 438
    • Aderem, A.1
  • 27
    • 0018733531 scopus 로고
    • Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • Fabiato M, Fabiato F. Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. J Physiol. 1979;75:463.
    • (1979) J Physiol , vol.75 , pp. 463
    • Fabiato, M.1    Fabiato, F.2
  • 28
    • 12944288138 scopus 로고    scopus 로고
    • Measurement of protein phosphorylation, kinase activity, and G protein function in intact platelets and membrane preparations
    • Watson SP, Authi KS, eds. Oxford, England: Oxford University Press
    • Wadman IA, Virdee K, Fernández DS, Wasunna CL, Farnale RW. Measurement of protein phosphorylation, kinase activity, and G protein function in intact platelets and membrane preparations. In: Watson SP, Authi KS, eds. Platelets. Oxford, England: Oxford University Press; 1996:173.
    • (1996) Platelets , pp. 173
    • Wadman, I.A.1    Virdee, K.2    Fernández, D.S.3    Wasunna, C.L.4    Farnale, R.W.5
  • 29
    • 0023953666 scopus 로고
    • A discontinuous lightly porous sodium dodecylsulfate-polyacrylamide slab gel system of high resolution
    • Doucet J-P, Trifaró J-M. A discontinuous lightly porous sodium dodecylsulfate-polyacrylamide slab gel system of high resolution. Anal Biochem. 1988;168:265.
    • (1988) Anal Biochem , vol.168 , pp. 265
    • Doucet, J.-P.1    Trifaró, J.-M.2
  • 30
    • 0026472164 scopus 로고
    • The MARCKS brothers: A family of protein kinase C substrates
    • Aderem A. The MARCKS brothers: a family of protein kinase C substrates. Cell. 1992;71:713.
    • (1992) Cell , vol.71 , pp. 713
    • Aderem, A.1
  • 31
    • 0025828318 scopus 로고
    • Phosphorylation-dependent binding of a synthetic MARCKS peptide to calmodulin
    • McIlroy BK, Walters JD, Blackshear PJ, Johnson JD. Phosphorylation-dependent binding of a synthetic MARCKS peptide to calmodulin. J Biol Chem. 1991;266:4959.
    • (1991) J Biol Chem , vol.266 , pp. 4959
    • McIlroy, B.K.1    Walters, J.D.2    Blackshear, P.J.3    Johnson, J.D.4
  • 32
    • 10244224044 scopus 로고    scopus 로고
    • Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4,5-Bisphosphate in lateral domains
    • Glasen M, Wanaski S, Buser A, et al. Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4,5-Bisphosphate in lateral domains. J Biol Chem. 1996;271:26,187.
    • (1996) J Biol Chem , vol.271
    • Glasen, M.1    Wanaski, S.2    Buser, A.3
  • 33
    • 0020183576 scopus 로고
    • Calcium/phospholipid regulates phosphorylation of a Mr "87k" Substrate protein in brain synaptosomes
    • Wu WC-S, Walaas SI, Nair AC, Greengard P. Calcium/phospholipid regulates phosphorylation of a Mr "87k" Substrate protein in brain synaptosomes. Proc Natl Acad Sci U S A. 1982;79:5249.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 5249
    • Wu, W.C.-S.1    Walaas, S.I.2    Nair, A.C.3    Greengard, P.4
  • 34
    • 0003474551 scopus 로고
    • Phosphorylation and associated translocation of the 87-kDa protein, a major protein kinase C substrate, in isolated nerve terminals
    • Wang JKT, Walaas SI, Sihra TS, Aderem A, Greengard P. Phosphorylation and associated translocation of the 87-kDa protein, a major protein kinase C substrate, in isolated nerve terminals. Proc Natl Acad Sci U S A. 1989;86:2253.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 2253
    • Wang, J.K.T.1    Walaas, S.I.2    Sihra, T.S.3    Aderem, A.4    Greengard, P.5
  • 35
    • 0026644057 scopus 로고
    • Glucose-induced phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) in isolated rat pancreatic islets
    • Calle R, Ganesan S, Smallwood JI, Rasmussen H. Glucose-induced phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) in isolated rat pancreatic islets. J Biol Chem. 1992;267:18,723.
    • (1992) J Biol Chem , vol.267
    • Calle, R.1    Ganesan, S.2    Smallwood, J.I.3    Rasmussen, H.4
  • 36
    • 0028102254 scopus 로고
    • Glutamate exocytosis and MARCKS phosphorylation are enhanced by a metabotropic glutamate receptor coupled to a protein kinase C synergistically activated by diacylglycerol and arachidonic acid
    • Coffey ET, Herrero I, Sihra TS, Sánchez-Prieto J, Nicholls DG. Glutamate exocytosis and MARCKS phosphorylation are enhanced by a metabotropic glutamate receptor coupled to a protein kinase C synergistically activated by diacylglycerol and arachidonic acid. J Neurochem. 1994;63:1303.
    • (1994) J Neurochem , vol.63 , pp. 1303
    • Coffey, E.T.1    Herrero, I.2    Sihra, T.S.3    Sánchez-Prieto, J.4    Nicholls, D.G.5
  • 37
    • 0028061890 scopus 로고
    • Arginine vasopressin (AVP) causes the reversible phosphorylation of the myristoylated alanine-rich C kinase substrate (MARCKS) protein in the ovine anterior pituitary: Evidence that MARCKS phosphorylation is associated with adrenocorticotropin (ACTH) secretion
    • Liu J-P, Engler D, Funder JW, Robinson PJ. Arginine vasopressin (AVP) causes the reversible phosphorylation of the myristoylated alanine-rich C kinase substrate (MARCKS) protein in the ovine anterior pituitary: evidence that MARCKS phosphorylation is associated with adrenocorticotropin (ACTH) secretion. Mol Cell Endocrinol. 1994;105:217.
    • (1994) Mol Cell Endocrinol , vol.105 , pp. 217
    • Liu, J.-P.1    Engler, D.2    Funder, J.W.3    Robinson, P.J.4
  • 38
    • 0031018777 scopus 로고    scopus 로고
    • Activation of protein kinase C-alpha and translocation of the myristoylated alanine-rich C-kinase substrate correlate with phorbol ester-enhanced noradrenaline release from SH-SY5Y human neuroblastoma cells
    • Goodall AR, Turner NA, Walker JH, Ball SG, Vaughan PF. Activation of protein kinase C-alpha and translocation of the myristoylated alanine-rich C-kinase substrate correlate with phorbol ester-enhanced noradrenaline release from SH-SY5Y human neuroblastoma cells. J Neurochem. 1997;68:392.
    • (1997) J Neurochem , vol.68 , pp. 392
    • Goodall, A.R.1    Turner, N.A.2    Walker, J.H.3    Ball, S.G.4    Vaughan, P.F.5
  • 39
    • 0019226552 scopus 로고
    • 2+-calmodulin-dependent phosphorylation and platelet secretion
    • 2+-calmodulin-dependent phosphorylation and platelet secretion. Nature. 1980;287:863.
    • (1980) Nature , vol.287 , pp. 863
    • Nishikawa, M.1    Tanaka, T.2    Hidaka, H.3
  • 40
    • 0025306169 scopus 로고
    • Phosphorylation of bovine platelet myosin by protein kinase C
    • Ikebe M, Reardon S. Phosphorylation of bovine platelet myosin by protein kinase C. Biochemistry. 1990;29:2713.
    • (1990) Biochemistry , vol.29 , pp. 2713
    • Ikebe, M.1    Reardon, S.2
  • 41
    • 0030220340 scopus 로고    scopus 로고
    • Recombinant scinderin enhances exocytosis, an effect blocked by two scinderin-derived actin-binding peptides and PIP2
    • Zhang L, Marcu MG, Nau-Staudt K, Trifaró J-M. Recombinant scinderin enhances exocytosis, an effect blocked by two scinderin-derived actin-binding peptides and PIP2. Neuron. 1996;17:287.
    • (1996) Neuron , vol.17 , pp. 287
    • Zhang, L.1    Marcu, M.G.2    Nau-Staudt, K.3    Trifaró, J.-M.4
  • 42
    • 0030670913 scopus 로고    scopus 로고
    • The cortical actin cytoskeleton of lactotropes as an intracellular target for the control of prolactin secretion
    • Carbajal ME, Vitale ML. The cortical actin cytoskeleton of lactotropes as an intracellular target for the control of prolactin secretion. Endocrinology. 1997;138:5374.
    • (1997) Endocrinology , vol.138 , pp. 5374
    • Carbajal, M.E.1    Vitale, M.L.2
  • 44
    • 0005796679 scopus 로고    scopus 로고
    • Chromaffin cell F-actin disassembly in response to PKC activation by phorbol esters is mediated through MARCKS
    • Sapporo, Japan May 26-30
    • Rosé SD, Zhang L, Trifaró J-M. Chromaffin cell F-actin disassembly in response to PKC activation by phorbol esters is mediated through MARCKS. In: 9th Int Sympon Chromaffin Cell Biology. Sapporo, Japan May 26-30: 1997;155.
    • (1997) 9th Int Sympon Chromaffin Cell Biology , pp. 155
    • Rosé, S.D.1    Zhang, L.2    Trifaró, J.-M.3
  • 45
    • 0025096430 scopus 로고
    • Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage filopodia
    • Rosen A, Keenan KF, Thelen M, Nairn AC, Aderem AA. Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage filopodia. J Exp Med. 1990;172:1211.
    • (1990) J Exp Med , vol.172 , pp. 1211
    • Rosen, A.1    Keenan, K.F.2    Thelen, M.3    Nairn, A.C.4    Aderem, A.A.5
  • 46
    • 0032488841 scopus 로고    scopus 로고
    • Localization by segmental deletion analysis and functional characterization of a third actin-binding site in domain 5 of scinderin
    • Marcu MG, Zhang L, Elzagallaai A, Trifaró J-M. Localization by segmental deletion analysis and functional characterization of a third actin-binding site in domain 5 of scinderin. J Biol Chem. 1998; 273:3661.
    • (1998) J Biol Chem , vol.273 , pp. 3661
    • Marcu, M.G.1    Zhang, L.2    Elzagallaai, A.3    Trifaró, J.-M.4


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