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Volumn 5, Issue 10, 2005, Pages 1507-1518

The use of okadaic acid to elucidate the intracellular role(s) of protein phosphatase 2A: Lessons from the mast cell model system

Author keywords

Cytokine synthesis; Granule exocytosis; Prostaglandin leukotriene synthesis; Serine threonine phosphatase

Indexed keywords

AUTACOID; FC RECEPTOR; IMMUNOGLOBULIN E; OKADAIC ACID; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN SERINE THREONINE KINASE; TUMOR PROMOTER;

EID: 22044432763     PISSN: 15675769     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.intimp.2005.05.007     Document Type: Review
Times cited : (26)

References (81)
  • 1
    • 0019443232 scopus 로고
    • Okadaic acid, a cytotoxic polyether from two marine sponges of the genus Halichondria
    • K. Tachibana, P.J. Scheuer, Y. Tsukitani, H. Kikuchi, D. Van Engen, and J. Clardy Okadaic acid, a cytotoxic polyether from two marine sponges of the genus Halichondria J Am Chem Soc 103 9 1981 2469 2471
    • (1981) J Am Chem Soc , vol.103 , Issue.9 , pp. 2469-2471
    • Tachibana, K.1    Scheuer, P.J.2    Tsukitani, Y.3    Kikuchi, H.4    Van Engen, D.5    Clardy, J.6
  • 2
    • 0022650550 scopus 로고
    • Synthetic studies toward marine toxic polyethers [5]. the total synthesis of okadaic acid
    • M. Isobe, Y. Ichikawa, and T. Goto Synthetic studies toward marine toxic polyethers [5]. The total synthesis of okadaic acid Tetrahedron Lett 27 8 1986 963 966
    • (1986) Tetrahedron Lett , vol.27 , Issue.8 , pp. 963-966
    • Isobe, M.1    Ichikawa, Y.2    Goto, T.3
  • 3
    • 0036032442 scopus 로고    scopus 로고
    • Okadaic acid: The archetypal serine/threonine protein phosphatase inhibitor
    • A.B. Dounay, and C.J. Forsyth Okadaic acid: the archetypal serine/threonine protein phosphatase inhibitor Curr Med Chem 9 22 2002 1939 1980
    • (2002) Curr Med Chem , vol.9 , Issue.22 , pp. 1939-1980
    • Dounay, A.B.1    Forsyth, C.J.2
  • 4
    • 0001540497 scopus 로고    scopus 로고
    • Biosynthesis of DTX-4: Confirmation of a polyketide pathway, proof of a Baeyer-Villiger oxidation step, and evidence for an unusual carbon deletion process
    • J.L.C. Wright, T. Hu, J.L. McLachlan, J. Needham, and J.A. Walter Biosynthesis of DTX-4: confirmation of a polyketide pathway, proof of a Baeyer-Villiger oxidation step, and evidence for an unusual carbon deletion process J Am Chem Soc 118 36 1996 8757 8758
    • (1996) J Am Chem Soc , vol.118 , Issue.36 , pp. 8757-8758
    • Wright, J.L.C.1    Hu, T.2    McLachlan, J.L.3    Needham, J.4    Walter, J.A.5
  • 5
    • 0025772442 scopus 로고
    • Okadaic acid: A proton and carbon NMR study
    • M. Norte, R. Gonzalez, and J.J. Fernandez Okadaic acid: a proton and carbon NMR study Tetrahedron 47 35 1991 7437 7446
    • (1991) Tetrahedron , vol.47 , Issue.35 , pp. 7437-7446
    • Norte, M.1    Gonzalez, R.2    Fernandez, J.J.3
  • 6
    • 0036378371 scopus 로고    scopus 로고
    • Toxic marine dinoflagellates in Singapore waters that cause seafood poisonings
    • M.J. Holmes, and S.L. Teo Toxic marine dinoflagellates in Singapore waters that cause seafood poisonings Clin Exp Pharmacol Physiol 29 9 2002 829 836
    • (2002) Clin Exp Pharmacol Physiol , vol.29 , Issue.9 , pp. 829-836
    • Holmes, M.J.1    Teo, S.L.2
  • 8
    • 0021227676 scopus 로고
    • The role of protein kinase C in cell surface signal transduction and tumour promotion
    • Y. Nishizuka The role of protein kinase C in cell surface signal transduction and tumour promotion Nature 308 5961 1984 693 698
    • (1984) Nature , vol.308 , Issue.5961 , pp. 693-698
    • Nishizuka, Y.1
  • 9
    • 0023880172 scopus 로고
    • Protein kinase C as the receptor for the phorbol ester tumor promoters: Sixth Rhoads memorial award lecture
    • P.M. Blumberg Protein kinase C as the receptor for the phorbol ester tumor promoters: sixth Rhoads memorial award lecture Cancer Res 48 1 1988 1 8
    • (1988) Cancer Res , vol.48 , Issue.1 , pp. 1-8
    • Blumberg, P.M.1
  • 10
    • 0023691731 scopus 로고
    • Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics
    • C. Bialojan, and A. Takai Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics Biochem J 256 1 1988 283 290
    • (1988) Biochem J , vol.256 , Issue.1 , pp. 283-290
    • Bialojan, C.1    Takai, A.2
  • 11
    • 0023648079 scopus 로고
    • Smooth muscle myosin phosphatase inhibition and force enhancement by black sponge toxin
    • A. Takai, C. Bialojan, M. Troschka, and J.C. Ruegg Smooth muscle myosin phosphatase inhibition and force enhancement by black sponge toxin FEBS Lett 217 1 1987 81 84
    • (1987) FEBS Lett , vol.217 , Issue.1 , pp. 81-84
    • Takai, A.1    Bialojan, C.2    Troschka, M.3    Ruegg, J.C.4
  • 12
    • 0037085442 scopus 로고    scopus 로고
    • Protein phosphatase 2A and protein kinase Calpha are physically associated and are involved in Pseudomonas aeruginosa-induced interleukin 6 production by mast cells
    • R.T. Boudreau, R. Garduno, and T.J. Lin Protein phosphatase 2A and protein kinase Calpha are physically associated and are involved in Pseudomonas aeruginosa-induced interleukin 6 production by mast cells J Biol Chem 277 7 2002 5322 5329
    • (2002) J Biol Chem , vol.277 , Issue.7 , pp. 5322-5329
    • Boudreau, R.T.1    Garduno, R.2    Lin, T.J.3
  • 13
    • 0030804330 scopus 로고    scopus 로고
    • Inhibition of the Ser-Thr phosphatases PP1 and PP2A by naturally occurring toxins
    • J.E. Sheppeck II, C.M. Gauss, and A.R. Chamberlin Inhibition of the Ser-Thr phosphatases PP1 and PP2A by naturally occurring toxins Bioorg Med Chem 5 9 1997 1739 1750
    • (1997) Bioorg Med Chem , vol.5 , Issue.9 , pp. 1739-1750
    • Sheppeck II, J.E.1    Gauss, C.M.2    Chamberlin, A.R.3
  • 14
    • 0037075845 scopus 로고    scopus 로고
    • Serine-threonine protein phosphatase inhibitors: Development of potential therapeutic strategies
    • A. McCluskey, A.T. Sim, and J.A. Sakoff Serine-threonine protein phosphatase inhibitors: development of potential therapeutic strategies J Med Chem 45 6 2002 1151 1175
    • (2002) J Med Chem , vol.45 , Issue.6 , pp. 1151-1175
    • McCluskey, A.1    Sim, A.T.2    Sakoff, J.A.3
  • 16
    • 0036032778 scopus 로고    scopus 로고
    • Regulators of serine/threonine protein phosphatases at the dawn of a clinical era?
    • R.E. Honkanen, and T. Golden Regulators of serine/threonine protein phosphatases at the dawn of a clinical era? Curr Med Chem 9 22 2002 2055 2075
    • (2002) Curr Med Chem , vol.9 , Issue.22 , pp. 2055-2075
    • Honkanen, R.E.1    Golden, T.2
  • 17
    • 0020540151 scopus 로고
    • The protein phosphatases involved in cellular regulation: 1. Classification and substrate specificities
    • T.S. Ingebritsen, and P. Cohen The protein phosphatases involved in cellular regulation: 1. Classification and substrate specificities Eur J Biochem 132 2 1983 255 261
    • (1983) Eur J Biochem , vol.132 , Issue.2 , pp. 255-261
    • Ingebritsen, T.S.1    Cohen, P.2
  • 18
    • 0020565637 scopus 로고
    • Protein phosphatases: Properties and role in cellular regulation
    • T.S. Ingebritsen, and P. Cohen Protein phosphatases: properties and role in cellular regulation Science 221 4608 1983 331 338
    • (1983) Science , vol.221 , Issue.4608 , pp. 331-338
    • Ingebritsen, T.S.1    Cohen, P.2
  • 19
    • 0032577483 scopus 로고    scopus 로고
    • Regulation of the calmodulin-stimulated protein phosphatase, calcineurin
    • C.B. Klee, H. Ren, and X. Wang Regulation of the calmodulin-stimulated protein phosphatase, calcineurin J Biol Chem 273 22 1998 13367 13370
    • (1998) J Biol Chem , vol.273 , Issue.22 , pp. 13367-13370
    • Klee, C.B.1    Ren, H.2    Wang, X.3
  • 20
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • V. Janssens, and J. Goris Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling Biochem J 353 Pt 3 2001 417 439
    • (2001) Biochem J , vol.353 , Issue.3 PART , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 21
    • 0031860103 scopus 로고    scopus 로고
    • The structure and mechanism of protein phosphatases: Insights into catalysis and regulation
    • D. Barford, A.K. Das, and M.P. Egloff The structure and mechanism of protein phosphatases: insights into catalysis and regulation Annu Rev Biophys Biomol Struct 27 1998 133 164
    • (1998) Annu Rev Biophys Biomol Struct , vol.27 , pp. 133-164
    • Barford, D.1    Das, A.K.2    Egloff, M.P.3
  • 22
    • 0024792262 scopus 로고
    • Protein phosphatases come of age
    • P. Cohen, and P.T. Cohen Protein phosphatases come of age J Biol Chem 264 36 1989 21435 21438
    • (1989) J Biol Chem , vol.264 , Issue.36 , pp. 21435-21438
    • Cohen, P.1    Cohen, P.T.2
  • 23
    • 0032159462 scopus 로고    scopus 로고
    • Physiologic importance of protein phosphatase inhibitors
    • C.J. Oliver, and S. Shenolikar Physiologic importance of protein phosphatase inhibitors Front Biosci 3 1998 D961 D972
    • (1998) Front Biosci , vol.3
    • Oliver, C.J.1    Shenolikar, S.2
  • 24
    • 0033141686 scopus 로고    scopus 로고
    • Molecular evolution of type 1 serine/threonine protein phosphatases
    • Q. Lin, Est. Buckler, S.V. Muse, and J.C. Walker Molecular evolution of type 1 serine/threonine protein phosphatases Mol Phylogenet Evol 12 1 1999 57 66
    • (1999) Mol Phylogenet Evol , vol.12 , Issue.1 , pp. 57-66
    • Lin, Q.1    Buckler, Est.2    Muse, S.V.3    Walker, J.C.4
  • 26
    • 0031017969 scopus 로고    scopus 로고
    • Separation of PP2A core enzyme and holoenzyme with monoclonal antibodies against the regulatory a subunit: Abundant expression of both forms in cells
    • E. Kremmer, K. Ohst, J. Kiefer, N. Brewis, and G. Walter Separation of PP2A core enzyme and holoenzyme with monoclonal antibodies against the regulatory A subunit: abundant expression of both forms in cells Mol Cell Biol 17 3 1997 1692 1701
    • (1997) Mol Cell Biol , vol.17 , Issue.3 , pp. 1692-1701
    • Kremmer, E.1    Ohst, K.2    Kiefer, J.3    Brewis, N.4    Walter, G.5
  • 27
    • 0023372798 scopus 로고
    • Molecular cloning and sequence analysis of the catalytic subunit of bovine type 2A protein phosphatase
    • D.D. Green, S.I. Yang, and M.C. Mumby Molecular cloning and sequence analysis of the catalytic subunit of bovine type 2A protein phosphatase Proc Natl Acad Sci U S A 84 14 1987 4880 4884
    • (1987) Proc Natl Acad Sci U S a , vol.84 , Issue.14 , pp. 4880-4884
    • Green, D.D.1    Yang, S.I.2    Mumby, M.C.3
  • 28
    • 0023676445 scopus 로고
    • Tissue-specific expression of mRNAs encoding alpha- and beta-catalytic subunits of protein phosphatase 2A
    • Y. Khew-Goodall, and B.A. Hemmings Tissue-specific expression of mRNAs encoding alpha- and beta-catalytic subunits of protein phosphatase 2A FEBS Lett 238 2 1988 265 268
    • (1988) FEBS Lett , vol.238 , Issue.2 , pp. 265-268
    • Khew-Goodall, Y.1    Hemmings, B.A.2
  • 29
    • 0023748777 scopus 로고
    • Human liver phosphatase 2A: CDNA and amino acid sequence of two catalytic subunit isotypes
    • J. Arino, C.W. Woon, D.L. Brautigan, T.B. Miller Jr., and G.L. Johnson Human liver phosphatase 2A: cDNA and amino acid sequence of two catalytic subunit isotypes Proc Natl Acad Sci U S A 85 12 1988 4252 4256
    • (1988) Proc Natl Acad Sci U S a , vol.85 , Issue.12 , pp. 4252-4256
    • Arino, J.1    Woon, C.W.2    Brautigan, D.L.3    Miller Jr., T.B.4    Johnson, G.L.5
  • 30
    • 0023658640 scopus 로고
    • Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A
    • S.R. Stone, J. Hofsteenge, and B.A. Hemmings Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A Biochemistry 26 23 1987 7215 7220
    • (1987) Biochemistry , vol.26 , Issue.23 , pp. 7215-7220
    • Stone, S.R.1    Hofsteenge, J.2    Hemmings, B.A.3
  • 31
    • 0025313882 scopus 로고
    • Protein serine/threonine phosphatases; An expanding family
    • P.T. Cohen, N.D. Brewis, V. Hughes, and D.J. Mann Protein serine/threonine phosphatases; an expanding family FEBS Lett 268 2 1990 355 359
    • (1990) FEBS Lett , vol.268 , Issue.2 , pp. 355-359
    • Cohen, P.T.1    Brewis, N.D.2    Hughes, V.3    Mann, D.J.4
  • 32
    • 0025275038 scopus 로고
    • Alpha-and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure
    • B.A. Hemmings, C. Adams-Pearson, F. Maurer, P. Muller, J. Goris, and W. Merlevede alpha-and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure Biochemistry 29 13 1990 3166 3173
    • (1990) Biochemistry , vol.29 , Issue.13 , pp. 3166-3173
    • Hemmings, B.A.1    Adams-Pearson, C.2    Maurer, F.3    Muller, P.4    Goris, J.5    Merlevede, W.6
  • 33
    • 0027462533 scopus 로고
    • Analysis of subunit isoforms in protein phosphatase 2A holoenzymes from rabbit and Xenopus
    • P. Hendrix, P. Turowski, R.E. Mayer-Jaekel, J. Goris, J. Hofsteenge, and W. Merlevede Analysis of subunit isoforms in protein phosphatase 2A holoenzymes from rabbit and Xenopus J Biol Chem 268 10 1993 7330 7337
    • (1993) J Biol Chem , vol.268 , Issue.10 , pp. 7330-7337
    • Hendrix, P.1    Turowski, P.2    Mayer-Jaekel, R.E.3    Goris, J.4    Hofsteenge, J.5    Merlevede, W.6
  • 34
    • 0026661827 scopus 로고
    • Identification of binding sites on the regulatory a subunit of protein phosphatase 2A for the catalytic C subunit and for tumor antigens of simian virus 40 and polyomavirus
    • R. Ruediger, D. Roeckel, J. Fait, A. Bergqvist, G. Magnusson, and G. Walter Identification of binding sites on the regulatory A subunit of protein phosphatase 2A for the catalytic C subunit and for tumor antigens of simian virus 40 and polyomavirus Mol Cell Biol 12 11 1992 4872 4882
    • (1992) Mol Cell Biol , vol.12 , Issue.11 , pp. 4872-4882
    • Ruediger, R.1    Roeckel, D.2    Fait, J.3    Bergqvist, A.4    Magnusson, G.5    Walter, G.6
  • 35
    • 0028082299 scopus 로고
    • Molecular model of the a subunit of protein phosphatase 2A: Interaction with other subunits and tumor antigens
    • R. Ruediger, M. Hentz, J. Fait, M. Mumby, and G. Walter Molecular model of the A subunit of protein phosphatase 2A: interaction with other subunits and tumor antigens J Virol 68 1 1994 123 129
    • (1994) J Virol , vol.68 , Issue.1 , pp. 123-129
    • Ruediger, R.1    Hentz, M.2    Fait, J.3    Mumby, M.4    Walter, G.5
  • 36
    • 0025998844 scopus 로고
    • Classification of protein-serine/threonine phosphatases: Identification and quantitation in cell extracts
    • P. Cohen Classification of protein-serine/threonine phosphatases: identification and quantitation in cell extracts Methods Enzymol 201 1991 389 398
    • (1991) Methods Enzymol , vol.201 , pp. 389-398
    • Cohen, P.1
  • 37
    • 0032535169 scopus 로고    scopus 로고
    • Role of PP2A in intracellular signal transduction pathways
    • A.H. Schonthal Role of PP2A in intracellular signal transduction pathways Front Biosci 3 1998 D1262 D1273
    • (1998) Front Biosci , vol.3
    • Schonthal, A.H.1
  • 40
    • 0030924806 scopus 로고    scopus 로고
    • Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin
    • B. Favre, P. Turowski, and B.A. Hemmings Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin J Biol Chem 272 21 1997 13856 13863
    • (1997) J Biol Chem , vol.272 , Issue.21 , pp. 13856-13863
    • Favre, B.1    Turowski, P.2    Hemmings, B.A.3
  • 41
    • 0034008926 scopus 로고    scopus 로고
    • Transient translocation and activation of protein phosphatase 2A during mast cell secretion
    • R.I. Ludowyke, J. Holst, L.M. Mudge, and A.T. Sim Transient translocation and activation of protein phosphatase 2A during mast cell secretion J Biol Chem 275 9 2000 6144 6152
    • (2000) J Biol Chem , vol.275 , Issue.9 , pp. 6144-6152
    • Ludowyke, R.I.1    Holst, J.2    Mudge, L.M.3    Sim, A.T.4
  • 42
    • 0033965301 scopus 로고    scopus 로고
    • Mast cells in innate immunity
    • Y.A. Mekori, and D.D. Metcalfe Mast cells in innate immunity Immunol Rev 173 2000 131 140
    • (2000) Immunol Rev , vol.173 , pp. 131-140
    • Mekori, Y.A.1    Metcalfe, D.D.2
  • 43
    • 0042380071 scopus 로고    scopus 로고
    • Involvement of both 'allergic' and 'autoimmune' mechanisms in EAE, MS and other autoimmune diseases
    • R. Pedotti, J.J. De Voss, L. Steinman, and S.J. Galli Involvement of both 'allergic' and 'autoimmune' mechanisms in EAE, MS and other autoimmune diseases Trends Immunol 24 9 2003 479 484
    • (2003) Trends Immunol , vol.24 , Issue.9 , pp. 479-484
    • Pedotti, R.1    De Voss, J.J.2    Steinman, L.3    Galli, S.J.4
  • 44
    • 0037383839 scopus 로고    scopus 로고
    • Immunoglobulin free light chains and mast cells: Pivotal role in T-cell-mediated immune reactions?
    • F.A. Redegeld, and F.P. Nijkamp Immunoglobulin free light chains and mast cells: pivotal role in T-cell-mediated immune reactions? Trends Immunol 24 4 2003 181 185
    • (2003) Trends Immunol , vol.24 , Issue.4 , pp. 181-185
    • Redegeld, F.A.1    Nijkamp, F.P.2
  • 45
    • 5644233966 scopus 로고    scopus 로고
    • Mast cells: The Jekyll and Hyde of tumor growth
    • T.C. Theoharides, and P. Conti Mast cells: the Jekyll and Hyde of tumor growth Trends Immunol 25 5 2004 235 241
    • (2004) Trends Immunol , vol.25 , Issue.5 , pp. 235-241
    • Theoharides, T.C.1    Conti, P.2
  • 46
    • 0036888683 scopus 로고    scopus 로고
    • Molecular adapters in Fc(epsilon)RI signaling and the allergic response
    • J. Rivera Molecular adapters in Fc(epsilon)RI signaling and the allergic response Curr Opin Immunol 14 6 2002 688 693
    • (2002) Curr Opin Immunol , vol.14 , Issue.6 , pp. 688-693
    • Rivera, J.1
  • 47
    • 0036344340 scopus 로고    scopus 로고
    • Uncovering new complexities in mast cell signaling
    • M.J. Nadler, and J.P. Kinet Uncovering new complexities in mast cell signaling Nat Immunol 3 8 2002 707 708
    • (2002) Nat Immunol , vol.3 , Issue.8 , pp. 707-708
    • Nadler, M.J.1    Kinet, J.P.2
  • 48
    • 0028887801 scopus 로고
    • Signal transduction in the activation of mast cells and basophils
    • E. Razin, I. Pecht, and J. Rivera Signal transduction in the activation of mast cells and basophils Immunol Today 16 8 1995 370 373
    • (1995) Immunol Today , vol.16 , Issue.8 , pp. 370-373
    • Razin, E.1    Pecht, I.2    Rivera, J.3
  • 49
    • 0029014963 scopus 로고
    • Activation of the mitogen-activated protein kinase/cytosolic phospholipase A2 pathway in a rat mast cell line. Indications of different pathways for release of arachidonic acid and secretory granules
    • N. Hirasawa, F. Santini, and M.A. Beaven Activation of the mitogen-activated protein kinase/cytosolic phospholipase A2 pathway in a rat mast cell line. Indications of different pathways for release of arachidonic acid and secretory granules J Immunol 154 10 1995 5391 5402
    • (1995) J Immunol , vol.154 , Issue.10 , pp. 5391-5402
    • Hirasawa, N.1    Santini, F.2    Beaven, M.A.3
  • 51
    • 0036888776 scopus 로고    scopus 로고
    • The role of mast cells in allergy and autoimmunity
    • M. Robbie-Ryan, and M. Brown The role of mast cells in allergy and autoimmunity Curr Opin Immunol 14 6 2002 728 733
    • (2002) Curr Opin Immunol , vol.14 , Issue.6 , pp. 728-733
    • Robbie-Ryan, M.1    Brown, M.2
  • 52
    • 0037180783 scopus 로고    scopus 로고
    • Mast cells in autoimmune disease
    • C. Benoist, and D. Mathis Mast cells in autoimmune disease Nature 420 6917 2002 875 878
    • (2002) Nature , vol.420 , Issue.6917 , pp. 875-878
    • Benoist, C.1    Mathis, D.2
  • 53
    • 0037108528 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa activates human mast cells to induce neutrophil transendothelial migration via mast cell-derived IL-1 alpha and beta
    • T.J. Lin, R. Garduno, R.T. Boudreau, and A.C. Issekutz Pseudomonas aeruginosa activates human mast cells to induce neutrophil transendothelial migration via mast cell-derived IL-1 alpha and beta J Immunol 169 8 2002 4522 4530
    • (2002) J Immunol , vol.169 , Issue.8 , pp. 4522-4530
    • Lin, T.J.1    Garduno, R.2    Boudreau, R.T.3    Issekutz, A.C.4
  • 54
    • 0034618130 scopus 로고    scopus 로고
    • Mast cells can amplify airway reactivity and features of chronic inflammation in an asthma model in mice
    • C.M. Williams, and S.J. Galli Mast cells can amplify airway reactivity and features of chronic inflammation in an asthma model in mice J Exp Med 192 3 2000 455 462
    • (2000) J Exp Med , vol.192 , Issue.3 , pp. 455-462
    • Williams, C.M.1    Galli, S.J.2
  • 55
    • 0025445902 scopus 로고
    • Evidence for protein dephosphorylation as a permissive step in GTP-gamma-S-induced exocytosis from permeabilized mast cells
    • Y. Churcher, K.M. Kramer, and B.D. Gomperts Evidence for protein dephosphorylation as a permissive step in GTP-gamma-S-induced exocytosis from permeabilized mast cells Cell Regul 1 7 1990 523 530
    • (1990) Cell Regul , vol.1 , Issue.7 , pp. 523-530
    • Churcher, Y.1    Kramer, K.M.2    Gomperts, B.D.3
  • 57
    • 0027305371 scopus 로고
    • Effect of okadaic acid on histamine release from rat peritoneal mast cells activated by anti-IgE
    • M. Takei, H. Mitsui, and K. Endo Effect of okadaic acid on histamine release from rat peritoneal mast cells activated by anti-IgE J Pharm Pharmacol 45 8 1993 750 752
    • (1993) J Pharm Pharmacol , vol.45 , Issue.8 , pp. 750-752
    • Takei, M.1    Mitsui, H.2    Endo, K.3
  • 58
    • 0029888742 scopus 로고    scopus 로고
    • The effect of okadaic acid on histamine release, cell morphology and phosphorylation in rat basophilic leukemia (RBL-2H3) cells, human basophils and rat peritoneal mast cells
    • S. Kitani, R. Teshima, Y. Nonomura, Y. Morita, and K. Ito The effect of okadaic acid on histamine release, cell morphology and phosphorylation in rat basophilic leukemia (RBL-2H3) cells, human basophils and rat peritoneal mast cells Int Arch Allergy Immunol 110 4 1996 339 347
    • (1996) Int Arch Allergy Immunol , vol.110 , Issue.4 , pp. 339-347
    • Kitani, S.1    Teshima, R.2    Nonomura, Y.3    Morita, Y.4    Ito, K.5
  • 59
    • 0028256156 scopus 로고
    • Effect of okadaic acid on immunologic and non-immunologic histamine release in rat mast cells
    • M.D. Estevez, M.R. Vieytes, M.C. Louzao, and L.M. Botana Effect of okadaic acid on immunologic and non-immunologic histamine release in rat mast cells Biochem Pharmacol 47 3 1994 591 593
    • (1994) Biochem Pharmacol , vol.47 , Issue.3 , pp. 591-593
    • Estevez, M.D.1    Vieytes, M.R.2    Louzao, M.C.3    Botana, L.M.4
  • 60
    • 0032296566 scopus 로고    scopus 로고
    • Inhibition of antigen and calcium ionophore induced secretion from RBL-2H3 cells by phosphatase inhibitors
    • R.I. Ludowyke, K. Warton, and L.L. Scurr Inhibition of antigen and calcium ionophore induced secretion from RBL-2H3 cells by phosphatase inhibitors Cell Biol Int 22 11-12 1998 855 865
    • (1998) Cell Biol Int , vol.22 , Issue.11-12 , pp. 855-865
    • Ludowyke, R.I.1    Warton, K.2    Scurr, L.L.3
  • 61
    • 0033369256 scopus 로고    scopus 로고
    • Role of protein phosphatases in the regulation of human mast cell and basophil function
    • M.J. Peirce, M.R. Munday, and P.T. Peachell Role of protein phosphatases in the regulation of human mast cell and basophil function Am J Physiol 277 6 Pt 1 1999 C1021 C1028
    • (1999) Am J Physiol , vol.277 , Issue.6 PART 1
    • Peirce, M.J.1    Munday, M.R.2    Peachell, P.T.3
  • 62
    • 0031762560 scopus 로고    scopus 로고
    • Characterization of protein serine/threonine phosphatase activities in human lung mast cells and basophils
    • M.J. Peirce, M.R. Munday, and P.T. Peachell Characterization of protein serine/threonine phosphatase activities in human lung mast cells and basophils Br J Pharmacol 125 5 1998 1095 1101
    • (1998) Br J Pharmacol , vol.125 , Issue.5 , pp. 1095-1101
    • Peirce, M.J.1    Munday, M.R.2    Peachell, P.T.3
  • 63
    • 0031023947 scopus 로고    scopus 로고
    • Preliminary characterization of the role of protein serine/threonine phosphatases in the regulation of human lung mast cell function
    • M.J. Peirce, S.E. Cox, M.R. Munday, and P.T. Peachell Preliminary characterization of the role of protein serine/threonine phosphatases in the regulation of human lung mast cell function Br J Pharmacol 120 2 1997 239 246
    • (1997) Br J Pharmacol , vol.120 , Issue.2 , pp. 239-246
    • Peirce, M.J.1    Cox, S.E.2    Munday, M.R.3    Peachell, P.T.4
  • 64
    • 0027205530 scopus 로고
    • Regulation of human lung mast cell function by phosphatase inhibitors
    • P.T. Peachell, and M.R. Munday Regulation of human lung mast cell function by phosphatase inhibitors J Immunol 151 7 1993 3808 3816
    • (1993) J Immunol , vol.151 , Issue.7 , pp. 3808-3816
    • Peachell, P.T.1    Munday, M.R.2
  • 65
    • 0035955397 scopus 로고    scopus 로고
    • Regulation of immunoglobulin E-mediated secretion by protein phosphatases in human basophils and mast cells of skin and lung
    • R. Bastan, M.J. Peirce, and P.T. Peachell Regulation of immunoglobulin E-mediated secretion by protein phosphatases in human basophils and mast cells of skin and lung Eur J Pharmacol 430 1 2001 135 141
    • (2001) Eur J Pharmacol , vol.430 , Issue.1 , pp. 135-141
    • Bastan, R.1    Peirce, M.J.2    Peachell, P.T.3
  • 66
    • 0036198540 scopus 로고    scopus 로고
    • Protein phosphatases 1 and 2A transiently associate with myosin during the peak rate of secretion from mast cells
    • J. Holst, A.T. Sim, and R.I. Ludowyke Protein phosphatases 1 and 2A transiently associate with myosin during the peak rate of secretion from mast cells Mol Biol Cell 13 3 2002 1083 1098
    • (2002) Mol Biol Cell , vol.13 , Issue.3 , pp. 1083-1098
    • Holst, J.1    Sim, A.T.2    Ludowyke, R.I.3
  • 67
    • 13444291243 scopus 로고    scopus 로고
    • Glutamate inhibits protein phosphatases and promotes insulin exocytosis in pancreatic beta-cells
    • M. Lehtihet, R.E. Honkanen, and A. Sjoholm Glutamate inhibits protein phosphatases and promotes insulin exocytosis in pancreatic beta-cells Biochem Biophys Res Commun 328 2 2005 601 607
    • (2005) Biochem Biophys Res Commun , vol.328 , Issue.2 , pp. 601-607
    • Lehtihet, M.1    Honkanen, R.E.2    Sjoholm, A.3
  • 68
    • 0028218772 scopus 로고
    • Cell proliferation status, cytokine action and protein tyrosine phosphorylation modulate leukotriene biosynthesis in a basophil leukaemia and a mastocytoma cell line
    • W. Hagmann Cell proliferation status, cytokine action and protein tyrosine phosphorylation modulate leukotriene biosynthesis in a basophil leukaemia and a mastocytoma cell line Biochem J 299 Pt 2 1994 467 472
    • (1994) Biochem J , vol.299 , Issue.2 PART , pp. 467-472
    • Hagmann, W.1
  • 69
    • 0029666270 scopus 로고    scopus 로고
    • Aggregation of the FcepsilonRI on mast cells stimulates c-Jun amino-terminal kinase activity. a response inhibited by wortmannin
    • T. Ishizuka, A. Oshiba, N. Sakata, N. Terada, G.L. Johnson, and E.W. Gelfand Aggregation of the FcepsilonRI on mast cells stimulates c-Jun amino-terminal kinase activity. A response inhibited by wortmannin J Biol Chem 271 22 1996 12762 12766
    • (1996) J Biol Chem , vol.271 , Issue.22 , pp. 12762-12766
    • Ishizuka, T.1    Oshiba, A.2    Sakata, N.3    Terada, N.4    Johnson, G.L.5    Gelfand, E.W.6
  • 71
    • 7644221446 scopus 로고    scopus 로고
    • Phosphatase inhibition potentiates IL-6 production by mast cells in response to FcepsilonRI-mediated activation: Involvement of p38 MAPK
    • R.T. Boudreau, D.W. Hoskin, and T.J. Lin Phosphatase inhibition potentiates IL-6 production by mast cells in response to FcepsilonRI-mediated activation: involvement of p38 MAPK J Leukoc Biol 76 5 2004 1075 1081
    • (2004) J Leukoc Biol , vol.76 , Issue.5 , pp. 1075-1081
    • Boudreau, R.T.1    Hoskin, D.W.2    Lin, T.J.3
  • 72
    • 14244260032 scopus 로고    scopus 로고
    • Protein phosphatase type 2A, PP2A, is involved in degradation of gp130
    • S. Mitsuhashi, H. Shima, N. Tanuma, S. Sasa, K. Onoe, and M. Ubukata Protein phosphatase type 2A, PP2A, is involved in degradation of gp130 Mol Cell Biochem 269 1-2 2005 183 187
    • (2005) Mol Cell Biochem , vol.269 , Issue.1-2 , pp. 183-187
    • Mitsuhashi, S.1    Shima, H.2    Tanuma, N.3    Sasa, S.4    Onoe, K.5    Ubukata, M.6
  • 73
    • 22044458643 scopus 로고    scopus 로고
    • Increases in intracellular calcium dephosphorylate histone H3 at serine 10 in human hepatoma cells: Potential role of protein phosphatase 2A-protein kinase CbetaII complex
    • W. Huang, S. Batra, B.A. Atkins, V. Mishra, and K.D. Mehta Increases in intracellular calcium dephosphorylate histone H3 at serine 10 in human hepatoma cells: potential role of protein phosphatase 2A-protein kinase CbetaII complex J Cell Physiol 204 2005
    • (2005) J Cell Physiol , vol.204
    • Huang, W.1    Batra, S.2    Atkins, B.A.3    Mishra, V.4    Mehta, K.D.5
  • 75
    • 20444464441 scopus 로고    scopus 로고
    • Membrane depolarization induces the undulating phosphorylation/ dephosphorylation of glycogen synthase kinase 3 beta and this dephosphorylation involves protein phosphatases 2A and 2B in SH-SY5Y human neuroblastoma cells
    • Y.I. Lee, M. Seo, Y. Kim, S.Y. Kim, U.G. Kang, and Y.S. Kim Membrane depolarization induces the undulating phosphorylation/dephosphorylation of glycogen synthase kinase 3 beta and this dephosphorylation involves protein phosphatases 2A and 2B in SH-SY5Y human neuroblastoma cells J Biol Chem 280 23 2005 22044 22052
    • (2005) J Biol Chem , vol.280 , Issue.23 , pp. 22044-22052
    • Lee, Y.I.1    Seo, M.2    Kim, Y.3    Kim, S.Y.4    Kang, U.G.5    Kim, Y.S.6
  • 76
    • 0026714727 scopus 로고
    • Influence of protein kinase C, cAMP and phosphatase activity on histamine release produced by compound 48/80 and sodium fluoride on rat mast cells
    • L.M. Botana, A. Alfonso, M.A. Botana, M.R. Vieytes, M.C. Louzao, and A.G. Cabado Influence of protein kinase C, cAMP and phosphatase activity on histamine release produced by compound 48/80 and sodium fluoride on rat mast cells Agents Actions 37 1-2 1992 1 7
    • (1992) Agents Actions , vol.37 , Issue.1-2 , pp. 1-7
    • Botana, L.M.1    Alfonso, A.2    Botana, M.A.3    Vieytes, M.R.4    Louzao, M.C.5    Cabado, A.G.6
  • 77
    • 0030889196 scopus 로고    scopus 로고
    • The antineoplastic drug vinorelbine activates non-immunological histamine release from rat mast cells
    • M.D. Estevez, M.R. Vieytes, M.C. Louzao, A. Alfonso, N. Vilarino, and L.M. Botana The antineoplastic drug vinorelbine activates non-immunological histamine release from rat mast cells Inflamm Res 46 4 1997 119 124
    • (1997) Inflamm Res , vol.46 , Issue.4 , pp. 119-124
    • Estevez, M.D.1    Vieytes, M.R.2    Louzao, M.C.3    Alfonso, A.4    Vilarino, N.5    Botana, L.M.6
  • 78
    • 0029887767 scopus 로고    scopus 로고
    • Mitoxantrone induces nonimmunological histamine release from rat mast cells
    • M.D. Estevez, M.R. Vieytes, and L.M. Botana Mitoxantrone induces nonimmunological histamine release from rat mast cells Inflamm Res 45 3 1996 113 117
    • (1996) Inflamm Res , vol.45 , Issue.3 , pp. 113-117
    • Estevez, M.D.1    Vieytes, M.R.2    Botana, L.M.3
  • 79
    • 0028171214 scopus 로고
    • Study of the activation mechanism of adriamycin on rat mast cells
    • M.D. Estevez, M.R. Vieytes, and L.M. Botana Study of the activation mechanism of adriamycin on rat mast cells Agents Actions 42 3-4 1994 86 91
    • (1994) Agents Actions , vol.42 , Issue.3-4 , pp. 86-91
    • Estevez, M.D.1    Vieytes, M.R.2    Botana, L.M.3
  • 80
    • 0028279707 scopus 로고
    • Effect of signal transduction pathways on the action of thapsigargin on rat mast cells. Crosstalks between cellular signalling and cytosolic pH
    • A. Alfonso, M.A. Botana, M.R. Vieytes, M.C. Louzao, and L.M. Botana Effect of signal transduction pathways on the action of thapsigargin on rat mast cells. Crosstalks between cellular signalling and cytosolic pH Biochem Pharmacol 47 10 1994 1813 1820
    • (1994) Biochem Pharmacol , vol.47 , Issue.10 , pp. 1813-1820
    • Alfonso, A.1    Botana, M.A.2    Vieytes, M.R.3    Louzao, M.C.4    Botana, L.M.5
  • 81
    • 0028915253 scopus 로고
    • Study of the activation mechanism of human GRF(1-29)NH2 on rat mast cell histamine release
    • M.D. Estevez, A. Alfonso, M.R. Vieytes, M.C. Louzao, and L.M. Botana Study of the activation mechanism of human GRF(1-29)NH2 on rat mast cell histamine release Inflamm Res 44 2 1995 87 91
    • (1995) Inflamm Res , vol.44 , Issue.2 , pp. 87-91
    • Estevez, M.D.1    Alfonso, A.2    Vieytes, M.R.3    Louzao, M.C.4    Botana, L.M.5


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