메뉴 건너뛰기




Volumn 111, Issue 21, 1998, Pages 3197-3207

Cytoplasmic calcium gradients and calmodulin in the early development of the fucoid alga Pelvetia compressa

Author keywords

Calcium gradient; Calmodulin; Pelvetia compressa

Indexed keywords

CALCIUM; CALMODULIN; CALMODULIN INHIBITOR; RHODAMINE B;

EID: 0031721932     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (49)

References (35)
  • 1
    • 0015322770 scopus 로고
    • Ionic concentrations in developing Pelvetia eggs
    • Allen, R. D., Jacobsen, L., Joaquin, J. and Jaffe, L. F. (1972). Ionic concentrations in developing Pelvetia eggs. Dev. Biol. 27, 538-545.
    • (1972) Dev. Biol. , vol.27 , pp. 538-545
    • Allen, R.D.1    Jacobsen, L.2    Joaquin, J.3    Jaffe, L.F.4
  • 2
    • 0031036871 scopus 로고    scopus 로고
    • Calmodulin regulation of calcium stores in phototransduction of Drosophila
    • Arnon, A., Cook, B., Montell, C., Selinger, Z. and Minke, B. (1997). Calmodulin regulation of calcium stores in phototransduction of Drosophila. Science 275, 1119-1121.
    • (1997) Science , vol.275 , pp. 1119-1121
    • Arnon, A.1    Cook, B.2    Montell, C.3    Selinger, Z.4    Minke, B.5
  • 3
    • 0030014203 scopus 로고    scopus 로고
    • Calmodulin binding to glutamate decarboxylase is required for regulation of glutamate and GABA metabolism and normal development in plants
    • Baum, G., Lev-Yadun, S., Fridmann, Y., Arazi, T., Katsnelson, H., Zik, M. and Fromm, H. (1996). Calmodulin binding to glutamate decarboxylase is required for regulation of glutamate and GABA metabolism and normal development in plants. EMBO J. 15, 2988-2996.
    • (1996) EMBO J. , vol.15 , pp. 2988-2996
    • Baum, G.1    Lev-Yadun, S.2    Fridmann, Y.3    Arazi, T.4    Katsnelson, H.5    Zik, M.6    Fromm, H.7
  • 4
    • 0020445335 scopus 로고
    • Dictyostelium calmodulin: Production of a specific antiserum and localization in amoebae
    • Bazari, W. L. and Clarke, M. (1982). Dictyostelium calmodulin: production of a specific antiserum and localization in amoebae. Cell Motil. 2, 471-482.
    • (1982) Cell Motil. , vol.2 , pp. 471-482
    • Bazari, W.L.1    Clarke, M.2
  • 5
    • 0027549865 scopus 로고
    • Ratio confocal imaging of free cytoplasmic calcium gradients in polarising and polarised Fucus zygotes
    • Berger, F. and Brownlee, C. (1993). Ratio confocal imaging of free cytoplasmic calcium gradients in polarising and polarised Fucus zygotes. Zygote 1, 9-15.
    • (1993) Zygote , vol.1 , pp. 9-15
    • Berger, F.1    Brownlee, C.2
  • 6
    • 0022002296 scopus 로고
    • Cytochalasin treatment disrupts the endogenous currents associated with cell polarization in fucoid zygotes: Studies of the role of F-actin in embryogenesis
    • Brawley, S. H. and Robinson, K. R. (1985). Cytochalasin treatment disrupts the endogenous currents associated with cell polarization in fucoid zygotes: studies of the role of F-actin in embryogenesis. J. Cell Biol. 100, 1173-1184.
    • (1985) J. Cell Biol. , vol.100 , pp. 1173-1184
    • Brawley, S.H.1    Robinson, K.R.2
  • 7
    • 0024615998 scopus 로고
    • Calmodulin-binding proteins are developmentally regulated in gametes and embryos of fucoid algae
    • Brawley, S. H. and Roberts, D. M. (1989). Calmodulin-binding proteins are developmentally regulated in gametes and embryos of fucoid algae. Dev. Biol. 131, 313-320.
    • (1989) Dev. Biol. , vol.131 , pp. 313-320
    • Brawley, S.H.1    Roberts, D.M.2
  • 8
    • 0022529190 scopus 로고
    • A gradient of cytoplasmic free calcium in growing rhizoid cells of Fucus serratus
    • Brownlee, C. and Wood, J. W. (1986). A gradient of cytoplasmic free calcium in growing rhizoid cells of Fucus serratus. Nature 320, 624-626.
    • (1986) Nature , vol.320 , pp. 624-626
    • Brownlee, C.1    Wood, J.W.2
  • 9
    • 0000674598 scopus 로고
    • 2+ gradient in Fucus serratus rhizoids: Correlation with cell ultrastructure and polarity
    • 2+ gradient in Fucus serratus rhizoids: correlation with cell ultrastructure and polarity. J. Cell Sci. 91, 249-256.
    • (1988) J. Cell Sci. , vol.91 , pp. 249-256
    • Brownlee, C.1    Pulsford, A.L.2
  • 10
    • 0019333537 scopus 로고
    • Interaction of calcium and calmodulin in the presence of sodium dodecyl sulfate
    • Burgess, W. H., Jemiolo, D. K. and Kretsinger, R. H. (1980). Interaction of calcium and calmodulin in the presence of sodium dodecyl sulfate. Biochim. Biophys. Acta 623, 257-270.
    • (1980) Biochim. Biophys. Acta , vol.623 , pp. 257-270
    • Burgess, W.H.1    Jemiolo, D.K.2    Kretsinger, R.H.3
  • 11
    • 0024313794 scopus 로고
    • Vertebrate and yeast calmodulin, despite significant sequence divergence, are functionally interchangeable
    • Davis, T. N. and Thorner, J. (1989). Vertebrate and yeast calmodulin, despite significant sequence divergence, are functionally interchangeable. Proc. Nat. Acad. Sci. USA 86, 7909-7913.
    • (1989) Proc. Nat. Acad. Sci. USA , vol.86 , pp. 7909-7913
    • Davis, T.N.1    Thorner, J.2
  • 12
    • 0029991047 scopus 로고    scopus 로고
    • Inactivation of NMDA receptors by direct interaction of calmodulin with the NRI subunit
    • Ehlers, M. D., Zhang, S., Bernhardt, J. P. and Huganir, R. L. (1996) Inactivation of NMDA receptors by direct interaction of calmodulin with the NRI subunit. Cell 84, 745-755.
    • (1996) Cell , vol.84 , pp. 745-755
    • Ehlers, M.D.1    Zhang, S.2    Bernhardt, J.P.3    Huganir, R.L.4
  • 13
    • 0025765499 scopus 로고
    • Purification and properties of an intracellular calmodulin-like protein from Bacillus subtilis cells
    • Fry, I. J., Becker-Hapak, M. and Hageman, J. H. (1991). Purification and properties of an intracellular calmodulin-like protein from Bacillus subtilis cells. J. Bacteriol. 173, 2506-2513.
    • (1991) J. Bacteriol. , vol.173 , pp. 2506-2513
    • Fry, I.J.1    Becker-Hapak, M.2    Hageman, J.H.3
  • 14
    • 0032101557 scopus 로고    scopus 로고
    • Roles of secretion and the cytoskeleton in cell adhesion and polarity establishment in Pelvetia compressa zygotes
    • Hable, W. E. and Kropf, D. L. (1998). Roles of secretion and the cytoskeleton in cell adhesion and polarity establishment in Pelvetia compressa zygotes. Dev. Biol. 198, 45-56.
    • (1998) Dev. Biol. , vol.198 , pp. 45-56
    • Hable, W.E.1    Kropf, D.L.2
  • 15
    • 0003490276 scopus 로고    scopus 로고
    • 2+ indicators excited by visible light
    • (ed. M. T. Z. Spence), Molecular Probes, Inc. Eugene, Oregon
    • 2+ indicators excited by visible light. In Handbook of Fluorescent Probes and Research Chemicals (ed. M. T. Z. Spence), pp. 511-522. Molecular Probes, Inc. Eugene, Oregon.
    • (1996) Handbook of Fluorescent Probes and Research Chemicals , pp. 511-522
    • Haugland, R.P.1
  • 16
    • 0025963550 scopus 로고
    • Production and specificity of monoclonal antibodies against calmodulin from Dictyostelium discoideum
    • Hulen, D., Baron, A., Salisbury, J. and Clarke, M. (1991). Production and specificity of monoclonal antibodies against calmodulin from Dictyostelium discoideum. Cell Motil. Cytoskel. 18, 113-122.
    • (1991) Cell Motil. Cytoskel. , vol.18 , pp. 113-122
    • Hulen, D.1    Baron, A.2    Salisbury, J.3    Clarke, M.4
  • 17
    • 0003827241 scopus 로고
    • Stimulation of the discharge of gametangia from a brown alga by a change from light to darkness
    • Jaffe, L. (1954). Stimulation of the discharge of gametangia from a brown alga by a change from light to darkness. Nature 174, 743.
    • (1954) Nature , vol.174 , pp. 743
    • Jaffe, L.1
  • 18
    • 0014364849 scopus 로고
    • Localization in the developing Fucus egg and the general role of localizing currents
    • Jaffe, L. F. (1968). Localization in the developing Fucus egg and the general role of localizing currents. Advan. Morphogen. 7, 295-328.
    • (1968) Advan. Morphogen. , vol.7 , pp. 295-328
    • Jaffe, L.F.1
  • 19
    • 0020002173 scopus 로고
    • Microinjection of echinoderm eggs: Apparatus and procedures
    • (ed. L. Wilson), Academic Press, Inc. New York
    • Kiehart, D. P. (1982). Microinjection of echinoderm eggs: apparatus and procedures. In Methods in Cell Biology, vol. 25 (ed. L. Wilson), pp. 13-31. Academic Press, Inc. New York.
    • (1982) Methods in Cell Biology , vol.25 , pp. 13-31
    • Kiehart, D.P.1
  • 21
    • 0024720291 scopus 로고
    • Protein synthesis and morphogenesis are not tightly linked during embryogenesis in Fucus
    • Kropf, D. L., Hopkins, R. and Quatrano, R. S. (1989). Protein synthesis and morphogenesis are not tightly linked during embryogenesis in Fucus. Dev. Biol. 134, 452-461.
    • (1989) Dev. Biol. , vol.134 , pp. 452-461
    • Kropf, D.L.1    Hopkins, R.2    Quatrano, R.S.3
  • 22
    • 0027988660 scopus 로고
    • Cytoskeletal control of cell polarity in a plant zygote
    • Kropf, D. L. (1994). Cytoskeletal control of cell polarity in a plant zygote. Dev. Biol. 165, 361-371.
    • (1994) Dev. Biol. , vol.165 , pp. 361-371
    • Kropf, D.L.1
  • 23
    • 0031397032 scopus 로고    scopus 로고
    • 2+ and calmodulin dynamics during photopolarization in Fucus serratus zygotes
    • 2+ and calmodulin dynamics during photopolarization in Fucus serratus zygotes. Plant Physiol. 115, 249-261.
    • (1997) Plant Physiol. , vol.115 , pp. 249-261
    • Love, J.1    Brownlee, C.2    Trewavas, A.J.3
  • 24
    • 0028250665 scopus 로고
    • i with aequorin using a photon imaging detector
    • (ed. R. Nuccitelli), Academic Press. Inc. New York
    • i with aequorin using a photon imaging detector. In Methods in Cell Biology, vol. 40 (ed. R. Nuccitelli), pp. 305-338. Academic Press. Inc. New York.
    • (1994) Methods in Cell Biology , vol.40 , pp. 305-338
    • Miller, A.L.1    Karplus, E.2    Jaffe, L.F.3
  • 25
    • 0015543145 scopus 로고
    • Cells without cytoplasmic movements respond to cytochalasin
    • Nelson, D. R. and Jaffe, L. F. (1973). Cells without cytoplasmic movements respond to cytochalasin. Dev. Biol. 30, 206-208.
    • (1973) Dev. Biol. , vol.30 , pp. 206-208
    • Nelson, D.R.1    Jaffe, L.F.2
  • 26
    • 0017903796 scopus 로고
    • Oöplasmic segregation and secretion in the Pelvetia egg is accompanied by a membrane-generated electrical current
    • Nuccitelli, R. (1978). Oöplasmic segregation and secretion in the Pelvetia egg is accompanied by a membrane-generated electrical current. Dev. Biol. 62, 13-33.
    • (1978) Dev. Biol. , vol.62 , pp. 13-33
    • Nuccitelli, R.1
  • 27
    • 0015539301 scopus 로고
    • Separation of processes associated with differentiation of two-celled Fucus embryos
    • Quatrano, R. S. (1973). Separation of processes associated with differentiation of two-celled Fucus embryos. Dev. Biol. 30, 209-213.
    • (1973) Dev. Biol. , vol.30 , pp. 209-213
    • Quatrano, R.S.1
  • 28
    • 0026743964 scopus 로고
    • Expression of a calmodulin methylation mutant affects the growth and development of transgenic tobacco plants
    • Roberts, D. M., Besl, L., Oh, S.-H., Masterson, R. V., Schell, J. and Stacey, G. (1992). Expression of a calmodulin methylation mutant affects the growth and development of transgenic tobacco plants. Proc. Nat. Acad. Sci. USA 89, 8394-8398.
    • (1992) Proc. Nat. Acad. Sci. USA , vol.89 , pp. 8394-8398
    • Roberts, D.M.1    Besl, L.2    Oh, S.-H.3    Masterson, R.V.4    Schell, J.5    Stacey, G.6
  • 29
    • 0016440577 scopus 로고
    • Polarizing fucoid eggs drive a calcium current through themselves
    • Robinson, K. R. and Jaffe, L. F. (1975). Polarizing fucoid eggs drive a calcium current through themselves. Science 187, 70-72.
    • (1975) Science , vol.187 , pp. 70-72
    • Robinson, K.R.1    Jaffe, L.F.2
  • 30
    • 0018838388 scopus 로고
    • Polarization of fucoid eggs by a calcium ionophore gradient
    • Robinson, K. R. and Cone, R. (1980). Polarization of fucoid eggs by a calcium ionophore gradient. Science 207, 77-78.
    • (1980) Science , vol.207 , pp. 77-78
    • Robinson, K.R.1    Cone, R.2
  • 31
    • 0030020939 scopus 로고    scopus 로고
    • Calcium and the photopolarization of Pelvetia zygotes
    • Robinson, K. R. (1996). Calcium and the photopolarization of Pelvetia zygotes. Planta 198, 378-384.
    • (1996) Planta , vol.198 , pp. 378-384
    • Robinson, K.R.1
  • 32
    • 0031193326 scopus 로고    scopus 로고
    • The coupling of cyclic GMP and pholopolarization of Pelvetia zygotes
    • Robinson, K. R. and Miller, B. J. (1997). The coupling of cyclic GMP and pholopolarization of Pelvetia zygotes. Dev. Biol. 187, 125-130.
    • (1997) Dev. Biol. , vol.187 , pp. 125-130
    • Robinson, K.R.1    Miller, B.J.2
  • 34
    • 0027966107 scopus 로고
    • Ion channel regulation by calmodulin binding
    • Saimi, Y. and Kung, C. (1994). Ion channel regulation by calmodulin binding. FEBS Lett. 350, 155-158.
    • (1994) FEBS Lett. , vol.350 , pp. 155-158
    • Saimi, Y.1    Kung, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.