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Volumn 1417, Issue 1, 1999, Pages 167-182

Heparin influence on α-staphylotoxin formed channel

Author keywords

Calcium; Gating; Heparin; Ion channel; Lipid bilayer; Staphylotoxin

Indexed keywords

HEPARIN; STAPHYLOCOCCUS ALPHA TOXIN;

EID: 0032992788     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(98)00244-2     Document Type: Article
Times cited : (7)

References (56)
  • 1
    • 0021747672 scopus 로고
    • Primary sequence of the alpha-toxin gene from Staphylococcus aureus Wood 46
    • Gray G.S., Kehoe M. Primary sequence of the alpha-toxin gene from Staphylococcus aureus Wood 46. Infect. Immun. 46:1984;615-618.
    • (1984) Infect. Immun. , vol.46 , pp. 615-618
    • Gray, G.S.1    Kehoe, M.2
  • 2
    • 0028567173 scopus 로고
    • Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: A heptameric transmembrane pore
    • Gouaux J.E., Braha O., Hobaugh M.R., Song L., Cheley S., Shustak C., Bayley H. Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore. Proc. Natl. Acad. Sci. USA. 91:1994;12828-12831.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12828-12831
    • Gouaux, J.E.1    Braha, O.2    Hobaugh, M.R.3    Song, L.4    Cheley, S.5    Shustak, C.6    Bayley, H.7
  • 4
    • 17744414381 scopus 로고
    • Properties of ion channels induced by alpha-staphylotoxin in bilayer lipid membranes
    • Krasilnikov O.V., Ternovsky V.I., Tashmukhamedov B.A. Properties of ion channels induced by alpha-staphylotoxin in bilayer lipid membranes. Biofizika. 26:1981;271-275.
    • (1981) Biofizika , vol.26 , pp. 271-275
    • Krasilnikov, O.V.1    Ternovsky, V.I.2    Tashmukhamedov, B.A.3
  • 5
    • 0022504362 scopus 로고
    • Ionic channel formed by S. aureus α-toxin: Voltage-dependent inhibition by divalent and trivalent cations
    • Menestrina G. Ionic channel formed by S. aureus α-toxin: voltage-dependent inhibition by divalent and trivalent cations. J. Membr. Biol. 90:1986;177-190.
    • (1986) J. Membr. Biol. , vol.90 , pp. 177-190
    • Menestrina, G.1
  • 6
    • 0344350873 scopus 로고
    • Pore formation by Staphylococcus aureus alpha-toxin: A study using planar bilayers
    • G. Menestrina, Pore formation by Staphylococcus aureus alpha-toxin: a study using planar bilayers, Zbl. Bakteriol. Suppl. 17 (1988) 295-302.
    • (1988) Zbl. Bakteriol. Suppl. , vol.17 , pp. 295-302
    • Menestrina, G.1
  • 8
    • 0025665205 scopus 로고
    • Memory is a property of an ion channels pool: Ion channels formed by Staphylococcus aureus alpha-toxin
    • Krasilnikov O.V., Merzliak P.G., Sabirov R.Z., Tashmukhamedov B.A. Memory is a property of an ion channels pool: ion channels formed by Staphylococcus aureus alpha-toxin. Gen. Physiol. Biophys. 9:1990;569-575.
    • (1990) Gen. Physiol. Biophys. , vol.9 , pp. 569-575
    • Krasilnikov, O.V.1    Merzliak, P.G.2    Sabirov, R.Z.3    Tashmukhamedov, B.A.4
  • 9
    • 0028980231 scopus 로고
    • Protonation dynamics of the alpha-toxin ion channel from spectral analysis of pH-dependent current fluctuations
    • Kasianowicz J.J., Bezrukov S.M. Protonation dynamics of the alpha-toxin ion channel from spectral analysis of pH-dependent current fluctuations. Biophys. J. 69:1995;94-105.
    • (1995) Biophys. J. , vol.69 , pp. 94-105
    • Kasianowicz, J.J.1    Bezrukov, S.M.2
  • 11
    • 0344350875 scopus 로고
    • The influence of ionic composition in the solution on kinetic of the ion channel formation by alpha-toxin S. aureus in bilayer lipid membranes
    • Krasilnikov O.V., Sabirov R.Z., Tashmukhamedov B.A. The influence of ionic composition in the solution on kinetic of the ion channel formation by alpha-toxin S. aureus in bilayer lipid membranes. Biol. Membr. 3:1986;1057-1061.
    • (1986) Biol. Membr. , vol.3 , pp. 1057-1061
    • Krasilnikov, O.V.1    Sabirov, R.Z.2    Tashmukhamedov, B.A.3
  • 12
    • 0344350874 scopus 로고
    • Anticoagulant, antithrombotic and antihemostatic activities of heparin: structural requirements, mechanism of action and clinical applications
    • H.B. Nader, C.P. Dietrich, Anticoagulant, antithrombotic and antihemostatic activities of heparin: structural requirements, mechanism of action and clinical applications, Ciência e Cultura (J. Braz. Assoc. Adv. Sci.) 46 (1994) 297-302.
    • (1994) Ciência e Cultura (J. Braz. Assoc. Adv. Sci.) , vol.46 , pp. 297-302
    • Nader, H.B.1    Dietrich, C.P.2
  • 14
    • 0027415003 scopus 로고
    • Activation of the calcium release channel (ryanodine receptor) by heparin and other polyanions is calcium dependent
    • Bezprozvanny I.B., Ondrias K., Kaftan E., Stoynovsky D.A. Activation of the calcium release channel (ryanodine receptor) by heparin and other polyanions is calcium dependent. Mol. Biol. Cell. 4:1993;347-350.
    • (1993) Mol. Biol. Cell. , vol.4 , pp. 347-350
    • Bezprozvanny, I.B.1    Ondrias, K.2    Kaftan, E.3    Stoynovsky, D.A.4
  • 15
    • 0028985342 scopus 로고
    • IP3 receptor purified from liver plasma membrane is an (1,4,5) IP3 activated and (1,3,4,5) IP4 inhibited calcium permeable ion channel
    • Mayrleitner M., Schafer R., Fleischer S. IP3 receptor purified from liver plasma membrane is an (1,4,5) IP3 activated and (1,3,4,5) IP4 inhibited calcium permeable ion channel. Cell. Calcium. 17:1995;141-153.
    • (1995) Cell. Calcium , vol.17 , pp. 141-153
    • Mayrleitner, M.1    Schafer, R.2    Fleischer, S.3
  • 16
    • 0030790118 scopus 로고    scopus 로고
    • Structure and function of inositol 1,4,5-trisphosphate receptor
    • Yoshida Y., Imai S. Structure and function of inositol 1,4,5-trisphosphate receptor. Jpn. J. Pharmacol. 74:1997;125-137.
    • (1997) Jpn. J. Pharmacol. , vol.74 , pp. 125-137
    • Yoshida, Y.1    Imai, S.2
  • 18
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties
    • Montal M., Mueller P. Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties. Proc. Natl. Acad. Sci. USA. 69:1972;3561-3566.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 3561-3566
    • Montal, M.1    Mueller, P.2
  • 19
    • 0017054558 scopus 로고
    • Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from paramecium mitochondria
    • Schein S.J., Colombini M., Finkelstein A. Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from paramecium mitochondria. J. Membr. Biol. 30:1976;99-120.
    • (1976) J. Membr. Biol. , vol.30 , pp. 99-120
    • Schein, S.J.1    Colombini, M.2    Finkelstein, A.3
  • 20
    • 0018960687 scopus 로고
    • Thermodynamic and kinetic studies of the gating behavior of a K-selective channel from the sarcoplasmic reticulum membrane
    • Labarca P., Coronado R., Miller C. Thermodynamic and kinetic studies of the gating behavior of a K-selective channel from the sarcoplasmic reticulum membrane. J. Gen. Physiol. 76:1980;397-424.
    • (1980) J. Gen. Physiol. , vol.76 , pp. 397-424
    • Labarca, P.1    Coronado, R.2    Miller, C.3
  • 21
    • 8244234955 scopus 로고
    • Statistical method for approaching
    • P11-6816, Dubna
    • H. Eler, Statistical method for approaching, AINP Rep., P11-6816, Dubna, 1972.
    • (1972) AINP Rep.
    • Eler, H.1
  • 22
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song L., Hobaugh M.R., Shustak C., Cheley S., Bayley H., Gouaux J.E. Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore. Science. 274:1996;1859-1866.
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 23
    • 0030975688 scopus 로고    scopus 로고
    • Influence of Cys-130 S. aureus alpha-toxin on planar lipid bilayer and erythrocyte membranes
    • Krasilnikov O.V., Capistrano M.-F.P., Yuldasheva L.N., Nogueira R.A. Influence of Cys-130 S. aureus alpha-toxin on planar lipid bilayer and erythrocyte membranes. J. Membr. Biol. 156:1997;157-172.
    • (1997) J. Membr. Biol. , vol.156 , pp. 157-172
    • Krasilnikov, O.V.1    Capistrano, M.-F.P.2    Yuldasheva, L.N.3    Nogueira, R.A.4
  • 25
    • 0024676138 scopus 로고
    • Ion transport through channels formed in lipid bilayers by Staphylococcus aureus alpha-toxin
    • Krasilnikov O.V., Sabirov R.Z. Ion transport through channels formed in lipid bilayers by Staphylococcus aureus alpha-toxin. Gen. Physiol. Biophys. 8:1989;213-222.
    • (1989) Gen. Physiol. Biophys. , vol.8 , pp. 213-222
    • Krasilnikov, O.V.1    Sabirov, R.Z.2
  • 26
    • 0014708021 scopus 로고
    • The nature of the negative resistance in bimolecular lipid membranes containing excitability-inducing material
    • Ehrenstein G., Lecar H., Nossal R. The nature of the negative resistance in bimolecular lipid membranes containing excitability-inducing material. J. Gen. Physiol. 55:1970;119-133.
    • (1970) J. Gen. Physiol. , vol.55 , pp. 119-133
    • Ehrenstein, G.1    Lecar, H.2    Nossal, R.3
  • 28
    • 0023030922 scopus 로고
    • Membrane damage by hemolytic viruses, toxins, complement, and other cytotoxic agents. Common mechanism blocked by divalent cations
    • Bashford C.L., Alder G.M., Menestrina G., Micklem K.J., Murphy J.J., Pasternak C.A. Membrane damage by hemolytic viruses, toxins, complement, and other cytotoxic agents. Common mechanism blocked by divalent cations. J. Biol. Chem. 261:1986;9300-9308.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9300-9308
    • Bashford, C.L.1    Alder, G.M.2    Menestrina, G.3    Micklem, K.J.4    Murphy, J.J.5    Pasternak, C.A.6
  • 29
    • 0023720483 scopus 로고
    • Ion modulation of membrane permeability: Effect of cations on intact cells and on cells and phospholipid bilayers treated with pore-forming agents
    • Bashford C.L., Alder G.M., Graham J.M., Menestrina G., Pasternak C.A. Ion modulation of membrane permeability: effect of cations on intact cells and on cells and phospholipid bilayers treated with pore-forming agents. J. Membr. Biol. 103:1988;79-94.
    • (1988) J. Membr. Biol. , vol.103 , pp. 79-94
    • Bashford, C.L.1    Alder, G.M.2    Graham, J.M.3    Menestrina, G.4    Pasternak, C.A.5
  • 30
    • 0018271004 scopus 로고
    • The adsorption of divalent cations to phosphatidylcholine bilayer membranes
    • McLaughlin A., Grathwohl C., McLaughlin S. The adsorption of divalent cations to phosphatidylcholine bilayer membranes. Biochim. Biophys. Acta. 513:1978;338-357.
    • (1978) Biochim. Biophys. Acta , vol.513 , pp. 338-357
    • McLaughlin, A.1    Grathwohl, C.2    McLaughlin, S.3
  • 32
    • 0345213557 scopus 로고
    • The stability of complexes of the group IIA metal ions
    • R.J.P. William, The stability of complexes of the group IIA metal ions, J. Chem. Soc. (1952) 3770-3778.
    • (1952) J. Chem. Soc. , pp. 3770-3778
    • William, R.J.P.1
  • 33
    • 0017615837 scopus 로고
    • Nature of interaction of dextran sulfate with lecithin dispersions and lisolecithin micelles
    • Kim Y.C., Nishida T. Nature of interaction of dextran sulfate with lecithin dispersions and lisolecithin micelles. J. Biol. Chem. 252:1977;1243-1249.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1243-1249
    • Kim, Y.C.1    Nishida, T.2
  • 34
    • 0018865358 scopus 로고
    • A physico-chemical study of heparin. Evidence for a calcium-induced co-operative conformational transition
    • Boyd J., Williamson F.B., Gettins P. A physico-chemical study of heparin. Evidence for a calcium-induced co-operative conformational transition. J. Mol. Biol. 137:(2):1980;175-190.
    • (1980) J. Mol. Biol. , vol.137 , Issue.2 , pp. 175-190
    • Boyd, J.1    Williamson, F.B.2    Gettins, P.3
  • 36
    • 0026462656 scopus 로고
    • Interaction of heparin with myosin ATPase: Possible involvement with the hemorrhagic activity and a correlation with antithrombin III rich affinity-heparin molecule
    • Tersariol I.L.S., Dietrich C.P., Nader H.B. Interaction of heparin with myosin ATPase: possible involvement with the hemorrhagic activity and a correlation with antithrombin III rich affinity-heparin molecule. Thromb. Res. 68:1992;247-258.
    • (1992) Thromb. Res. , vol.68 , pp. 247-258
    • Tersariol, I.L.S.1    Dietrich, C.P.2    Nader, H.B.3
  • 37
    • 0023658323 scopus 로고
    • Extracellular mammalian polysaccharides: Glycosaminoglycans and proteoglycans
    • Beaty N.B., Mello R.J. Extracellular mammalian polysaccharides: glycosaminoglycans and proteoglycans. J. Chromatogr. 418:1987;187-222.
    • (1987) J. Chromatogr. , vol.418 , pp. 187-222
    • Beaty, N.B.1    Mello, R.J.2
  • 39
    • 0025174948 scopus 로고
    • Redistribution of the electric field within the pore contributes to the voltage-dependence of mitochondrial porin channel
    • Ermishkin L.N., Mirzabekov T.A. Redistribution of the electric field within the pore contributes to the voltage-dependence of mitochondrial porin channel. Biochim. Biophys. Acta. 1021:1990;161-168.
    • (1990) Biochim. Biophys. Acta , vol.1021 , pp. 161-168
    • Ermishkin, L.N.1    Mirzabekov, T.A.2
  • 40
    • 0023373137 scopus 로고
    • Ultrasteep voltage dependence in a membrane channel
    • Mangan P.S., Colombini M. Ultrasteep voltage dependence in a membrane channel. Proc. Natl. Acad. Sci. USA. 84:1987;4896-4900.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4896-4900
    • Mangan, P.S.1    Colombini, M.2
  • 41
    • 0024458675 scopus 로고
    • Voltage gating in the mitochondrial channel
    • Colombini M. Voltage gating in the mitochondrial channel. J. Membr. Biol. 111:1989;103-111.
    • (1989) J. Membr. Biol. , vol.111 , pp. 103-111
    • Colombini, M.1
  • 42
    • 0025055367 scopus 로고
    • Biophysical properties of porin pores from mitochondrial outer membrane of eukaryotic cells
    • Benz R. Biophysical properties of porin pores from mitochondrial outer membrane of eukaryotic cells. Experientia. 46:1990;131-137.
    • (1990) Experientia , vol.46 , pp. 131-137
    • Benz, R.1
  • 43
    • 0027315863 scopus 로고
    • Mapping of residues forming the voltage sensor of the voltage-dependent anion-selective channel
    • Thomas L., Blachly-Dyson E., Colombini M., Forte M. Mapping of residues forming the voltage sensor of the voltage-dependent anion-selective channel. Proc. Natl. Acad. Sci. USA. 90:1993;5446-5449.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5446-5449
    • Thomas, L.1    Blachly-Dyson, E.2    Colombini, M.3    Forte, M.4
  • 45
    • 0014962801 scopus 로고
    • Nature of the interaction of dextran sulfate with low density lipoproteins of plasma
    • Nishida T., Cogan U. Nature of the interaction of dextran sulfate with low density lipoproteins of plasma. J. Biol. Chem. 245:1970;4689-4697.
    • (1970) J. Biol. Chem. , vol.245 , pp. 4689-4697
    • Nishida, T.1    Cogan, U.2
  • 46
    • 0015522929 scopus 로고
    • The interaction between human plasma lipoproteins and connective tissue glycosaminoglycans
    • Iverius P.-H. The interaction between human plasma lipoproteins and connective tissue glycosaminoglycans. J. Biol. Chem. 247:1972;2607-2613.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2607-2613
    • Iverius, P.-H.1
  • 49
    • 0025266223 scopus 로고
    • Microelectrophoresis studies of the binding of glycosaminoglycans to phosphatidylcholine liposomes
    • Krumbiegel M., Arnold K. Microelectrophoresis studies of the binding of glycosaminoglycans to phosphatidylcholine liposomes. Chem. Phys. Lipids. 54:1990;1-7.
    • (1990) Chem. Phys. Lipids , vol.54 , pp. 1-7
    • Krumbiegel, M.1    Arnold, K.2
  • 51
    • 0027223744 scopus 로고
    • Relation between ionic channel conductance and conductivity of media containing different nonelectrolytes. A novel method of pore size determination
    • Sabirov R.Z., Krasilnikov O.V., Ternovsky V.I., Merzliak P.G. Relation between ionic channel conductance and conductivity of media containing different nonelectrolytes. A novel method of pore size determination. Gen. Physiol. Biophys. 12:1993;95-111.
    • (1993) Gen. Physiol. Biophys. , vol.12 , pp. 95-111
    • Sabirov, R.Z.1    Krasilnikov, O.V.2    Ternovsky, V.I.3    Merzliak, P.G.4
  • 52
    • 0027164634 scopus 로고
    • N.m.r and molecular-modeling studies of the solution conformation of heparin
    • Mulloy B., Forster M.J., Jones C., Davies D.B. N.m.r and molecular-modeling studies of the solution conformation of heparin. Biochem. J. 293:1993;849-858.
    • (1993) Biochem. J. , vol.293 , pp. 849-858
    • Mulloy, B.1    Forster, M.J.2    Jones, C.3    Davies, D.B.4
  • 54
    • 0030465241 scopus 로고    scopus 로고
    • Characterization of individual polynucleotide molecules using a membrane channel
    • Kasianowicz J.J., Brandin E., Branton D., Deamer D.W. Characterization of individual polynucleotide molecules using a membrane channel. Proc. Natl. Acad. Sci. USA. 93:1996;13770-13773.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13770-13773
    • Kasianowicz, J.J.1    Brandin, E.2    Branton, D.3    Deamer, D.W.4
  • 55
    • 0024021040 scopus 로고
    • Conformational flexibility: A new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans
    • Casu B., Petitou M., Provasoli M., Sinay P. Conformational flexibility: a new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans. Trends Biochem. Sci. 13:1988;221-225.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 221-225
    • Casu, B.1    Petitou, M.2    Provasoli, M.3    Sinay, P.4
  • 56
    • 0027336584 scopus 로고
    • 2+ channel modulating effects of heparin in mammalian cardiac myocytes
    • 2+ channel modulating effects of heparin in mammalian cardiac myocytes. J. Physiol. 465:1993;181-201.
    • (1993) J. Physiol. , vol.465 , pp. 181-201
    • Lacinova, L.1    Cleemann, L.2    Morad, M.3


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