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Volumn 63, Issue 7, 1999, Pages 1279-1284

Molecular mechanism for pore-formation in lipid membranes by the hemolytic lectin CEL-III from Marine Invertebrate Cucumaria echinata

Author keywords

Cucumaria echinata; Hemolytic lectin; Ion channel; Liposome; Pore forming protein

Indexed keywords

6 CARBOXYFLUORESCEIN; 6-CARBOXYFLUORESCEIN; FLUORESCEIN DERIVATIVE; LECTIN; LIPOSOME;

EID: 0033162762     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.1279     Document Type: Article
Times cited : (8)

References (22)
  • 1
    • 0028167669 scopus 로고
    • Purification and characterization of four Ca2+-dependent lectins from the marine invertebrate, Cucumaria echinata
    • 2+-dependent lectins from the marine invertebrate, Cucumaria echinata. J. Biochem., 116, 209-214 (1994).
    • (1994) J. Biochem. , vol.116 , pp. 209-214
    • Hatakeyama, T.1    Kohzaki, H.2    Nagatomo, H.3    Yamasaki, N.4
  • 2
    • 0030910331 scopus 로고    scopus 로고
    • Temperature- and pH-depen-dent cytotoxic effect of the hemolytic lectin CEL-III from the marine invertabrate Cucumaria echinata on various cell lines
    • Oda, T., Tsuru, M., Hatakeyama, T., Nagatomo, H., Muramatsu, T., and Yamasaki, N., Temperature- and pH-depen-dent cytotoxic effect of the hemolytic lectin CEL-III from the marine invertabrate Cucumaria echinata on various cell lines. J. Biochem., 121, 560-567 (1997).
    • (1997) J. Biochem. , vol.121 , pp. 560-567
    • Oda, T.1    Tsuru, M.2    Hatakeyama, T.3    Nagatomo, H.4    Muramatsu, T.5    Yamasaki, N.6
  • 3
    • 0028967311 scopus 로고
    • Interaction of the hemolytic lectin CEL-III from the marine invertabrate Cucumaria echinata with erythrocyte membrane
    • Hatakeyama, T., Nagatomo, H., and Yamasaki, N., Interaction of the hemolytic lectin CEL-III from the marine invertabrate Cucumaria echinata with erythrocyte membrane. J. Biol. Chem., 270, 3560-3564 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 3560-3564
    • Hatakeyama, T.1    Nagatomo, H.2    Yamasaki, N.3
  • 4
    • 0029927152 scopus 로고    scopus 로고
    • Oligomerization of the hemolytic lectin CEL-III from the marine invertabrate Cucumaria echinata induced by the binding of carbohydrate ligands
    • Hatakeyama, T., Furukawa, M., Nagatomo, H., Yamasaki, N., and Mori, T., Oligomerization of the hemolytic lectin CEL-III from the marine invertabrate Cucumaria echinata induced by the binding of carbohydrate ligands. J. Biol. Chem., 271, 16915-16920 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 16915-16920
    • Hatakeyama, T.1    Furukawa, M.2    Nagatomo, H.3    Yamasaki, N.4    Mori, T.5
  • 5
    • 0020803175 scopus 로고
    • Phospholipid bilayers made from monolayers on patch-clamp pipettes
    • Coronado, R. and Latorre, R., Phospholipid bilayers made from monolayers on patch-clamp pipettes. Biophys. J., 43, 231-236 (1983).
    • (1983) Biophys. J. , vol.43 , pp. 231-236
    • Coronado, R.1    Latorre, R.2
  • 6
    • 37049073063 scopus 로고
    • Conformational studies and pore-forming properties of an α-aminoisobutyric acid analogue of gramicidin B
    • Jelokhani-Niaraki, M., Kodama, H., Ehara, T., and Kondo, M., Conformational studies and pore-forming properties of an α-aminoisobutyric acid analogue of gramicidin B. J. Chem. Soc. Perkin Trans., 2, 801-808 (1995).
    • (1995) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 801-808
    • Jelokhani-Niaraki, M.1    Kodama, H.2    Ehara, T.3    Kondo, M.4
  • 8
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Bartlett, G. R., Phosphorus assay in column chromatography. J. Biol. Chem., 254, 466-468 (1959)
    • (1959) J. Biol. Chem. , vol.254 , pp. 466-468
    • Bartlett, G.R.1
  • 9
    • 0032153691 scopus 로고    scopus 로고
    • Studies on the Carbohydrate Binding Site of the Hemolytic Lectin CEL-III Isolated from the Marine Invertebrate Cucumaria echinata
    • Sally, I., Hatakeyama, T., and Yamasaki, N., Studies on the Carbohydrate Binding Site of the Hemolytic Lectin CEL-III Isolated from the Marine Invertebrate Cucumaria echinata. Biosci. Biotechnol. Biochem., 62, 1757-1761 (1998).
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1757-1761
    • Sally, I.1    Hatakeyama, T.2    Yamasaki, N.3
  • 10
    • 0022504362 scopus 로고
    • Ionic channels formed by Staphylococcus aureus Alpha-toxin: Voltage-dependent inhibition by divalent and trivalent cations
    • Menestrina, G., Ionic channels formed by Staphylococcus aureus Alpha-toxin: voltage-dependent inhibition by divalent and trivalent cations. J. Membr. Biolol., 90, 177-190 (1986).
    • (1986) J. Membr. Biolol. , vol.90 , pp. 177-190
    • Menestrina, G.1
  • 11
    • 0028980231 scopus 로고
    • Protonation dynamics of the Alpha-toxin ion channel from spectral analysis of pH-de-pendent current fluctuations
    • Kasianowicz, J. J. and Bezrukov, S. M., Protonation dynamics of the Alpha-toxin ion channel from spectral analysis of pH-de-pendent current fluctuations. Biophys. J., 69, 94-105 (1995).
    • (1995) Biophys. J. , vol.69 , pp. 94-105
    • Kasianowicz, J.J.1    Bezrukov, S.M.2
  • 12
    • 0025357554 scopus 로고
    • Aerolysin, a hemolysin from Aeromonas hydrophila, forms voltage-gated channels in planar lipid bilayers
    • Wilmsen, H. U., Pattus, F., and Buckley, J. T., Aerolysin, a hemolysin from Aeromonas hydrophila, forms voltage-gated channels in planar lipid bilayers. J. Membr. Biolol., 115, 71-81 (1990).
    • (1990) J. Membr. Biolol. , vol.115 , pp. 71-81
    • Wilmsen, H.U.1    Pattus, F.2    Buckley, J.T.3
  • 13
    • 0026721371 scopus 로고
    • The aerolysin membrane channel is formed by heptamerization of the monomer
    • Wilmsen, H. U., Leonard, K. R., Tichelaar, W., Buckley, J. T., and Pattus, F., The aerolysin membrane channel is formed by heptamerization of the monomer. EMBO J., 11, 2457-2463 (1992).
    • (1992) EMBO J. , vol.11 , pp. 2457-2463
    • Wilmsen, H.U.1    Leonard, K.R.2    Tichelaar, W.3    Buckley, J.T.4    Pattus, F.5
  • 14
    • 0028231277 scopus 로고
    • The cytolytic toxin aerolysin: From the soluble form to the transmembrane channel
    • van der Goot, F. G., Pattus, F., Parker, M., and Buckley, J. T., The cytolytic toxin aerolysin: from the soluble form to the transmembrane channel. Toxicology, 87, 19-28 (1994).
    • (1994) Toxicology , vol.87 , pp. 19-28
    • Van Der Goot, F.G.1    Pattus, F.2    Parker, M.3    Buckley, J.T.4
  • 15
    • 0024455884 scopus 로고
    • Electrical properties and molecular architecture of the channel formed by Escherichia coli hemolysin in planar lipid membranes
    • Ropele, M. and Menestrina, G., Electrical properties and molecular architecture of the channel formed by Escherichia coli hemolysin in planar lipid membranes. Biochim. Biophys. Acta., 985, 9-18 (1989).
    • (1989) Biochim. Biophys. Acta. , vol.985 , pp. 9-18
    • Ropele, M.1    Menestrina, G.2
  • 16
    • 0025787798 scopus 로고
    • Alpha-toxin of Staphylococcus aureus
    • Bakdie, S. and Tranum-Jensen, J., Alpha-toxin of Staphylococcus aureus. Microbiol. Rev., 55, 733-751 (1992).
    • (1992) Microbiol. Rev. , vol.55 , pp. 733-751
    • Bakdie, S.1    Tranum-Jensen, J.2
  • 17
    • 0025947639 scopus 로고
    • Staphylococcus aureus Alpha-toxin. Dual mechanism of binding to target cells
    • Hildebrand, A., Pohl, M., and Bakdie, S., Staphylococcus aureus Alpha-toxin. Dual mechanism of binding to target cells. J. Biol. Chem., 266, 17195-17200 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 17195-17200
    • Hildebrand, A.1    Pohl, M.2    Bakdie, S.3
  • 18
    • 0029991990 scopus 로고    scopus 로고
    • Partial C-terminal unfolding is required for channel formation by Staphylococcal Alpha-toxin
    • Vecsey-Semjen, B., Mollby, R., and van der Goot, F. G., Partial C-terminal unfolding is required for channel formation by Staphylococcal Alpha-toxin. J. Biol. Chem., 271, 8655-8660 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 8655-8660
    • Vecsey-Semjen, B.1    Mollby, R.2    Van Der Goot, F.G.3
  • 19
    • 0024399624 scopus 로고
    • Staphylococcal Alpha-toxin increases the permeability of lipid vesicles by cholesterol- and pH-dependent assembly of oligomeric channels
    • Forti, N. and Menestrina, G., Staphylococcal Alpha-toxin increases the permeability of lipid vesicles by cholesterol- and pH-dependent assembly of oligomeric channels. Eur. J. Biochem., 181, 767-773 (1989).
    • (1989) Eur. J. Biochem. , vol.181 , pp. 767-773
    • Forti, N.1    Menestrina, G.2
  • 20
    • 0030789217 scopus 로고    scopus 로고
    • The erythrocyte receptor for the channel-forming toxin aerolysin is a novel glycosylphosphatidylinositol-anchored protein
    • Cowell, S., Aschauer, W., Gruber, H. J., Nelson, K. L., and Buckley, J. T., The erythrocyte receptor for the channel-forming toxin aerolysin is a novel glycosylphosphatidylinositol-anchored protein. Mol. Microbiol., 25, 343-50 (1997).
    • (1997) Mol. Microbiol. , vol.25 , pp. 343-350
    • Cowell, S.1    Aschauer, W.2    Gruber, H.J.3    Nelson, K.L.4    Buckley, J.T.5
  • 21
    • 0023181113 scopus 로고
    • Activities of Aeromonas hydrophila hemolysins and their interaction with erythrocyte membranes
    • Kozaki, S., Kato, K., Asao, T., Kamata, Y., and Sakaguchi, G., Activities of Aeromonas hydrophila hemolysins and their interaction with erythrocyte membranes. Infec. Immun., 55, 1594-1599 (1987).
    • (1987) Infec. Immun. , vol.55 , pp. 1594-1599
    • Kozaki, S.1    Kato, K.2    Asao, T.3    Kamata, Y.4    Sakaguchi, G.5
  • 22
    • 0033032077 scopus 로고    scopus 로고
    • Characterization of the interaction of hemolytic lectin CEL-III from the marine invertebrate, Cucumaria echinata, with artificial lipid membranes: Involvement of neutral sphingoglycolipids in the pore-forming process
    • Hatakeyama, T., Sato, T., Taira, T., Kuwahara, H., Niidome, T., and Aoyagi, H., Characterization of the interaction of hemolytic lectin CEL-III from the marine invertebrate, Cucumaria echinata, with artificial lipid membranes: involvement of neutral sphingoglycolipids in the pore-forming process. J. Biochem., 125, 277-284 (1999).
    • (1999) J. Biochem. , vol.125 , pp. 277-284
    • Hatakeyama, T.1    Sato, T.2    Taira, T.3    Kuwahara, H.4    Niidome, T.5    Aoyagi, H.6


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