메뉴 건너뛰기




Volumn 60, Issue 5, 2012, Pages 724-733

Sticholysin II: A pore-forming toxin as a probe to recognize sphingomyelin in artificial and cellular membranes

Author keywords

Actinoporins; Cell membrane; Sphingomyelin; Stichodactyla helianthus; Sticholysin II

Indexed keywords

CHOLERA TOXIN; DODECYL SULFATE SODIUM; GANGLIOSIDE GM1; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY A10; SEA ANEMONE TOXIN; SPHINGOMYELIN; STICHOLYSIN II; TOXIN ANTIBODY; UNCLASSIFIED DRUG;

EID: 84863658657     PISSN: 00410101     EISSN: 18793150     Source Type: Journal    
DOI: 10.1016/j.toxicon.2012.05.018     Document Type: Article
Times cited : (15)

References (38)
  • 1
    • 33644943981 scopus 로고    scopus 로고
    • Detergent-resistant membranes are platforms for actinoporin pore-forming activity on intact cells
    • Alegre-Cebollada J., Rodriguez-Crespo I., Gavilanes J.G., Del Pozo A.M. Detergent-resistant membranes are platforms for actinoporin pore-forming activity on intact cells. FEBS J. 2006, 273:863-871.
    • (2006) FEBS J. , vol.273 , pp. 863-871
    • Alegre-Cebollada, J.1    Rodriguez-Crespo, I.2    Gavilanes, J.G.3    Del Pozo, A.M.4
  • 2
    • 68949088726 scopus 로고    scopus 로고
    • Sticholysins, two pore-forming toxins produced by the Caribbean Sea anemone Stichodactyla helianthus: their interaction with membranes
    • Alvarez C., Mancheno J.M., Martinez D., Tejuca M., Pazos F., Lanio M.E. Sticholysins, two pore-forming toxins produced by the Caribbean Sea anemone Stichodactyla helianthus: their interaction with membranes. Toxicon 2009, 54:1135-1147.
    • (2009) Toxicon , vol.54 , pp. 1135-1147
    • Alvarez, C.1    Mancheno, J.M.2    Martinez, D.3    Tejuca, M.4    Pazos, F.5    Lanio, M.E.6
  • 3
    • 0036027362 scopus 로고    scopus 로고
    • Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria)
    • Anderluh G., Macek P. Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria). Toxicon 2002, 40:111-124.
    • (2002) Toxicon , vol.40 , pp. 111-124
    • Anderluh, G.1    Macek, P.2
  • 4
    • 77955868782 scopus 로고    scopus 로고
    • Molecular mechanism of sphingomyelin-specific membrane binding and pore formation by actinoporins
    • Bakrac B., Anderluh G. Molecular mechanism of sphingomyelin-specific membrane binding and pore formation by actinoporins. Adv. Exp. Med. Biol. 2010, 677:106-115.
    • (2010) Adv. Exp. Med. Biol. , vol.677 , pp. 106-115
    • Bakrac, B.1    Anderluh, G.2
  • 7
    • 0038883648 scopus 로고
    • Properties of a toxin from the sea anemone Stoichactis helianthus, including specific binding to sphingomyelin
    • Bernheimer A.W., Avigad L.S. Properties of a toxin from the sea anemone Stoichactis helianthus, including specific binding to sphingomyelin. Proc. Natl. Acad. Sci. USA 1976, 73:467-471.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 467-471
    • Bernheimer, A.W.1    Avigad, L.S.2
  • 9
    • 0022555992 scopus 로고
    • Methods for high frequency production of soluble antigen-specific hybridomas; specificities and affinities of the monoclonal antibodies obtained
    • Cianfriglia M., Mariani M., Armellini D., Massone A., Lafata M., Presentini R., Antoni G. Methods for high frequency production of soluble antigen-specific hybridomas; specificities and affinities of the monoclonal antibodies obtained. Methods Enzymol. 1986, 121:193-210.
    • (1986) Methods Enzymol. , vol.121 , pp. 193-210
    • Cianfriglia, M.1    Mariani, M.2    Armellini, D.3    Massone, A.4    Lafata, M.5    Presentini, R.6    Antoni, G.7
  • 10
    • 55949090292 scopus 로고    scopus 로고
    • Complex gangliosides are apically sorted in polarized MDCK cells and internalized by clathrin-independent endocytosis
    • Crespo P.M., Von Muhlinen N., Iglesias-Bartolom R., Daniotti J.L. Complex gangliosides are apically sorted in polarized MDCK cells and internalized by clathrin-independent endocytosis. FEBS J. 2008, 275:6043-6056.
    • (2008) FEBS J. , vol.275 , pp. 6043-6056
    • Crespo, P.M.1    Von Muhlinen, N.2    Iglesias-Bartolom, R.3    Daniotti, J.L.4
  • 11
    • 79952208111 scopus 로고    scopus 로고
    • Segregation of fluorescent membrane lipids into distinct micrometric domains: evidence for phase compartmentation of natural lipids?
    • D'Auria L., Van der Smissen P., Bruyneel F., Courtoy P.J., Tyteca D. Segregation of fluorescent membrane lipids into distinct micrometric domains: evidence for phase compartmentation of natural lipids?. PLoS One 2011, 6:17021-17036.
    • (2011) PLoS One , vol.6 , pp. 17021-17036
    • D'Auria, L.1    Van der Smissen, P.2    Bruyneel, F.3    Courtoy, P.J.4    Tyteca, D.5
  • 12
    • 0032999454 scopus 로고    scopus 로고
    • Sticholysin II, a cytolysin from the sea anemone Stichodactyla helianthus, is a monomer-tetramer associating protein
    • de los Rios V., Mancheno J.M., del Pozo M.A., Alfonso C., Rivas G., Onaderra M., Gavilanes J.G. Sticholysin II, a cytolysin from the sea anemone Stichodactyla helianthus, is a monomer-tetramer associating protein. FEBS Lett. 2009, 455:27-30.
    • (2009) FEBS Lett. , vol.455 , pp. 27-30
    • de los Rios, V.1    Mancheno, J.M.2    del Pozo, M.A.3    Alfonso, C.4    Rivas, G.5    Onaderra, M.6    Gavilanes, J.G.7
  • 13
    • 77952898456 scopus 로고    scopus 로고
    • Phase separation in biological membranes: integration of theory and experiment
    • Elson E.L., Fried E., Dolbow J.E., Genin G.M. Phase separation in biological membranes: integration of theory and experiment. Annu. Rev. Biophys. 2010, 39:207-226.
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 207-226
    • Elson, E.L.1    Fried, E.2    Dolbow, J.E.3    Genin, G.M.4
  • 14
    • 69449096573 scopus 로고    scopus 로고
    • Molecular mechanisms of clathrin-independent endocytosis
    • Hansen C.G., Nichols B.J. Molecular mechanisms of clathrin-independent endocytosis. J. Cell Sci. 2009, 122:1713-1721.
    • (2009) J. Cell Sci. , vol.122 , pp. 1713-1721
    • Hansen, C.G.1    Nichols, B.J.2
  • 15
    • 0016360614 scopus 로고
    • Preparation of homogeneous, single-walled phosphatidylcholine vesicles
    • Huang C., Thompson T.E. Preparation of homogeneous, single-walled phosphatidylcholine vesicles. Methods Enzymol. 1974, 32:485-489.
    • (1974) Methods Enzymol. , vol.32 , pp. 485-489
    • Huang, C.1    Thompson, T.E.2
  • 16
    • 0028969849 scopus 로고
    • Specific binding of a synthetic peptide derived from an antibody complementarity determining region to phosphatidylserine
    • Igarashi K., Asai K., Kaneda M., Umeda M., Inoue K. Specific binding of a synthetic peptide derived from an antibody complementarity determining region to phosphatidylserine. J. Biochem. 1995, 117:452-457.
    • (1995) J. Biochem. , vol.117 , pp. 452-457
    • Igarashi, K.1    Asai, K.2    Kaneda, M.3    Umeda, M.4    Inoue, K.5
  • 17
    • 0024212323 scopus 로고
    • Separation and characterization of four different amino acid sequence variants of a sea anemone (Stichodactyla helianthus) protein cytolysin
    • Kem W.R., Dunn B.M. Separation and characterization of four different amino acid sequence variants of a sea anemone (Stichodactyla helianthus) protein cytolysin. Toxicon 1988, 26:997-1008.
    • (1988) Toxicon , vol.26 , pp. 997-1008
    • Kem, W.R.1    Dunn, B.M.2
  • 18
    • 21244442348 scopus 로고    scopus 로고
    • Spatial and functional heterogeneity of sphingolipid-rich membrane domains
    • Kiyokawa E., Baba T., Otsuka N., Makino A., Ohno S., Kobayashi T. Spatial and functional heterogeneity of sphingolipid-rich membrane domains. J. Biol. Chem. 2005, 280:24072-24084.
    • (2005) J. Biol. Chem. , vol.280 , pp. 24072-24084
    • Kiyokawa, E.1    Baba, T.2    Otsuka, N.3    Makino, A.4    Ohno, S.5    Kobayashi, T.6
  • 19
    • 0034598640 scopus 로고    scopus 로고
    • Purification and characterization of two hemolysins from Stichodactyla helianthus
    • Lanio M.E., Morera V., Alvarez C., Tejuca M., Gomez T. Purification and characterization of two hemolysins from Stichodactyla helianthus. Toxicon 2001, 39:187-194.
    • (2001) Toxicon , vol.39 , pp. 187-194
    • Lanio, M.E.1    Morera, V.2    Alvarez, C.3    Tejuca, M.4    Gomez, T.5
  • 20
    • 0242542032 scopus 로고    scopus 로고
    • Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation
    • Mancheno J.M., Martin-Benito J., Martinez-Ripoll M., Gavilanes J.G., Hermoso J.A. Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation. Structure 2003, 11:1319-1328.
    • (2003) Structure , vol.11 , pp. 1319-1328
    • Mancheno, J.M.1    Martin-Benito, J.2    Martinez-Ripoll, M.3    Gavilanes, J.G.4    Hermoso, J.A.5
  • 21
    • 33644503593 scopus 로고    scopus 로고
    • Isolation and characterization of lipid microdomains from apical and basolateral plasma membranes of rat hepatocytes
    • Mazzone A., Tietz P., Jefferson J., Pagano R., LaRusso N.F. Isolation and characterization of lipid microdomains from apical and basolateral plasma membranes of rat hepatocytes. Hepatology 2006, 43:287-296.
    • (2006) Hepatology , vol.43 , pp. 287-296
    • Mazzone, A.1    Tietz, P.2    Jefferson, J.3    Pagano, R.4    LaRusso, N.F.5
  • 23
    • 0021222922 scopus 로고
    • Bacterial toxins: cellular mechanisms of action
    • Middlebrook J.L., Dorland R.B. Bacterial toxins: cellular mechanisms of action. Microbiol. Rev. 1984, 48:199-221.
    • (1984) Microbiol. Rev. , vol.48 , pp. 199-221
    • Middlebrook, J.L.1    Dorland, R.B.2
  • 24
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: elusive or illusive?
    • Munro S. Lipid rafts: elusive or illusive?. Cell 2003, 115:377-388.
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 25
    • 0037304544 scopus 로고    scopus 로고
    • Properties of palmitoylphosphatidylcholine, sphingomyelin, and dihydrosphingomyelin bilayer membranes as reported by different fluorescent reporter molecules
    • Nyholm T., Nylund M., Soderholm A., Slotte J.P. Properties of palmitoylphosphatidylcholine, sphingomyelin, and dihydrosphingomyelin bilayer membranes as reported by different fluorescent reporter molecules. Biophys. J. 2003, 84:987-997.
    • (2003) Biophys. J. , vol.84 , pp. 987-997
    • Nyholm, T.1    Nylund, M.2    Soderholm, A.3    Slotte, J.P.4
  • 26
    • 0031880777 scopus 로고    scopus 로고
    • Use of Bodipy-labeled sphingolipids to study membrane traffic along the endocytic pathway
    • Pagano R.E., Chen C.S. Use of Bodipy-labeled sphingolipids to study membrane traffic along the endocytic pathway. Ann. N. Y. Acad. Sci. 1998, 845:152-160.
    • (1998) Ann. N. Y. Acad. Sci. , vol.845 , pp. 152-160
    • Pagano, R.E.1    Chen, C.S.2
  • 27
    • 77951877935 scopus 로고    scopus 로고
    • 1H, 13C, and 15N NMR assignments of StnII-Y111N, a highly impaired mutant of the sea anemone actinoporin Sticholysin II
    • Pardo-Cea M.A., Alegre-Cebollada J., Martinez-del-Pozo A., Gavilanes J.G., Bruix M. 1H, 13C, and 15N NMR assignments of StnII-Y111N, a highly impaired mutant of the sea anemone actinoporin Sticholysin II. Biomol. NMR Assign. 2010, 4:69-72.
    • (2010) Biomol. NMR Assign. , vol.4 , pp. 69-72
    • Pardo-Cea, M.A.1    Alegre-Cebollada, J.2    Martinez-del-Pozo, A.3    Gavilanes, J.G.4    Bruix, M.5
  • 28
    • 41149124594 scopus 로고    scopus 로고
    • Caveolae as organizers of pharmacologically relevant signal transduction molecules
    • Patel H.H., Murray F., Insel P.A. Caveolae as organizers of pharmacologically relevant signal transduction molecules. Annu. Rev. Pharmacol. Toxicol. 2008, 48:359-391.
    • (2008) Annu. Rev. Pharmacol. Toxicol. , vol.48 , pp. 359-391
    • Patel, H.H.1    Murray, F.2    Insel, P.A.3
  • 29
    • 0025092390 scopus 로고
    • Beta-bungarotoxin-mediated liposome fusion: spectroscopic characterization by fluorescence and ESR
    • Rufini S., Pedersen J.Z., Desideri A., Luly P. Beta-bungarotoxin-mediated liposome fusion: spectroscopic characterization by fluorescence and ESR. Biochemistry 1990, 29:9644-9651.
    • (1990) Biochemistry , vol.29 , pp. 9644-9651
    • Rufini, S.1    Pedersen, J.Z.2    Desideri, A.3    Luly, P.4
  • 30
    • 77957167810 scopus 로고    scopus 로고
    • Revitalizing membrane rafts: new tools and insights
    • Simons K., Gerl M.J. Revitalizing membrane rafts: new tools and insights. Nat. Rev. Mol. Cell Biol. 2010, 11:688-699.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 688-699
    • Simons, K.1    Gerl, M.J.2
  • 31
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., Ikonen E. Functional rafts in cell membranes. Nature 1997, 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 32
    • 0023377985 scopus 로고
    • Lipid composition and temperature adaptation of the nervous system of the leech Hirudo Medicinalis
    • Spinedi A., Rufini S., Luly P. Lipid composition and temperature adaptation of the nervous system of the leech Hirudo Medicinalis. J. Neurochem. 1987, 49:45-49.
    • (1987) J. Neurochem. , vol.49 , pp. 45-49
    • Spinedi, A.1    Rufini, S.2    Luly, P.3
  • 33
    • 77951910348 scopus 로고    scopus 로고
    • Ceramide-rich platforms in transmembrane signaling
    • Stancevic B., Kolesnick R. Ceramide-rich platforms in transmembrane signaling. FEBS Lett. 2010, 584:1728-1740.
    • (2010) FEBS Lett. , vol.584 , pp. 1728-1740
    • Stancevic, B.1    Kolesnick, R.2
  • 34
    • 0036424759 scopus 로고    scopus 로고
    • Investigation of cytolysin variants by peptide mapping: an enhanced protein characterization using complementary ionization and mass spectrometric techniques
    • Stevens S.M., Kem W.R., Prokai L. Investigation of cytolysin variants by peptide mapping: an enhanced protein characterization using complementary ionization and mass spectrometric techniques. Rapid Commun. Mass Spectrom. 2002, 16:1-8.
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 1-8
    • Stevens, S.M.1    Kem, W.R.2    Prokai, L.3
  • 35
    • 3042555480 scopus 로고    scopus 로고
    • Pleurotolysin, a novel sphingomyelin-specific two-component cytolysin from the edible mushroom Pleurotus ostreatus, assembles into a transmembrane pore complex
    • Tomita T., Noguchi K., Mimuro H., Ukaji F., Ito H., Sugawara-Tomita N., Hashimoto Y. Pleurotolysin, a novel sphingomyelin-specific two-component cytolysin from the edible mushroom Pleurotus ostreatus, assembles into a transmembrane pore complex. J. Biol. Chem. 2004, 279:26975-26982.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26975-26982
    • Tomita, T.1    Noguchi, K.2    Mimuro, H.3    Ukaji, F.4    Ito, H.5    Sugawara-Tomita, N.6    Hashimoto, Y.7
  • 36
    • 0029981514 scopus 로고    scopus 로고
    • Sorting of newly synthesized galactosphingolipids to the two surface domains of epithelial cells
    • Van der Bijl P., Lopes-Cardozo M., Van Meer G. Sorting of newly synthesized galactosphingolipids to the two surface domains of epithelial cells. J. Cell Biol. 1996, 132:813-821.
    • (1996) J. Cell Biol. , vol.132 , pp. 813-821
    • Van der Bijl, P.1    Lopes-Cardozo, M.2    Van Meer, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.