Effect of the hemolytic lectin CEL-III from Holothuroidea Cucumaria echinata on the ANS fluorescence responses in sensitive MDCK and resistant CHO cells

Journal of Biochemistry

Volumn 125, Issue 4, 1999, Pages 713-720

  Oda, Tatsuya ^a   Shinmura, Naoko ^a   Nishioka, Yuka ^a   Komatsu, Nobukazu ^a   Hatakeyama, Tomomitsu ^a   Muramatsu, Tsuyoshi ^a  

^a NAGASAKI UNIVERSITY   (Japan)

Author keywords

ANS fluorescence; CEL III; Cytotoxicity; Lectin; Pore forming protein

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; CALCIUM ION; LECTIN;

ANIMAL CELL; ARTICLE; CHO CELL; CYTOTOXICITY; FLUORESCENCE; HEMOLYSIS; HYDROPHOBICITY; IMMUNOBLOTTING; INVERTEBRATE; KIDNEY CELL; NONHUMAN; OLIGOMERIZATION;

ANIMALIA; CUCUMARIA ECHINATA; HOLOTHUROIDEA; INVERTEBRATA;

EID: 0032962923     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022341     Document Type: Article

References (30)

1. Komano, H., Mizuno, D., and Natori, S. (1980) Purification of lectin induced in the hemolymph of Sarcophaga peregrina larvae on injury. J. Biol. Chem. 255, 2919-2924
2. Yamazaki, M., Ikenami, M., Komano, H., Tsunawaki, S., Kamiya, H., Natori, S., and Mizuno, D. (1983) Polymorphonuclear leukocyte-mediated cytolysis induced by animal lectin. Gann 74, 576-583
3. Drickamer, K. (1988) Two distinct classes of carbohydrate-recognition domains in animal lectins. J. Biol. Chem. 263, 9557-9560
4. Barondes, S.H., Castronovo, V., Cooper, D.N.W., Cummings, R.D., Drickamer, K., Feizi, T., Gitt, M.A., Hirabayashi, J., Hughes, C., Kasai, K., Leffler, H., Liu, F.-T., Lotan, R., Mercurio, A.M., Monsigny, M., Pillai, S., Poirer, F., Raz, A., Rigby, P.W.J., Rini, J.M., and Wang, J.L. (1994) Galectins: A family of animal β-galactoside-binding lectins. Cell 76, 597-598
5. Giga, Y., Ikai, A., and Takahashi, K. (1987) The complete amino acid sequence of echinoidin, a lectin from the coelomic fluid of the sea urchin Anthocidaris crassispina. J. Biol. Chem. 262, 6197-6203
6. Muramoto, K. and Kamiya, H. (1990) The amino-acid sequences of multiple lectins of the acorn barnacle Megabalanus rosa and its homology with animal lectins. Biochim. Biophys. Acta 1039, 42-51
7. Suzuki, T., Takagi, T., Furukohri, T., Kawamura, K., and Nakauchi, M. (1990) A calcium-dependent galactose-binding lectin from the tunicate Polyandrocarpa misakiensis. J. Biol. Chem. 265, 1274-1281
8. Himeshima, T., Hatakeyama, T., and Yamasaki, N. (1994) Amino acid sequence of a lectin from the sea cucumber, Stichopus japonicus, and its structural relationship to the C-type animal lectin family. J. Biochem. 115, 689-692
9. 2+-dependent lectins from the marine invertebrate, Cucumaria echinata. J. Biochem. 116, 209-214
10. Hatakeyama, T., Nagatomo, H., and Yamasaki, N. (1995) Interaction of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata with the erythrocyte membrane. J. Biol. Chem. 270, 3560-3564
11. Jursch, R., Hildebrand, A., Hobom, G.,Traum-Jensen, J., Ward, R., Kehoe, M., and Bhakdi, S. (1994) Histidine residues near the N terminus of staphylococcal alpha-toxin as reporters of regions that are critical for oligomerization and pore formation. Infect. Immun. 62, 2249-2256
12. Walker, B., Krishnasastry, M., Zorn, L., and Bayley, H. (1992) Assembly of the oligomeric membrane pore formed by staphylococcal α-hemolysin examined by truncation mutagenesis. J. Biol. Chem. 267, 21782-21786
13. Parker, M.W., Buckley, J.T., Postma, J.P.M., Tucker, A.D., Leonard, K., Pattus, F., and Tsernoglou, D. (1994) Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature 367, 292-295
14. Bhakdi, S., Mackman, N., Nicaud, J.-M., and Holland, I.B. (1986) Escherichia coli hemolysin may damage target cell membranes by generating transmembrane pores. Infect. Immun. 52, 63-69
15. Oda, T., Tsuru, M., Hatakeyama, T., Nagatomo, H., Muramatsu, T., and Yamasaki, N. (1997) Temperature- and pH-dependent cytotoxic effect of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata on various cell lines. J. Biochem. 121, 560-567
16. Weber, L.D., Tulinsky, A., Johnson, D.J., and EI-Bayoumi, M.A. (1979) Expression of functionality of α-chymotrypsin. The structure of a fluorescent probe-α-chymotrypsin complex and the nature of its pH dependence. Biochemistry 18, 1297-1303
17. Andley, U.P. and Chakrabarti, B. (1981) Interaction of 8-anilino-1-naphthalenesulfonate with rod outer segment membrane. Biochemistry 20, 1687-1693
18. Fujiwara, T., Kuwahara, H., Hiromasa, Y., Niidome, T., Aoyagi, H., and Hatakeyama, T. (1997) Small-angle X-ray scattering study on CEL-III, a hemolytic lectin from Holothuroidea Cucumaria echinata, and its oligomer induced by the binding of specific carbohydrate. FEBS Lett. 414, 79-83
19. Mise, T., Funatsu, G., Ishiguro, M., and Funatsu, M. (1977) Isolation and characterization of ricin E from castor beans. Agric. Biol. Chem. 41, 2041-2046
20. Oda, T. and Maeda, H. (1987) Binding to and internalization by cultured cells of neocarzinostatin and enhancement of its actions by conjugation with lipophilic styrene-maleic acid copolymer. Cancer Res. 47, 3206-3211
21. Oda, T. and Wu, H.C. (1993) Cerulenin inhibits the cytotoxicity of ricin, modeccin, Pseudomonas toxin, and diphtheria toxin in brefeldin A-resistant cell lines. J. Biol. Chem. 268, 12596-12602
22. Ueno, T. and Sekine, T. (1978) Study on calcium transport by sarcoplasmic reticulum vesicles using fluorescence probes. J. Biochem. 84, 784-794
23. Bernheimer, A.W. and Rudy, B. (1986) Interactions between membranes and cytolytic peptides. Biochim. Biophys. Acta 864, 123-141
24. Hugo, F., Reichwein, J., Arvand, M., Krämer, S., and Bhakdi, S. (1986) Use of a monoclonal antibody to determine the mode of transmembrane pore formation by streptolysin O. Infect. Immun. 54, 641-645
25. Mangel, A., Leitão, J.M., Batel, R., Zimmermann, H., Müller, W.E.G., and Schröder, H.C. (1992) Purification and characterization of a pore-forming protein from the marine sponge Tethya lyncurium. Eur. J. Biochem. 210, 499-507
26. Hatakeyama, T., Miyamoto, Y., Nagatomo, H., Sallay, I., and Yamasaki, N. (1997) Carbohydrate-binding properties of the hemolytic lectin CEL-III from the Holothuroidea Cucumaria echinata as analyzed using carbohydrate-coated microplate. J. Biochem. 121, 63-67
27. Slavik, J. (1982) Anilinonaphthalene sulfonate as a probe of membrane composition and function. Biochim. Biophys. Acta 694, 1-25
28. Hildebrand, A., Pohl, M., and Bhakdi, S. (1991) Staphylococcus aureus α-toxin. J. Biol. Chem. 266, 17195-17200
29. Hatakeyama, T., Furukawa, M., Nagatomo, H., Yamasaki, N., and Mori, T. (1996) Oligomerization of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata induced by the binding of carbohydrate ligands. J. Biol. Chem. 271, 16915-16920
30. Yguerabide, J. and Foster, M.C. (1981) Fluorescence spectroscopy of biological membranes in Molecular Biology, Biochemistry and Biophysics (Grell, E., ed.) Vol. 31, pp. 246-250, Springer-Verlag, Berlin