메뉴 건너뛰기




Volumn 67, Issue 3, 1999, Pages 1139-1148

Vibrio parahaemolyticus thermostable direct hemolysin modulates cytoskeletal organization and calcium homeostasis in intestinal cultured cells

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CALCIUM; HEMOLYSIN; VIRULENCE FACTOR;

EID: 0033052675     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.67.3.1139-1148.1999     Document Type: Article
Times cited : (44)

References (25)
  • 1
    • 0032498627 scopus 로고    scopus 로고
    • A pore-forming toxin interacts with a GPI-anchored protein and causes vacuolation of the endoplasmic reticulum
    • Abrami, L., M. Fivaz, P. E. Glauser, R. G. Parton, and F. G. van der Goot. 1998. A pore-forming toxin interacts with a GPI-anchored protein and causes vacuolation of the endoplasmic reticulum. J. Cell Biol. 140:525-540.
    • (1998) J. Cell Biol. , vol.140 , pp. 525-540
    • Abrami, L.1    Fivaz, M.2    Glauser, P.E.3    Parton, R.G.4    Van Der Goot, F.G.5
  • 2
    • 0031988007 scopus 로고    scopus 로고
    • Toxins from anaerobic bacteria: Specificity and molecular mechanisms of action
    • Boquet, P., P. Munro, C. Florentini, and I. Just. 1998. Toxins from anaerobic bacteria: specificity and molecular mechanisms of action. Curr. Opin. Microbiol. 1:66-74.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 66-74
    • Boquet, P.1    Munro, P.2    Florentini, C.3    Just, I.4
  • 3
    • 0028244823 scopus 로고
    • Jasplakinolide, a cytotoxic natural product, induces action polymerization and competitively inhibits the binding of phalloidin to F-actin
    • Budd, M., A. Senderowicz, E. Sausville, K. Duncan, and E. Korn. 1994. Jasplakinolide, a cytotoxic natural product, induces action polymerization and competitively inhibits the binding of phalloidin to F-actin. J. Biol. Chem. 269:14869-14871.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14869-14871
    • Budd, M.1    Senderowicz, A.2    Sausville, E.3    Duncan, K.4    Korn, E.5
  • 4
    • 0020410432 scopus 로고
    • The purification of the Kanagawa haemolysin from Vibrio parahaemolyticus
    • Abstract
    • Cherwonogrodzky, J. W., and A. G. Clark. 1982. The purification of the Kanagawa haemolysin from Vibrio parahaemolyticus. FEMS Microbiol. Lett. 15:175. (Abstract.)
    • (1982) FEMS Microbiol. Lett. , vol.15 , pp. 175
    • Cherwonogrodzky, J.W.1    Clark, A.G.2
  • 5
    • 0031036984 scopus 로고    scopus 로고
    • Cytometry in cell necrobiology: Analysis of apoptosis and accidental cell death (necrosis)
    • Darzynkiewicz, Z., G. Juan, X. Li, W. Gorczyca, T. Murakami, and F. Traganos. 1997. Cytometry in cell necrobiology: analysis of apoptosis and accidental cell death (necrosis). Cytometry 27:1-20.
    • (1997) Cytometry , vol.27 , pp. 1-20
    • Darzynkiewicz, Z.1    Juan, G.2    Li, X.3    Gorczyca, W.4    Murakami, T.5    Traganos, F.6
  • 6
    • 0028525837 scopus 로고
    • Bacterial protein toxins acting on the cell cytoskeleton
    • Donelli, G., and C. Fiorentini. 1994. Bacterial protein toxins acting on the cell cytoskeleton. Microbiologica 17:345-362.
    • (1994) Microbiologica , vol.17 , pp. 345-362
    • Donelli, G.1    Fiorentini, C.2
  • 10
    • 0018217008 scopus 로고
    • Requirement of calcium ions for cell degeneration with a toxin (vibriolysin) from Vibrio parahaemolyticus
    • Goshima, K., K. Owaribe, H. Yamanaka, and S. Yoshino. 1978. Requirement of calcium ions for cell degeneration with a toxin (vibriolysin) from Vibrio parahaemolyticus. Infect. Immun. 22:821-832.
    • (1978) Infect. Immun. , vol.22 , pp. 821-832
    • Goshima, K.1    Owaribe, K.2    Yamanaka, H.3    Yoshino, S.4
  • 11
    • 0027080440 scopus 로고
    • The thermostable direct hemolysin of Vibrio parahaemolyticus is a pore forming toxin
    • Honda, T., Y. Ni, T. Miwatani, T. Adachi, and J. Kim. 1992. The thermostable direct hemolysin of Vibrio parahaemolyticus is a pore forming toxin. Can. J. Microbiol. 38:1175-1180.
    • (1992) Can. J. Microbiol. , vol.38 , pp. 1175-1180
    • Honda, T.1    Ni, Y.2    Miwatani, T.3    Adachi, T.4    Kim, J.5
  • 12
    • 0027233062 scopus 로고
    • The pathogenicity of Vibrio parahaemolyticus and the role of the thermostable direct hemolysin and related hemolysins
    • Honda, T., and T. Iida. 1993. The pathogenicity of Vibrio parahaemolyticus and the role of the thermostable direct hemolysin and related hemolysins. Rev. Med. Microbiol. 4:106-113.
    • (1993) Rev. Med. Microbiol. , vol.4 , pp. 106-113
    • Honda, T.1    Iida, T.2
  • 13
    • 0027378511 scopus 로고
    • Cation flux studies of the lesion induced in human erythrocyte membranes by the thermostable direct hemolysin of Vibrio parahaemolyticus
    • Huntley, J. S., A. C. Hall, V. Sathyamoorthy, and R. H. Hall. 1993. Cation flux studies of the lesion induced in human erythrocyte membranes by the thermostable direct hemolysin of Vibrio parahaemolyticus. Infect. Immun. 61:4326-4332.
    • (1993) Infect. Immun. , vol.61 , pp. 4326-4332
    • Huntley, J.S.1    Hall, A.C.2    Sathyamoorthy, V.3    Hall, R.H.4
  • 14
    • 0027970243 scopus 로고
    • Aspects of the haemolytic reaction induced by Kanagawa haemolysin of Vibrio parahaemolyticus
    • Huntley, J. S., and A. C. Hall. 1994. Aspects of the haemolytic reaction induced by Kanagawa haemolysin of Vibrio parahaemolyticus. Toxicon 32: 1397-1412.
    • (1994) Toxicon , vol.32 , pp. 1397-1412
    • Huntley, J.S.1    Hall, A.C.2
  • 15
    • 0023683788 scopus 로고
    • Current perspectives on the epidemiology and pathogenesis of clinically significant Vibrio spp Clin
    • Janda, J. M., C. Powers, R. G. Bryant, and S. L. Abbott. 1988. Current perspectives on the epidemiology and pathogenesis of clinically significant Vibrio spp Clin. Microbiol. Rev. 1:245-267.
    • (1988) Microbiol. Rev. , vol.1 , pp. 245-267
    • Janda, J.M.1    Powers, C.2    Bryant, R.G.3    Abbott, S.L.4
  • 16
    • 0023252077 scopus 로고
    • A mitotic form of the Golgi apparatus in HeLa cells
    • Lucocq, J. M., J. G. Pryde, E. G. Berger, and G. Warren. 1987. A mitotic form of the Golgi apparatus in HeLa cells. J. Cell Biol. 104:865-874.
    • (1987) J. Cell Biol. , vol.104 , pp. 865-874
    • Lucocq, J.M.1    Pryde, J.G.2    Berger, E.G.3    Warren, G.4
  • 17
    • 0030043134 scopus 로고    scopus 로고
    • Aerolysin - The ins and outs of a model channel-forming toxin
    • Parker, M. W., F. G. van der Goot, and J. T. Buckley. 1996. Aerolysin - the ins and outs of a model channel-forming toxin. Mol. Microbiol. 19:205-212.
    • (1996) Mol. Microbiol. , vol.19 , pp. 205-212
    • Parker, M.W.1    Van Der Goot, F.G.2    Buckley, J.T.3
  • 18
    • 0029103068 scopus 로고
    • Calcium-dependent intestinal chloride secretion by Vibrio parahaemolyticus thermostable direct hemolysin in a rabbit model
    • Raimondi, F., J. P. Kao, J. B. Kaper, S. Guandalini, and A. Fasano. 1995. Calcium-dependent intestinal chloride secretion by Vibrio parahaemolyticus thermostable direct hemolysin in a rabbit model. Gastroenterology 109:381-386.
    • (1995) Gastroenterology , vol.109 , pp. 381-386
    • Raimondi, F.1    Kao, J.P.2    Kaper, J.B.3    Guandalini, S.4    Fasano, A.5
  • 19
    • 0017287479 scopus 로고
    • Cytotoxic effect of the thermostable direct hemolysin produced by Vibrio parahaemolyticus on FL cells
    • Sakurai, J., T. Honda, Y. Jinguji, M. Arita, and T. Miwatani. 1976. Cytotoxic effect of the thermostable direct hemolysin produced by Vibrio parahaemolyticus on FL cells. Infect. Immun. 13:876-883.
    • (1976) Infect. Immun. , vol.13 , pp. 876-883
    • Sakurai, J.1    Honda, T.2    Jinguji, Y.3    Arita, M.4    Miwatani, T.5
  • 20
    • 0024268113 scopus 로고
    • Thermostable direct hemolysin of Vibrio parahaemolyticus
    • Takeda, Y. 1988. Thermostable direct hemolysin of Vibrio parahaemolyticus. Methods Enzymol. 165:189-193.
    • (1988) Methods Enzymol. , vol.165 , pp. 189-193
    • Takeda, Y.1
  • 21
    • 0020309153 scopus 로고
    • Thermostable direct hemolysin of Vibrio parahaemolyticus
    • Takeda, Y. 1983. Thermostable direct hemolysin of Vibrio parahaemolyticus. Pharmacol. Ther. 19:123-146.
    • (1983) Pharmacol. Ther. , vol.19 , pp. 123-146
    • Takeda, Y.1
  • 22
    • 0017169549 scopus 로고
    • Inactivation of the biological activities of the thermostable direct hemolysin of Vibrio parahaemolyticus by ganglioside GT1
    • Takeda, Y., T. Takeda, T. Honda, and T. Miwatani. 1976. Inactivation of the biological activities of the thermostable direct hemolysin of Vibrio parahaemolyticus by ganglioside GT1. Infect. Immun. 14:1-5.
    • (1976) Infect. Immun. , vol.14 , pp. 1-5
    • Takeda, Y.1    Takeda, T.2    Honda, T.3    Miwatani, T.4
  • 23
    • 0027930306 scopus 로고
    • A mutant toxin of Vibrio parahaemolyticus thermostable direct hemolysin which has lost hemolytic activity but retains ability to bind to erythrocytes
    • Tang, G. Q., T. Iida, K. Yamamoto, T. Honda. 1994. A mutant toxin of Vibrio parahaemolyticus thermostable direct hemolysin which has lost hemolytic activity but retains ability to bind to erythrocytes. Infect. Immun. 62:3299-3304.
    • (1994) Infect. Immun. , vol.62 , pp. 3299-3304
    • Tang, G.Q.1    Iida, T.2    Yamamoto, K.3    Honda, T.4
  • 24
    • 0028972794 scopus 로고
    • Ca+2-independent cytotoxicity of Vibrio parahaemolyticus thermostable direct hemolysin (TDH) on Intestine 407, a cell line derived from human embryonic intestine
    • Tang, G. Q., T. Iida, K. Yamamoto, and T. Honda. 1995. Ca+2-independent cytotoxicity of Vibrio parahaemolyticus thermostable direct hemolysin (TDH) on Intestine 407, a cell line derived from human embryonic intestine. FEMS Microbiol. Lett. 134:233-238.
    • (1995) FEMS Microbiol. Lett. , vol.134 , pp. 233-238
    • Tang, G.Q.1    Iida, T.2    Yamamoto, K.3    Honda, T.4
  • 25
    • 0027183419 scopus 로고
    • Membrane partitioning during cell division
    • Warren, G. 1993. Membrane partitioning during cell division. Annu. Rev. Biochem. 62:323-348.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 323-348
    • Warren, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.