메뉴 건너뛰기




Volumn 98, Issue 3, 1996, Pages 641-649

Rabbit sucrase-isomaltase contains a functional intestinal receptor for Clostridium difficile toxin A

Author keywords

Clostridium difficile; enterotoxin; lectin binding; sucrase isomaltase; toxin receptor

Indexed keywords

CLOSTRIDIUM DIFFICILE TOXIN A; ENTEROTOXIN; GALACTOSE; SUCRASE ISOMALTASE;

EID: 10244233005     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI118835     Document Type: Article
Times cited : (91)

References (56)
  • 4
    • 0023852615 scopus 로고
    • Effects of Clostridium difficile toxins A and B in rabbit small and large intestine in vivo and on cultured cells in vitro
    • Lima, A.A.M., D.M. Lyerly, T.D. Wilkins, D.J. Innes, and R.L. Guerrant. 1988. Effects of Clostridium difficile toxins A and B in rabbit small and large intestine in vivo and on cultured cells in vitro. Infect. Immun. 56:582-588.
    • (1988) Infect. Immun. , vol.56 , pp. 582-588
    • Lima, A.A.M.1    Lyerly, D.M.2    Wilkins, T.D.3    Innes, D.J.4    Guerrant, R.L.5
  • 6
    • 0028948208 scopus 로고
    • The low molecular mass GTP-binding protein Rho is affected by toxin A from Clostridium difficile
    • Just, I., J. Selzer, C. Von Eichel-Striber, and K. Aktories. 1995. The low molecular mass GTP-binding protein Rho is affected by toxin A from Clostridium difficile. J. Clin. Invest. 95:1026-1031.
    • (1995) J. Clin. Invest. , vol.95 , pp. 1026-1031
    • Just, I.1    Selzer, J.2    Von Eichel-Striber, C.3    Aktories, K.4
  • 8
    • 0026089562 scopus 로고
    • Protection against experimental pseudomembranous enterocolitis in gnotobiotic mice by use of monoclonal antibodies against Clostridium difficile toxin A
    • Corthier, G., M.C. Muller, T.D. Wilkins, D.M. Lyerly, and R.L. Haridon. 1991. Protection against experimental pseudomembranous enterocolitis in gnotobiotic mice by use of monoclonal antibodies against Clostridium difficile toxin A. Infect. Immun. 59:1192-1195.
    • (1991) Infect. Immun. , vol.59 , pp. 1192-1195
    • Corthier, G.1    Muller, M.C.2    Wilkins, T.D.3    Lyerly, D.M.4    Haridon, R.L.5
  • 9
    • 0025030511 scopus 로고
    • Vaccination against lethal Clostridium difficile enterocolitis with a nontoxic recombinant peptide of toxin A
    • Lyerly, D.M., J.L. Johnson, S.M. Frey, and T.D. Wilkins. 1990. Vaccination against lethal Clostridium difficile enterocolitis with a nontoxic recombinant peptide of toxin A. Curr. Microbiol. 21:29-32.
    • (1990) Curr. Microbiol. , vol.21 , pp. 29-32
    • Lyerly, D.M.1    Johnson, J.L.2    Frey, S.M.3    Wilkins, T.D.4
  • 10
    • 0025893128 scopus 로고
    • Characterization of rabbit ileal receptors for Clostridium difficile toxin A. Evidence for a receptor-coupled G pathway
    • Pothoulakis, C., J.T. LaMont, R. Eglow, N. Gao, J.B. Rubins, T.C. Theoharides, and B.F. Dickey. 1991. Characterization of rabbit ileal receptors for Clostridium difficile toxin A. Evidence for a receptor-coupled G pathway. J. Clin. Invest. 88:119-125.
    • (1991) J. Clin. Invest. , vol.88 , pp. 119-125
    • Pothoulakis, C.1    LaMont, J.T.2    Eglow, R.3    Gao, N.4    Rubins, J.B.5    Theoharides, T.C.6    Dickey, B.F.7
  • 11
    • 0022525082 scopus 로고
    • Cell surface binding site for Clostridium difficile enterotoxin: Evidence for a glycoconjugate containing the sequence Galα1-3Galβ1-4GlcNAc
    • Krivan, H., C.F. Klark, D.F. Smith, and T.D. Wilkins. 1986. Cell surface binding site for Clostridium difficile enterotoxin: evidence for a glycoconjugate containing the sequence Galα1-3Galβ1-4GlcNAc. Infect. Immun. 53:573-581.
    • (1986) Infect. Immun. , vol.53 , pp. 573-581
    • Krivan, H.1    Klark, C.F.2    Smith, D.F.3    Wilkins, T.D.4
  • 12
    • 0027256162 scopus 로고
    • Purification of a functional receptor for Clostridium difficile toxin A from intestinal brush border membranes of infant hamsters
    • Rolfe, R.D., and W. Song. 1993. Purification of a functional receptor for Clostridium difficile toxin A from intestinal brush border membranes of infant hamsters. Clin. Infect. Dis. 16(Suppl. 4):S219-S227.
    • (1993) Clin. Infect. Dis. , vol.16 , Issue.4 SUPPL.
    • Rolfe, R.D.1    Song, W.2
  • 13
  • 17
    • 0344655717 scopus 로고
    • Comparative study of Clostridium difficile toxin A and cholera toxin in rabbit ileum. Role of prostaglandins and leukotrienes
    • Triadafilopoulos, G., C. Pothoulakis, R. Weiss, C. Giampaolo, and J.T. LaMont. 1987. Comparative study of Clostridium difficile toxin A and cholera toxin in rabbit ileum. Role of prostaglandins and leukotrienes. Gastroenterology. 92:1174-1180.
    • (1987) Gastroenterology , vol.92 , pp. 1174-1180
    • Triadafilopoulos, G.1    Pothoulakis, C.2    Weiss, R.3    Giampaolo, C.4    LaMont, J.T.5
  • 21
    • 0025977235 scopus 로고
    • Construction and expression of the complete Clostridium difficile toxin A gene in Escherichia coli
    • Phelps, C.J., D.M. Lyerly, T.D. Johnson, and T.D. Wilkins. 1990. Construction and expression of the complete Clostridium difficile toxin A gene in Escherichia coli. Infect. Immun. 59:150-153.
    • (1990) Infect. Immun. , vol.59 , pp. 150-153
    • Phelps, C.J.1    Lyerly, D.M.2    Johnson, T.D.3    Wilkins, T.D.4
  • 24
    • 0026764540 scopus 로고
    • Localization of two epitopes recognized by monoclonal antibody PCG-4 on Clostridium difficile toxin A
    • Frey, S.M., and T.D. Wilkins. 1992. Localization of two epitopes recognized by monoclonal antibody PCG-4 on Clostridium difficile toxin A. Infect. Immun. 60:2488-2492.
    • (1992) Infect. Immun. , vol.60 , pp. 2488-2492
    • Frey, S.M.1    Wilkins, T.D.2
  • 25
    • 0020971364 scopus 로고
    • A computerized analysis of ligand binding data
    • Munson, P. 1983. A computerized analysis of ligand binding data. Methods Enzymol. 92:543-576.
    • (1983) Methods Enzymol. , vol.92 , pp. 543-576
    • Munson, P.1
  • 26
    • 0022504432 scopus 로고
    • The sucrase-isomaltase complex: Primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein
    • Hunziker, W., M. Spiess, G. Semenza, and H.F. Lodish. 1986. The sucrase-isomaltase complex: primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein. Cell. 46:227-234.
    • (1986) Cell , vol.46 , pp. 227-234
    • Hunziker, W.1    Spiess, M.2    Semenza, G.3    Lodish, H.F.4
  • 27
    • 0015847039 scopus 로고
    • A new technique for the assay of infectivity of human adenovirus 5 DNA
    • Graham, F.J., and A. Van der Eb. 1973. A new technique for the assay of infectivity of human adenovirus 5 DNA. Virology. 52:456-460.
    • (1973) Virology , vol.52 , pp. 456-460
    • Graham, F.J.1    Van Der Eb, A.2
  • 28
    • 0021710934 scopus 로고
    • Hygromycin B phosphotransferase as a selectable marker for DNA transfer experiments with higher eukaryotic cells
    • Blochlinger, K., and H. Diggelmann. 1984. Hygromycin B phosphotransferase as a selectable marker for DNA transfer experiments with higher eukaryotic cells. Mol. Cell. Biol. 4:2929-2931.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 2929-2931
    • Blochlinger, K.1    Diggelmann, H.2
  • 29
    • 0021838285 scopus 로고
    • Construction of a fusion gene that confers resistance against hygromycin B to mammalian cells in culture
    • Bernard, U.H., G. Kramer, and W.G. Rowekamp. 1985. Construction of a fusion gene that confers resistance against hygromycin B to mammalian cells in culture. Exp. Cell Res. 158:237-243.
    • (1985) Exp. Cell Res. , vol.158 , pp. 237-243
    • Bernard, U.H.1    Kramer, G.2    Rowekamp, W.G.3
  • 30
    • 0021101221 scopus 로고
    • Analysis of a bacterial hygromycin B resistance gene by transcriptional and translational fusions and by DNA sequencing
    • Kaster, K.R., S.G. Burgett, R.N. Rao, and T.D. Ingolia. 1983. Analysis of a bacterial hygromycin B resistance gene by transcriptional and translational fusions and by DNA sequencing. Nucleic Acids Res. 11:6895-6911.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 6895-6911
    • Kaster, K.R.1    Burgett, S.G.2    Rao, R.N.3    Ingolia, T.D.4
  • 31
    • 0023277545 scopus 로고
    • Single-step method for RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and N. Sacchi. 1987. Single-step method for RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 32
    • 4444368426 scopus 로고
    • Method for assay of intestinal disaccharidases
    • Dahlqvist, A. 1964. Method for assay of intestinal disaccharidases. Anal. Biochem. 7:18-25.
    • (1964) Anal. Biochem. , vol.7 , pp. 18-25
    • Dahlqvist, A.1
  • 33
    • 0028944568 scopus 로고
    • Clostridium difficile toxin B activates calcium influx which is required for actin disassembly during cytotoxicity
    • Gilbert, R.J., C. Pothoulakis, J.T. LaMont, and M. Yakubovich. 1995. Clostridium difficile toxin B activates calcium influx which is required for actin disassembly during cytotoxicity. Am. J. Physiol. 268:G487-G495.
    • (1995) Am. J. Physiol. , vol.268
    • Gilbert, R.J.1    Pothoulakis, C.2    LaMont, J.T.3    Yakubovich, M.4
  • 35
    • 0023928894 scopus 로고
    • Clostridium difficile toxin A stimulates intracellular calcium release and chemotactic response in human neutrophils
    • Pothoulakis, C., R. Sullivan, D.A. Melnick, A.S. Gadenne, T. Meshulan, and J.T. LaMont. 1988. Clostridium difficile toxin A stimulates intracellular calcium release and chemotactic response in human neutrophils. J. Clin. Invest. 81: 1741-1745.
    • (1988) J. Clin. Invest. , vol.81 , pp. 1741-1745
    • Pothoulakis, C.1    Sullivan, R.2    Melnick, D.A.3    Gadenne, A.S.4    Meshulan, T.5    LaMont, J.T.6
  • 36
    • 0025551066 scopus 로고
    • Regulation of sucrase-isomaltase gene expression along the crypt-villus axis of rat small intestine
    • Traber, P.G. 1990. Regulation of sucrase-isomaltase gene expression along the crypt-villus axis of rat small intestine. Biochem. Biophys. Res. Commun. 173:765-773.
    • (1990) Biochem. Biophys. Res. Commun. , vol.173 , pp. 765-773
    • Traber, P.G.1
  • 37
    • 0018389608 scopus 로고
    • The mode of association of the enzyme complex sucrase-isomaltase with the intestinal brush border membrane
    • Brunner, J., H. Hauser, H. Braun, K.J. Wilson, H. Wacker, B. O'Neill, and G. Semenza. 1979. The mode of association of the enzyme complex sucrase-isomaltase with the intestinal brush border membrane. J. Biol. Chem. 254: 1821-1828.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1821-1828
    • Brunner, J.1    Hauser, H.2    Braun, H.3    Wilson, K.J.4    Wacker, H.5    O'Neill, B.6    Semenza, G.7
  • 38
    • 0025026471 scopus 로고
    • A pertussis toxin-sensitive G-protein mediates some aspects of insulin action in BC3H-1 murine myocytes
    • Luttrell, L., E. Kilgour, J. Larner, and G. Romero. 1990. A pertussis toxin-sensitive G-protein mediates some aspects of insulin action in BC3H-1 murine myocytes. J. Biol. Chem. 265:16873-16879.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16873-16879
    • Luttrell, L.1    Kilgour, E.2    Larner, J.3    Romero, G.4
  • 39
    • 0028923485 scopus 로고
    • A region in the cytosolic domain of the epidermal growth factor receptor antithetically regulates the stimulatory and inhibitory guanine nucleotide-binding regulatory proteins of adenylyl cyclase
    • Sun, H., J.M. Seyer, and T.B. Patel. 1995. A region in the cytosolic domain of the epidermal growth factor receptor antithetically regulates the stimulatory and inhibitory guanine nucleotide-binding regulatory proteins of adenylyl cyclase. Proc. Natl. Acad. Sci. USA. 92:2229-2233.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2229-2233
    • Sun, H.1    Seyer, J.M.2    Patel, T.B.3
  • 41
    • 0029094342 scopus 로고
    • Activation of a G protein complex by aggregation of β-1.4-galactosyltransferase of the surface of the sperm
    • Gong, X., D.H. Dubois, D.J. Miller, and B.D. Shur. 1995. Activation of a G protein complex by aggregation of β-1.4-galactosyltransferase of the surface of the sperm. Science (Wash. DC). 269:1718-1721.
    • (1995) Science (Wash. DC) , vol.269 , pp. 1718-1721
    • Gong, X.1    Dubois, D.H.2    Miller, D.J.3    Shur, B.D.4
  • 42
    • 0028807998 scopus 로고
    • Phosphorylation of the N-terminal intracellular tail of sucrase-isomaltase by cAMP-dependent protein kinase
    • Keller, P., G. Semenza, and S. Shaltiel. 1995. Phosphorylation of the N-terminal intracellular tail of sucrase-isomaltase by cAMP-dependent protein kinase. Eur. J. Biochem. 233:963-968.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 963-968
    • Keller, P.1    Semenza, G.2    Shaltiel, S.3
  • 44
    • 0026555970 scopus 로고
    • Sucrase-isomaltase gene expression along the crypt-villus axis of human small intestine is regulated at level of mRNA abundance
    • Gastrointest. Liver Physiol. 25
    • Traber, P.G., Y. Lai, G.D. Wu, and T.A. Judge. 1992. Sucrase-isomaltase gene expression along the crypt-villus axis of human small intestine is regulated at level of mRNA abundance. Am. J. Physiol. 262(Gastrointest. Liver Physiol. 25):G123-G130.
    • (1992) Am. J. Physiol. , vol.262
    • Traber, P.G.1    Lai, Y.2    Wu, G.D.3    Judge, T.A.4
  • 45
    • 0025297184 scopus 로고
    • Enterotoxins from Clostridiuin difficile; diarrhoeogenic potency and morphological effects in the rat intestine
    • Torres, J., E. Jennische, S. Lang, und I. Lonnroth, 1990. Enterotoxins from Clostridiuin difficile; diarrhoeogenic potency and morphological effects in the rat intestine. Gut. 31:781-785.
    • (1990) Gut , vol.31 , pp. 781-785
    • Torres, J.1    Jennische, E.2    Lang, S.3    Lonnroth, I.4
  • 46
    • 0016767705 scopus 로고
    • Catalytically inactive sucrase antigen of rabbit small intestine: The enzyme precursor
    • Dubs, R., R. Gitzelmann, B. Steinmann, and J. Lindermann. 1975. Catalytically inactive sucrase antigen of rabbit small intestine: the enzyme precursor. Helv. Paediatr. Acta. 30:89-102.
    • (1975) Helv. Paediatr. Acta , vol.30 , pp. 89-102
    • Dubs, R.1    Gitzelmann, R.2    Steinmann, B.3    Lindermann, J.4
  • 48
    • 0020520658 scopus 로고
    • A role of the B-oligomer moiety of islet activating protein, pertussis toxin, in development of the biologic effects on intact cells
    • Tamura, M., K. Nogimory, M. Yajima, K. Ase, and M. Ui. 1983. A role of the B-oligomer moiety of islet activating protein, pertussis toxin, in development of the biologic effects on intact cells. J. Biol. Chem. 258:6756-6761.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6756-6761
    • Tamura, M.1    Nogimory, K.2    Yajima, M.3    Ase, K.4    Ui, M.5
  • 49
    • 0005836734 scopus 로고
    • A protein factor responsible for the early cytopathic effect of adenoviruses
    • Pereira, H.G. 1958. A protein factor responsible for the early cytopathic effect of adenoviruses. Virology. 6:601-611.
    • (1958) Virology , vol.6 , pp. 601-611
    • Pereira, H.G.1
  • 50
    • 0027435087 scopus 로고
    • Integrins as receptors for virus attachment and cell entry
    • Bergelson, J.M., and R.W. Finberg. 1993. Integrins as receptors for virus attachment and cell entry. Trends Microbiol. 1:287-288.
    • (1993) Trends Microbiol. , vol.1 , pp. 287-288
    • Bergelson, J.M.1    Finberg, R.W.2
  • 54
    • 0026078094 scopus 로고
    • Toxin A of Clostridium difficile binds to the human carbohydrate antigens I, X, and Y
    • Tucker, K.T., and T.D. Wilkins. 1991. Toxin A of Clostridium difficile binds to the human carbohydrate antigens I, X, and Y. Infect. Immun. 59:73-78.
    • (1991) Infect. Immun. , vol.59 , pp. 73-78
    • Tucker, K.T.1    Wilkins, T.D.2
  • 55
    • 0019868369 scopus 로고
    • Interaction of cholera toxin with ral intestinal brush border membranes
    • Critchley, D.R., J.L. Magnani, and P.H. Fishman. 1981. Interaction of cholera toxin with ral intestinal brush border membranes. J. Biol. Chem. 256: 8724-8731.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8724-8731
    • Critchley, D.R.1    Magnani, J.L.2    Fishman, P.H.3
  • 56
    • 0027282778 scopus 로고
    • Xenogenic thyroid-stimulating hormone-like activity of the human anti-Gal antibody. Interaction of anti-Gal with porcine thyrocytes and with recombinant human thyroid-stimulating hormone receptors expressed on mouse cells
    • Winand, R.J., F. Anaraki, J. Etienne-Decerf, and U. Galili. 1993. Xenogenic thyroid-stimulating hormone-like activity of the human anti-Gal antibody. Interaction of anti-Gal with porcine thyrocytes and with recombinant human thyroid-stimulating hormone receptors expressed on mouse cells. J. Immunol. 151:3923-3934.
    • (1993) J. Immunol. , vol.151 , pp. 3923-3934
    • Winand, R.J.1    Anaraki, F.2    Etienne-Decerf, J.3    Galili, U.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.