메뉴 건너뛰기




Volumn 184, Issue 3, 1996, Pages 1045-1059

Role of the glycocalyx in regulating access of microparticles to apical plasma membranes of intestinal epithelial cells: Implications for microbial attachment and oral vaccine targeting

Author keywords

[No Author keywords available]

Indexed keywords

CHOLERA TOXIN; GLYCOLIPID; ISOTHIOCYANIC ACID;

EID: 0029787628     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.184.3.1045     Document Type: Article
Times cited : (365)

References (52)
  • 1
    • 0030000550 scopus 로고    scopus 로고
    • Antigen sampling across epithelial barriers and induction of niucosal immune responses
    • Neutra, M.R., E. Pringault, andJ.P. Kraehenbuhl. 1996. Antigen sampling across epithelial barriers and induction of niucosal immune responses. Atmmun. Rev. Iinniuiiol. 14:275-300.
    • (1996) Atmmun. Rev. Iinniuiiol. , vol.14 , pp. 275-300
    • Neutra, M.R.1    Pringault, E.2    Kraehenbuhl, J.P.3
  • 2
    • 0026605546 scopus 로고
    • Transepithelial transport and mucosal defense: The role of M cells
    • Neutra, M.R., and J.P. Kraehenbuhl. 1992. Transepithelial transport and mucosal defense: the role of M cells. Trends Cell Dial. 2:134-138.
    • (1992) Trends Cell Dial. , vol.2 , pp. 134-138
    • Neutra, M.R.1    Kraehenbuhl, J.P.2
  • 3
    • 0026521943 scopus 로고
    • Transepithelial transport and mucosal defense: Secretion of IgA
    • Kraehenbuhl, J.P., and M.R. Neutra. 1992. Transepithelial transport and mucosal defense: secretion of IgA. Trends Cell Bid. 2:170-174.
    • (1992) Trends Cell Bid. , vol.2 , pp. 170-174
    • Kraehenbuhl, J.P.1    Neutra, M.R.2
  • 6
    • 0027056687 scopus 로고
    • Bacterial mucosal vaccines. /// Genetically Engineered Vaccines
    • Mekalanos, J.J. 1992. Bacterial mucosal vaccines. /// Genetically Engineered Vaccines. Advances in Experimental Medicine and Biology-. Vol. 237. J.E. Ciardi, J.R. McGhee, and J.M. Kieth, editors. Plenum Press, New York. 43-50.
    • (1992) Advances in Experimental Medicine and Biology-. , vol.237 , pp. 43-50
    • Mekalanos, J.J.1
  • 9
    • 0028798530 scopus 로고
    • Uptake and transport of copolymer biodegradable microspheres by rabbit Peyer's patch M cells
    • Ermak, T.H., E.P. Dougherty, H.R. Bhaçat, Z. Kabok, and J. Pappo. 1995. Uptake and transport of copolymer biodegradable microspheres by rabbit Peyer's patch M cells. Cell Tissue Res. 279:433-436.
    • (1995) Cell Tissue Res. , vol.279 , pp. 433-436
    • Ermak, T.H.1    Dougherty, E.P.2    Bhaçat, H.R.3    Kabok, Z.4    Pappo, J.5
  • 10
    • 0024594088 scopus 로고
    • Uptake and translocation of fluorescent latex particles by rabbit Peyer's patch follicle epithelium: A quantitative model for M cell uptake
    • Pappo, J., and T.H. Ermak. 1989. Uptake and translocation of fluorescent latex particles by rabbit Peyer's patch follicle epithelium: a quantitative model for M cell uptake. Clin. Exp. Inwniiwl. 76:144-148.
    • (1989) Clin. Exp. Inwniiwl. , vol.76 , pp. 144-148
    • Pappo, J.1    Ermak, T.H.2
  • 11
    • 0026950068 scopus 로고
    • Confocal analysis of fluorescent bead uptake by mouse Peyer's patch follicle-associated M cells
    • Porta, C., P.S. James, A.D. Phillips, T.C. Savidge, M.W. Smith, and D. Cremaschi. 1992. Confocal analysis of fluorescent bead uptake by mouse Peyer's patch follicle-associated M cells. Exp. Physiol. 77:929-932.
    • (1992) Exp. Physiol. , vol.77 , pp. 929-932
    • Porta, C.1    James, P.S.2    Phillips, A.D.3    Savidge, T.C.4    Smith, M.W.5    Cremaschi, D.6
  • 12
    • 0026458260 scopus 로고
    • Structure and function of cholera toxin and the related Eschcrichia coli heat-labile enterotoxin
    • Spangler, B.D. 1992. Structure and function of cholera toxin and the related Eschcrichia coli heat-labile enterotoxin. Microbiol. Rci. 56:622-647.
    • (1992) Microbiol. Rci. , vol.56 , pp. 622-647
    • Spangler, B.D.1
  • 13
    • 0026681578 scopus 로고
    • Mechanism of cholera toxin action on a polarized human intestinal epithelial cell line: Role of vesicular traffic
    • Lencer, W.I., C. Delp, M.R. Neutra, and J.L. Madara. 1992. Mechanism of cholera toxin action on a polarized human intestinal epithelial cell line: role of vesicular traffic. J. Cell Bid. 117:1197-1209.
    • (1992) J. Cell Bid. , vol.117 , pp. 1197-1209
    • Lencer, W.I.1    Delp, C.2    Neutra, M.R.3    Madara, J.L.4
  • 14
    • 0024565465 scopus 로고
    • Oral administration of a streptococcal antigen coupled to cholera toxin B subunit evokes strong antibody.responses in salivary glands and extramucosal tissues
    • Czerkinsky, C., M.W. Russell, N. Lycke, M Lindblad, andj. Holmgren. 1989. Oral administration of a streptococcal antigen coupled to cholera toxin B subunit evokes strong antibody.responses in salivary glands and extramucosal tissues. Infect. Immummunn. 57:1072-1077.
    • (1989) Infect. Immummunn. , vol.57 , pp. 1072-1077
    • Czerkinsky, C.1    Russell, M.W.2    Lycke, N.3    Lindblad, M.4    Holmgren, A.5
  • 15
    • 0022172245 scopus 로고
    • Organization, chemistry and assembly of the cytoskeletal apparatus of the intestinal brush border
    • Mooseker, M.S. 1985. Organization, chemistry and assembly of the cytoskeletal apparatus of the intestinal brush border. Anmi. Rev. Cell Bhl. 1:209-241.
    • (1985) Anmi. Rev. Cell Bhl. , vol.1 , pp. 209-241
    • Mooseker, M.S.1
  • 16
    • 0022854871 scopus 로고
    • Anchoring and biosynthesis of stalked brush border membrane glycoproteins
    • Semenza, G. 1986. Anchoring and biosynthesis of stalked brush border membrane glycoproteins. Annii. Rev. Cell Dial. 2:255-314.
    • (1986) Annii. Rev. Cell Dial. , vol.2 , pp. 255-314
    • Semenza, G.1
  • 17
    • 0016401870 scopus 로고
    • Form and function of the glycocalyx on free cell surfaces
    • Ito, S. 1974. Form and function of the glycocalyx on free cell surfaces. Philos. Tr,ms. R. See. Loud. B. Bhl. Sä. 268:55-66.
    • (1974) Philos. Tr,ms. R. See. Loud. B. Bhl. Sä. , vol.268 , pp. 55-66
    • Ito, S.1
  • 18
    • 0028933093 scopus 로고
    • The filamentous brush border glycocalyx, a mucin-like marker of enterocyte hyper-polarization
    • Maury, J., C. Nicoletti, I. Guzzo-Chambraud, and S. Maroux. 1995. The filamentous brush border glycocalyx, a mucin-like marker of enterocyte hyper-polarization. Eur.J. Bioclieni. 228:323-331.
    • (1995) Eur.J. Bioclieni. , vol.228 , pp. 323-331
    • Maury, J.1    Nicoletti, C.2    Guzzo-Chambraud, I.3    Maroux, S.4
  • 19
    • 0029098227 scopus 로고
    • Expression and glycosylation of the filamentous brush border glycocalyx (FBDG) during rabbit enterocyte differentiation along the crypt-villus axis
    • Maury, J., A. lîernadac, A. Rigal, and S. Maroux. 1995. Expression and glycosylation of the filamentous brush border glycocalyx (FBDG) during rabbit enterocyte differentiation along the crypt-villus axis. J. Cell Sei. 108:2705-2713.
    • (1995) J. Cell Sei. , vol.108 , pp. 2705-2713
    • Maury, J.1    Lîernadac, A.2    Rigal, A.3    Maroux, S.4
  • 20
    • 0023092367 scopus 로고
    • Transport of membrane-bound macromolecules by M cells in follicle-associated epithelium of rabbit Peyer's patch
    • Neutra, M.R., T.L. Phillips, E.L. Mayer, and DJ. Fishkind. 1987. Transport of membrane-bound macromolecules by M cells in follicle-associated epithelium of rabbit Peyer's patch. Cell Tissue Res. 247:537-546.
    • (1987) Cell Tissue Res. , vol.247 , pp. 537-546
    • Neutra, M.R.1    Phillips, T.L.2    Mayer, E.L.3    Fishkind, D.J.4
  • 22
    • 0027994227 scopus 로고
    • Selective regulation of epithelial gene expression in rabbit Peyer's patch tissue. lyincgcrs Arch
    • Savidge, T.C., M.W. Smith, S. Mayel-Afshar, AJ. Collins, and T.C. Freeman. 1994. Selective regulation of epithelial gene expression in rabbit Peyer's patch tissue. lyincgcrs Arch. Eur.J. I'liysiol. 428:391-399;
    • (1994) Eur.J. I'liysiol. , vol.428 , pp. 391-399
    • Savidge, T.C.1    Smith, M.W.2    Mayel-Afshar, S.3    Collins, A.J.4    Freeman, T.C.5
  • 23
    • 0028564716 scopus 로고
    • Regional differences in glycoconjugates of intestinal M cells in mice: Potential targets for mucosal vaccines
    • Giannasca, PJ., K.T. Giannasca, P. Falk, J.I. Gordon, and M R. Neutra. 1994. Regional differences in glycoconjugates of intestinal M cells in mice: potential targets for mucosal vaccines. Am. J. Physiol. 267:G1108-G1121.
    • (1994) Am. J. Physiol. , vol.267
    • Giannasca, P.J.1    Giannasca, K.T.2    Falk, P.3    Gordon, J.I.4    Neutra, M.R.5
  • 24
    • 0021270537 scopus 로고
    • Structure, distribution and origin of M cells in Peyer's patches of mouse ileum
    • Bye, W.A., C.H. Allan, andJ.S. Trier. 1984. Structure, distribution and origin of M cells in Peyer's patches of mouse ileum. Gastrocnterobgy. 86:789-801.
    • (1984) Gastrocnterobgy. , vol.86 , pp. 789-801
    • Bye, W.A.1    Allan, C.H.2    Trier, J.S.3
  • 25
    • 0020482987 scopus 로고
    • Characterization of the cholera toxin receptor on Balb/c 3T3 cells as a ganglioside similar to, or identical with, ganglioside GM1
    • Critchley, D.R., C.H. Streuli, S. Kellie, S. Ansell, and B. Patel. 1982. Characterization of the cholera toxin receptor on Balb/c 3T3 cells as a ganglioside similar to, or identical with, ganglioside GM1. Bioclmn.J. 204:209-219.
    • (1982) Bioclmn.J. , vol.204 , pp. 209-219
    • Critchley, D.R.1    Streuli, C.H.2    Kellie, S.3    Ansell, S.4    Patel, B.5
  • 26
    • 0022493589 scopus 로고
    • Characterization of the receptor for cholera toxin and Eschcrichia cali heat-labile toxin in rabbit intestinal brush borders
    • Griffiths, S.L., R.A. Finkelstein, and D.R. Critchley. 1986. Characterization of the receptor for cholera toxin and Eschcrichia cali heat-labile toxin in rabbit intestinal brush borders. Biochcin.J. 238:313-322.
    • (1986) Biochcin.J. , vol.238 , pp. 313-322
    • Griffiths, S.L.1    Finkelstein, R.A.2    Critchley, D.R.3
  • 27
    • 0027959631 scopus 로고
    • The heat-labile enterotoxin of Escliericliia coli binds to polylactosaminoglycan-containing receptors in Caco-2 human intestinal epithelial cells
    • Orlandi, P.A., D.R. Critchley, and P.M. Fishman. 1994. The heat-labile enterotoxin of Escliericliia coli binds to polylactosaminoglycan-containing receptors in Caco-2 human intestinal epithelial cells. Biochemistry. 33:12886-12895.
    • (1994) Biochemistry. , vol.33 , pp. 12886-12895
    • Orlandi, P.A.1    Critchley, D.R.2    Fishman, P.M.3
  • 30
    • 0022406059 scopus 로고
    • Study of intestinal differentiation with monoclonal antibodies to intestinal cell surface components
    • Quaroni, A., and K.J. Isselbacher. 1985. Study of intestinal differentiation with monoclonal antibodies to intestinal cell surface components. Der. Biol. Ill :267-279.
    • (1985) Der. Biol. Ill , pp. 267-279
    • Quaroni, A.1    Isselbacher, K.J.2
  • 31
    • 0021806048 scopus 로고
    • A new method of preparing gold probes for multiple-labeling cytochemistry
    • Slot, J.W., and H.J. Geuze. 1984. A new method of preparing gold probes for multiple-labeling cytochemistry. Enr. J. Cell Biol. 38:87-93.
    • (1984) Enr. J. Cell Biol. , vol.38 , pp. 87-93
    • Slot, J.W.1    Geuze, H.J.2
  • 32
    • 0024203712 scopus 로고
    • Production and purification of cholera toxin
    • Mekalanos, JJ. 1988. Production and purification of cholera toxin. Methods Eiizymol. 165:169-175.
    • (1988) Methods Eiizymol. , vol.165 , pp. 169-175
    • Mekalanos, J.J.1
  • 33
    • 0027214259 scopus 로고
    • Three-dimensional structure of the tetragonal crystal form of egg-white avidin in its functional complex with biotin at 2.7 a resolution J
    • Pugliese, L., A. Coda, M. Malcovati, and M. Bolognesi. 1993. Three-dimensional structure of the tetragonal crystal form of egg-white avidin in its functional complex with biotin at 2.7 A resolution J. Mol. Biol. 231:698-710.
    • (1993) Mol. Biol. , vol.231 , pp. 698-710
    • Pugliese, L.1    Coda, A.2    Malcovati, M.3    Bolognesi, M.4
  • 34
    • 0026611627 scopus 로고
    • A 9 Atwodimensional projected structure of cholera toxin B-subunitGM1 complexes determined by electron crystallography
    • Mosser, G., V. Mallotih, and A. Brisson. 1992. A 9 Atwodimensional projected structure of cholera toxin B-subunitGM1 complexes determined by electron crystallography. J. Mol. Biol. 226:23-28.
    • (1992) J. Mol. Biol. , vol.226 , pp. 23-28
    • Mosser, G.1    Mallotih, V.2    Brisson, A.3
  • 35
    • 0019578657 scopus 로고
    • The purification of avidin and its derivatives on 2-iminobiotin-6-aminohexyl-sepharose 4B
    • Heney, G., and G.A. Orr. 1981. The purification of avidin and its derivatives on 2-iminobiotin-6-aminohexyl-sepharose 4B. Anal. Biocliein. 114:92-96.
    • (1981) Anal. Biocliein. , vol.114 , pp. 92-96
    • Heney, G.1    Orr, G.A.2
  • 36
    • 0024597894 scopus 로고
    • Binding and transepithelial transport of immunoglobulins by intestinal M cells: Demonstration using monoclonal IgA antibodies against enteric viral proteinsj
    • Weltzin, R.L., P. Lucia-Jandris, P. Michetti, D.N. Fields, J.P. Kraehenbuhl, and M.R. Neutra. 1989. Binding and transepithelial transport of immunoglobulins by intestinal M cells: demonstration using monoclonal IgA antibodies against enteric viral proteinsj. CellBhl. 108:1673-1685.
    • (1989) CellBhl. , vol.108 , pp. 1673-1685
    • Weltzin, R.L.1    Lucia-Jandris, P.2    Michetti, P.3    Fields, D.N.4    Kraehenbuhl, J.P.5    Neutra, M.R.6
  • 37
    • 0026755585 scopus 로고
    • Characterization of the enterocyte-like brush border cytoskeleton of the C2UB,. clones of the human intestinal cell line, Caco-2
    • Peterson, M.D., and M.S. Mooseker. 1992. Characterization of the enterocyte-like brush border cytoskeleton of the C2UB,. clones of the human intestinal cell line, Caco-2. J. Cell Sei. 102:581-600.
    • (1992) J. Cell Sei. , vol.102 , pp. 581-600
    • Peterson, M.D.1    Mooseker, M.S.2
  • 38
    • 0030053637 scopus 로고    scopus 로고
    • Adherence of Salmonella typliimtirmmuni to Caco-2 cells: Identification of a glycoconjugate receptor
    • Giannasca, K.T., PJ. Giannasca, and M.R. Neutra. 1996. Adherence of Salmonella typliimtirmmuni to Caco-2 cells: identification of a glycoconjugate receptor. Infect. Immun. 64:135-145.
    • (1996) Infect. Immun. , vol.64 , pp. 135-145
    • Giannasca, K.T.1    Giannasca, P.J.2    Neutra, M.R.3
  • 39
    • 0025744789 scopus 로고
    • Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human small intestine and colon
    • Gorvel, J.P., A. Ferrero, L. Chambraud, A. RigalJ. Bonicel, and S. Maroux. 1991. Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human small intestine and colon. Gastrocntcrology. 101:618-625.
    • (1991) Gastrocntcrology. , vol.101 , pp. 618-625
    • Gorvel, J.P.1    Ferrero, A.2    Chambraud, L.3    Rigalj Bonicel, A.4    Maroux, S.5
  • 40
    • 0026631750 scopus 로고
    • Transient mosaic patterns of morphological and functional differentiation in the Caco-2 cell line
    • Vachon, P.H., and J.-F. Beaulieu. 1992. Transient mosaic patterns of morphological and functional differentiation in the Caco-2 cell line. Gastrocntcrohgy. 103:414-423. .
    • (1992) Gastrocntcrohgy. , vol.103 , pp. 414-423
    • Vachon, P.H.1    Beaulieu, J.-F.2
  • 41
    • 0019572737 scopus 로고
    • Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins
    • Debray, H., D. Decout, G. Strecker, G. Spik, andj. Montreuil. 1981. Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins. Enr. J. Biochcm. 117:41-55.
    • (1981) Enr. J. Biochcm. , vol.117 , pp. 41-55
    • Debray, H.1    Decout, D.2    Strecker, G.3    Spik, G.4    Montreuil, A.5
  • 43
    • 0021111873 scopus 로고
    • The B4 lectin from Vicia villosa seeds interacts with N-acetylgalactosamine residues alpha-linked to serine or threonine residues in cell surface glycoproteins.J. biol
    • Tollefsen, S.E., and R. Kornfeld. 1983. The B4 lectin from Vicia villosa seeds interacts with N-acetylgalactosamine residues alpha-linked to serine or threonine residues in cell surface glycoproteins.J. biol. Cliein. 258:5172-5176.
    • (1983) Cliein. , vol.258 , pp. 5172-5176
    • Tollefsen, S.E.1    Kornfeld, R.2
  • 44
    • 0018412113 scopus 로고
    • The affinity of the fucosebinding lectin from Lotus tetragoiwlobns for glycopeptides and oligosaccharides accumulating in fucosidosis
    • Susz, J.P., and G. Dawson. 1979. The affinity of the fucosebinding lectin from Lotus tetragoiwlobns for glycopeptides and oligosaccharides accumulating in fucosidosis. J. Neiirocliein. 32:1009-1013.
    • (1979) J. Neiirocliein. , vol.32 , pp. 1009-1013
    • Susz, J.P.1    Dawson, G.2
  • 49
    • 0027411206 scopus 로고
    • Infection of colonie epithelial cell lines by type 1 human immunodeficiency virus (HIV-1) is associated with cell surface expression of galactosyl ceramide, a potential alternative gp!20 receptor
    • Fantini, J., D.G. Cook, N. Nathanson, S.L. Spitalnik, and F. Gonzalez-Scarano. 1993. Infection of colonie epithelial cell lines by type 1 human immunodeficiency virus (HIV-1) is associated with cell surface expression of galactosyl ceramide, a potential alternative gp!20 receptor. Proc. Natl. Acad. Sei. USA. 90:2700-2704.
    • (1993) Proc. Natl. Acad. Sei. USA. , vol.90 , pp. 2700-2704
    • Fantini, J.1    Cook, D.G.2    Nathanson, N.3    Spitalnik, S.L.4    Gonzalez-Scarano, F.5
  • 50
    • 0018754650 scopus 로고
    • Linear arrays of intramembrane particles in microvilli in primate large intestine
    • Neutra, M. 1979. Linear arrays of intramembrane particles in microvilli in primate large intestine. Anat. Rcc. 193:367-381.
    • (1979) Anat. Rcc. , vol.193 , pp. 367-381
    • Neutra, M.1
  • 51
    • 0015228513 scopus 로고
    • Isoelectric focussing behavior of bovine plasma albumin, mercaptalbumin, and -lactoglobulins a and B
    • Kaplan, L.J., andJ.F. Foster. 1971. Isoelectric focussing behavior of bovine plasma albumin, mercaptalbumin, and -lactoglobulins A and B. Biochemistry. 10:630-636.
    • (1971) Biochemistry. , vol.10 , pp. 630-636
    • Kaplan, L.J.1    Foster, A.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.