메뉴 건너뛰기




Volumn 3, Issue 12, 2002, Pages 944-955

Immunoglobulin transport across polarized epithelial cells

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN A; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M;

EID: 0036902323     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm972     Document Type: Review
Times cited : (259)

References (108)
  • 2
    • 0030861590 scopus 로고    scopus 로고
    • Interaction of antigens and antibodies at mucosal surfaces
    • Lamm, M. Interaction of antigens and antibodies at mucosal surfaces. Annu. Rev. Microbiol. 51, 311-340 (1997).
    • (1997) Annu. Rev. Microbiol. , vol.51 , pp. 311-340
    • Lamm, M.1
  • 4
    • 0035174046 scopus 로고    scopus 로고
    • Collaboration of epthelial cells with organized mucosal lymphoid tissues
    • Neutra, M. R., Mantis, N. J. & Kraehenbuhl, J.-P. Collaboration of epthelial cells with organized mucosal lymphoid tissues. Nature Immunol. 2, 1004-1009 (2001).
    • (2001) Nature Immunol. , vol.2 , pp. 1004-1009
    • Neutra, M.R.1    Mantis, N.J.2    Kraehenbuhl, J.-P.3
  • 7
    • 0023608934 scopus 로고
    • Biogenesis of the rat hepatocyte plasma membrane in vivo: Comparison of the pathways taken by apical and basolateral proteins using subcellular fractionation
    • Bartles, J. R., Ferraci, H. M., Stieger, B. & Hubbard, A. L. Biogenesis of the rat hepatocyte plasma membrane in vivo: Comparison of the pathways taken by apical and basolateral proteins using subcellular fractionation. J. Cell Biol. 105, 1241-1251 (1987).
    • (1987) J. Cell Biol. , vol.105 , pp. 1241-1251
    • Bartles, J.R.1    Ferraci, H.M.2    Stieger, B.3    Hubbard, A.L.4
  • 8
    • 0028202474 scopus 로고
    • Transepithelial transport of immunogbbulins
    • Mostov, K. E. Transepithelial transport of immunogbbulins. Annu Rev. Immunol. 12, 63-84 (1994).
    • (1994) Annu Rev. Immunol. , vol.12 , pp. 63-84
    • Mostov, K.E.1
  • 9
    • 0034705397 scopus 로고    scopus 로고
    • A primitive T cell-independent mechanism of intestinal mucosal IgA responses to commensal bacteria
    • Macpherson, A. J. et al. A primitive T cell-independent mechanism of intestinal mucosal IgA responses to commensal bacteria. Science 288, 2222-2226 (2000). Describes a T-cell-Independent mechanism for the production of IgA directed against commensal bacteria.
    • (2000) Science , vol.288 , pp. 2222-2226
    • Macpherson, A.J.1
  • 10
    • 0035846113 scopus 로고    scopus 로고
    • In situ class switching and differentiation of IgA-producing cells in the gut lamina propria
    • Fagarasan,S., Kinoshita, K., Muramatsu, M., Ikuta, K. & Honjo, T. In situ class switching and differentiation of IgA-producing cells in the gut lamina propria. Nature 413, 639-643 (2001).
    • (2001) Nature , vol.413 , pp. 639-643
    • Fagarasan, S.1    Kinoshita, K.2    Muramatsu, M.3    Ikuta, K.4    Honjo, T.5
  • 11
    • 0035321325 scopus 로고    scopus 로고
    • Dendritic cells express tight junction proteins and penetrate gut epithelial monclayers to sample bacteria
    • Rescigno, M et al. Dendritic cells express tight junction proteins and penetrate gut epithelial monclayers to sample bacteria, Nature Immunol. 2, 361-367 (2001). Shows that dendritic cells can directly sample the gut microflora.
    • (2001) Nature Immunol. , vol.2 , pp. 361-367
    • Rescigno, M.1
  • 12
    • 0021241263 scopus 로고
    • The receptor for transepithelial transport of IgA and IgM contains multiple immunoglobulin-like domains
    • Mostov, K. E., Friedlander, M. & Blobel, G. The receptor for transepithelial transport of IgA and IgM contains multiple immunoglobulin-like domains. Nature 308, 37-43 (1984).
    • (1984) Nature , vol.308 , pp. 37-43
    • Mostov, K.E.1    Friedlander, M.2    Blobel, G.3
  • 13
    • 0033571756 scopus 로고    scopus 로고
    • Generation of polymeric immunoglobulin receptor-deficient mouse with marked reduction of secretory IgA
    • Shimada, S.-I. et al. Generation of polymeric immunoglobulin receptor-deficient mouse with marked reduction of secretory IgA. J. Immunol. 163, 5367-5373 (1999).
    • (1999) J. Immunol. , vol.163 , pp. 5367-5373
    • Shimada, S.-I.1
  • 14
    • 0034664821 scopus 로고    scopus 로고
    • The polymeric immunoglobuin receptor translocates pneumococci across human nasopharyngeal epithelial cells
    • Zhang, J-R. et al. The polymeric immunoglobuin receptor translocates pneumococci across human nasopharyngeal epithelial cells. Cell 102, 827-837 (2000). This paper identifies the pIgR as a receptor for Pneumococci.
    • (2000) Cell , vol.102 , pp. 827-837
    • Zhang, J.-R.1
  • 15
    • 0015874382 scopus 로고
    • Protection against enteric bacterial infection by secretory IgA antibodies
    • Fubara, E. S. & Freter, R. Protection against enteric bacterial infection by secretory IgA antibodies. J. Immunol. 111, 395-403 (1973).
    • (1973) J. Immunol. , vol.111 , pp. 395-403
    • Fubara, E.S.1    Freter, R.2
  • 16
    • 0025008801 scopus 로고
    • Mechanism of neutralization of influenza virus on mouse tracheal epithelial cells by mouse monoclonal polymeric IgA and polyclonal IgM directed against the wral haemaglutinin
    • Outlaw, M. C. & Dimmock, N. J. Mechanism of neutralization of influenza virus on mouse tracheal epithelial cells by mouse monoclonal polymeric IgA and polyclonal IgM directed against the wral haemaglutinin. J. Gen. Virol. 71, 69-76 (1990).
    • (1990) J. Gen. Virol. , vol.71 , pp. 69-76
    • Outlaw, M.C.1    Dimmock, N.J.2
  • 17
    • 3543022665 scopus 로고    scopus 로고
    • Role of immunoglobulin A monoclonal antibodies against P 23 in controlling murine Cryptosporidium parvum infection
    • Ennquez, F. J. & Riggs, M. W. Role of immunoglobulin A monoclonal antibodies against P23 in controlling murine Cryptosporidium parvum infection. Infect. Immun. 66, 4469-4473 (1998).
    • (1998) Infect. Immun. , vol.66 , pp. 4469-4473
    • Ennquez, F.J.1    Riggs, M.W.2
  • 18
    • 0015523566 scopus 로고
    • Inhibition of bacterial adherence by secretory immunoglobulin A: A mechanism of antigen disposal
    • Williams, R. C. & Gibbons, R. J. Inhibition of bacterial adherence by secretory immunoglobulin A: A mechanism of antigen disposal. Science 177, 697-699 (1972).
    • (1972) Science , vol.177 , pp. 697-699
    • Williams, R.C.1    Gibbons, R.J.2
  • 19
    • 0035873475 scopus 로고    scopus 로고
    • Secretory IgA specific for a conserved epitope on gp41 envelope glycoprotein inhibits epithelial transcytosis of HIV-1
    • Alfsen, A., Iniguez, P., Bouguyon, E. & Bomsel, M. Secretory IgA specific for a conserved epitope on gp41 envelope glycoprotein inhibits epithelial transcytosis of HIV-1. J. Immunol. 166, 6257-6265 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 6257-6265
    • Alfsen, A.1    Iniguez, P.2    Bouguyon, E.3    Bomsel, M.4
  • 20
    • 0032920937 scopus 로고    scopus 로고
    • Infectious human immunodeficiency virus can rapidly penetrate a tight human epithelial barrier by transcytosis in a process impaired by mucosal immunoglobulins
    • Hocini, H. & Bomsel, M. Infectious human immunodeficiency virus can rapidly penetrate a tight human epithelial barrier by transcytosis in a process impaired by mucosal immunoglobulins. J. Infect. Dis. 179, S448-S453 (1999).
    • (1999) J. Infect. Dis. , vol.179
    • Hocini, H.1    Bomsel, M.2
  • 21
    • 0021923306 scopus 로고
    • Neutralization of cholera toxin by rat bile secretory IgA antibodies
    • Vaerman, J. P., Derick-Langendries, A., Rits, M. & Delacroix, D. Neutralization of cholera toxin by rat bile secretory IgA antibodies. Immunol. 54, 601-603 (1985).
    • (1985) Immunol. , vol.54 , pp. 601-603
    • Vaerman, J.P.1    Derick-Langendries, A.2    Rits, M.3    Delacroix, D.4
  • 22
    • 0032487496 scopus 로고    scopus 로고
    • Immunocytochemical colocalization of specific immunoglobulin A with sendal virus protein in infected polarized epithelium
    • Fujicka, H. et al. Immunocytochemical colocalization of specific immunoglobulin A with sendal virus protein in infected polarized epithelium. J. Exp. Med. 188, 1223-1229 (1998)
    • (1998) J. Exp. Med. , vol.188 , pp. 1223-1229
    • Fujicka, H.1
  • 23
    • 0026684832 scopus 로고
    • Intracellular neutralization of virus by immunoglobulin A antibodies
    • Mazanec, M. B., Kaetzel, C. S., Lamm, M., Fletcher, D. & Nedrud, J. G. Intracellular neutralization of virus by immunoglobulin A antibodies. Proc. Natl. Acad. Sci. USA 89, 6901-6905 (1992). The first demonstration of the intracellular virus neutralization by pIgR-dIgA.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6901-6905
    • Mazanec, M.B.1    Kaetzel, C.S.2    Lamm, M.3    Fletcher, D.4    Nedrud, J.G.5
  • 24
    • 0025944505 scopus 로고
    • The polymeric immunoglobulin receptor (secretory component) mediates transport of immune complexes across epithelial cells: A local defense function of IgA
    • Kaetzel, C. S., Robinson, J. K., Chintalachavuru, K. R., Vaerman, J.-P. & Lamm, M. The polymeric immunoglobulin receptor (secretory component) mediates transport of immune complexes across epithelial cells: A local defense function of IgA Proc. Natl. Acad. Sci. USA 88, 8796-8780 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8796-8780
    • Kaetzel, C.S.1    Robinson, J.K.2    Chintalachavuru, K.R.3    Vaerman, J.-P.4    Lamm, M.5
  • 25
    • 0030929805 scopus 로고    scopus 로고
    • Fo receptor biology
    • Daeron, M. Fo receptor biology. Annu. Rev. Immunol. 15, 203-234 (1997).
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 203-234
    • Daeron, M.1
  • 26
    • 0024529856 scopus 로고
    • An Fc receptor structurally related to MHC class I antigens
    • Simister, N. E. & Mostov, K. E. An Fc receptor structurally related to MHC class I antigens. Nature 337, 184-187 (1989).
    • (1989) Nature , vol.337 , pp. 184-187
    • Simister, N.E.1    Mostov, K.E.2
  • 27
    • 0028051652 scopus 로고
    • Crystal structure at 2.2 A resolution of the MHC-related neonatal Fc receptor
    • Burmeister, W. P., Gastinel, L. N., Simister, N. E., Blum, M. L. & Bjorkman, P. J. Crystal structure at 2.2 A resolution of the MHC-related neonatal Fc receptor. Nature 372, 336-343 (1994). Determination of the crystal structure of FcRn.
    • (1994) Nature , vol.372 , pp. 336-343
    • Burmeister, W.P.1    Gastinel, L.N.2    Simister, N.E.3    Blum, M.L.4    Bjorkman, P.J.5
  • 28
    • 0036591969 scopus 로고    scopus 로고
    • β2-microglobulin is important for cell surface expression and pH-dependent IgG binding of human FcRn
    • Praetor, A. & Hunziker, W. β2-microglobulin is important for cell surface expression and pH-dependent IgG binding of human FcRn J. Cell Sci. 115, 2389-2397 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 2389-2397
    • Praetor, A.1    Hunziker, W.2
  • 29
    • 0017166982 scopus 로고
    • pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat
    • Rodewald, R. pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat. J. Cell Biol. 71, 666-670 (1976).
    • (1976) J. Cell Biol. , vol.71 , pp. 666-670
    • Rodewald, R.1
  • 30
    • 0015877138 scopus 로고
    • Intestinal transport of antibodies in the newborn rat
    • Rodewald, R. Intestinal transport of antibodies in the newborn rat. J. Cell Biol. 58, 189-211 (1973).
    • (1973) J. Cell Biol. , vol.58 , pp. 189-211
    • Rodewald, R.1
  • 32
    • 0025134727 scopus 로고
    • Isolation and characterization of the Fc receptor from fetal yolk sac of the rat
    • Roberts, D. M., Guenthert, M, & Rodewald, R. Isolation and characterization of the Fc receptor from fetal yolk sac of the rat. J. Cell Biol. 111, 1867-1876 (1990). Shows that IgG binding to FcRn could occur in endosomes and not only at the plasma membrane.
    • (1990) J. Cell Biol. , vol.111 , pp. 1867-1876
    • Roberts, D.M.1    Guenthert, M.2    Rodewald, R.3
  • 33
    • 0030587958 scopus 로고    scopus 로고
    • Isolation from human placenta of the IgG transporter, FcRn, and localization to the syncytiotrophoblast
    • Leach, J. L. et al. Isolation from human placenta of the IgG transporter, FcRn, and localization to the syncytiotrophoblast. J. Immunol. 157, 3317-3322 (1996).
    • (1996) J. Immunol. , vol.157 , pp. 3317-3322
    • Leach, J.L.1
  • 34
    • 0000146003 scopus 로고
    • A theoretical model of gammaglobulin catabolism
    • Brambell, F. W. R., Hemmings, W. A. & Moms, I. G. A theoretical model of gammaglobulin catabolism. Nature 203, 1352-1355 (1964).
    • (1964) Nature , vol.203 , pp. 1352-1355
    • Brambell, F.W.R.1    Hemmings, W.A.2    Moms, I.G.3
  • 35
    • 0031685365 scopus 로고    scopus 로고
    • Functional expression of the MHC class I-related receptor, FcRn, in endothelial cells of mice
    • Borvak, J. et al. Functional expression of the MHC class I-related receptor, FcRn, in endothelial cells of mice. Int. Immunol. 10, 1289-1298 (1998).
    • (1998) Int. Immunol. , vol.10 , pp. 1289-1298
    • Borvak, J.1
  • 36
    • 0029927482 scopus 로고    scopus 로고
    • Abnormally short serum half-lives of IgG in β2-microglobulin-deficient mice
    • Ghetie, V. et al. Abnormally short serum half-lives of IgG in β2-microglobulin-deficient mice. Eur. J. Immunol. 26, 690-696 (1996). Confirms that FcRn is important in IgG catabolism.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 690-696
    • Ghetie, V.1
  • 37
    • 0034042660 scopus 로고    scopus 로고
    • Multiple roles for the major histocompatibility complex class I-related receptor FcRn
    • Ghetie, V. & Ward, E. S. Multiple roles for the major histocompatibility complex class I-related receptor FcRn. Annu. Rev. Immunol. 18, 739-766 (2000).
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 739-766
    • Ghetie, V.1    Ward, E.S.2
  • 38
    • 0030880901 scopus 로고    scopus 로고
    • Expression of the neonatal Fc receptor, FcRn on human intestinal epithelial cells
    • Israel, E. J. et al. Expression of the neonatal Fc receptor, FcRn on human intestinal epithelial cells. Immunol. 92, 69-74 (1997).
    • (1997) Immunol. , vol.92 , pp. 69-74
    • Israel, E.J.1
  • 39
    • 0032741975 scopus 로고    scopus 로고
    • Bidirectional FcRn-dependent IgG transport in a polarized human intestinal epithelial cell line
    • Dickinson, B. L. et al. Bidirectional FcRn-dependent IgG transport in a polarized human intestinal epithelial cell line. J. Clin. Invest. 104, 903-911 (1999).
    • (1999) J. Clin. Invest. , vol.104 , pp. 903-911
    • Dickinson, B.L.1
  • 40
    • 0037025895 scopus 로고    scopus 로고
    • Receptor-mediated immunoglobulin G transport across mucosal barriers in adult life: Functional expression of FcRn in the mammalian lung
    • Spiekermann, G. M. et al. Receptor-mediated immunoglobulin G transport across mucosal barriers in adult life: Functional expression of FcRn in the mammalian lung. J. Exp. Med. 196, 303-310 (2002). Demonstrates that FcRn can transport antigens from the luminal to serosal surface of the epithelium.
    • (2002) J. Exp. Med. , vol.196 , pp. 303-310
    • Spiekermann, G.M.1
  • 41
    • 0021848960 scopus 로고
    • Immunoglobulin Immunoglobulln G subclass proteins in serum and lavage fluid of normal subjects. Quantitation and comparison with immunoglobulins A and E
    • Merill, W. W., Naegel, G. P., Olchowski, J. J. & Reynolds, H. Y. Immunoglobulin Immunoglobulln G subclass proteins in serum and lavage fluid of normal subjects. Quantitation and comparison with immunoglobulins A and E. Am. Rev. Respir. Dis. 131, 584-587 (1985).
    • (1985) Am. Rev. Respir. Dis. , vol.131 , pp. 584-587
    • Merill, W.W.1    Naegel, G.P.2    Olchowski, J.J.3    Reynolds, H.Y.4
  • 42
    • 0034089437 scopus 로고    scopus 로고
    • Immunoglobulin levels in bronchoalveolar lavage fluid of children with chronic chest disease
    • Kitz, R., Ahrens, P. & Zielen, S. Immunoglobulin levels in bronchoalveolar lavage fluid of children with chronic chest disease. Pediatr. Pulmonol. 29, 443-451 (2000).
    • (2000) Pediatr. Pulmonol. , vol.29 , pp. 443-451
    • Kitz, R.1    Ahrens, P.2    Zielen, S.3
  • 43
    • 0026667712 scopus 로고
    • The cytoplasmic domain of the polymeric immunoglobulin receptor contains two internalization signals that are distinct from its basolateral sorting signal
    • Okamoto, C. T., Shia, S.-P., Bird, C., Mostov, K. E. & Roth, M. G. The cytoplasmic domain of the polymeric immunoglobulin receptor contains two internalization signals that are distinct from its basolateral sorting signal. J. Biol. Chem. 267, 9925-9932 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 9925-9932
    • Okamoto, C.T.1    Shia, S.-P.2    Bird, C.3    Mostov, K.E.4    Roth, M.G.5
  • 44
    • 0028358382 scopus 로고
    • Rapid internalization of the polymeric immunoglobulin receptor requires phosphorylated serine 726
    • Okamoto, C. T., Song, W., Bomsel, M. & Mostov, K. E. Rapid internalization of the polymeric immunoglobulin receptor requires phosphorylated serine 726. J. Biol. Chem. 269, 15676-15682 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 15676-15682
    • Okamoto, C.T.1    Song, W.2    Bomsel, M.3    Mostov, K.E.4
  • 45
    • 0028290669 scopus 로고
    • Rab 5a is a common component of the apical and basolateral endocytic machinery in polarized epithelial cells
    • Bucci, C. et al. Rab5a is a common component of the apical and basolateral endocytic machinery in polarized epithelial cells. Proc. Natl. Acad. Sci. USA 91, 5061-5065 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5061-5065
    • Bucci, C.1
  • 46
    • 0034084289 scopus 로고    scopus 로고
    • Sorting of membrane and fluid at the apical pole of polarized MDCK cell
    • Leung, S.-M., Ruiz, W. G. & Apodaca, G. Sorting of membrane and fluid at the apical pole of polarized MDCK cell. Mol. Biol. Cell 11 (2000).
    • (2000) Mol. Biol. Cell , pp. 11
    • Leung, S.-M.1    Ruiz, W.G.2    Apodaca, G.3
  • 47
    • 0028346520 scopus 로고
    • Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes
    • Apodaca, G., Katz, L. A. & Mostov, K. E. Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes. J. Cell Biol. 125, 67-86 (1994).
    • (1994) J. Cell Biol. , vol.125 , pp. 67-86
    • Apodaca, G.1    Katz, L.A.2    Mostov, K.E.3
  • 48
    • 0034208649 scopus 로고    scopus 로고
    • Apical and basolateral pathways of MDCK cells meet in acidic common endosomes distinct from a nearly-neutral apical recycling endosome
    • Wang, E. et al. Apical and basolateral pathways of MDCK cells meet in acidic common endosomes distinct from a nearly-neutral apical recycling endosome. Traffic 1 480-493 (2000).
    • (2000) Traffic , vol.1 , pp. 480-493
    • Wang, E.1
  • 49
    • 0033525930 scopus 로고    scopus 로고
    • The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions
    • Sheff, D. R., Daro, E. A., Hull, M. & Mellman, I. The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions, J. Cell Biol. 145, 123-139 (1999).
    • (1999) J. Cell Biol. , vol.145 , pp. 123-139
    • Sheff, D.R.1    Daro, E.A.2    Hull, M.3    Mellman, I.4
  • 50
    • 0029820888 scopus 로고    scopus 로고
    • Apical and basolateral endosomes of MDCK cells are interconnected and contain a polarized sorting mechanism
    • Odorizzi, G., Pearse, A., Domingo, D., Trowbridge, I. S. & Hopkins, C. R. Apical and basolateral endosomes of MDCK cells are interconnected and contain a polarized sorting mechanism, J. Cell Biol. 135, 139-152 (1996).
    • (1996) J. Cell Biol. , vol.135 , pp. 139-152
    • Odorizzi, G.1    Pearse, A.2    Domingo, D.3    Trowbridge, I.S.4    Hopkins, C.R.5
  • 51
    • 0034139848 scopus 로고    scopus 로고
    • Definition of distinct compartments in polarized Madin-Darby Canine Kidney (MDCK) cells for membrane-volume sorting, polarized sorting and apical recycling
    • Brown, P. S. et al. Definition of distinct compartments in polarized Madin-Darby Canine Kidney (MDCK) cells for membrane-volume sorting, polarized sorting and apical recycling. Traffic 1, 124-140 (2000).
    • (2000) Traffic , vol.1 , pp. 124-140
    • Brown, P.S.1
  • 52
    • 0029893859 scopus 로고    scopus 로고
    • The transcytotic pathway of an apical plasma membrane protein (B10) in hepatocytes is similar to that of IgA and occurs via a tubular pericentriolar compartment
    • Hemery, L., Durand-Schneider, A.-M., Feldmann, G., Vaerman, J.-P. & Maurice, M. The transcytotic pathway of an apical plasma membrane protein (B10) in hepatocytes is similar to that of IgA and occurs via a tubular pericentriolar compartment. J. Cell Sci. 109, 1215-1227 (1996).
    • (1996) J. Cell Sci. , vol.109 , pp. 1215-1227
    • Hemery, L.1    Durand-Schneider, A.-M.2    Feldmann, G.3    Vaerman, J.-P.4    Maurice, M.5
  • 53
    • 0027761004 scopus 로고
    • WIF-B cells: An in vitro model for studies of hepatocyte polarity
    • Ihrke, G. et al. WIF-B cells: An in vitro model for studies of hepatocyte polarity. J. Cell Biol. 123, 1761-75 (1993).
    • (1993) J. Cell Biol. , vol.123 , pp. 1761-1775
    • Ihrke, G.1
  • 54
    • 0032498797 scopus 로고    scopus 로고
    • Rab 17 regulates membrane trafficking through apical recycling endosomes in polarized epithelial cells
    • Zacchi, P. et al. Rab17 regulates membrane trafficking through apical recycling endosomes in polarized epithelial cells. J. Cell Biol. 140, 1039-1053 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 1039-1053
    • Zacchi, P.1
  • 55
    • 0032547083 scopus 로고    scopus 로고
    • Rab17 localizes to recycling endosomes and regulates receptor-mediated transcytosis in epithelial cells
    • Hunziker, W. & Peters, P. J. Rab17 localizes to recycling endosomes and regulates receptor-mediated transcytosis in epithelial cells. J. Biol. Chem. 273, 15734-15741 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 15734-15741
    • Hunziker, W.1    Peters, P.J.2
  • 56
    • 0028009419 scopus 로고
    • Basolateral to apical transcytosis in polarized cells is indirect and involves BFA and trimeric G protein sensitive passage through the apical endosome
    • Barroso, M. & Sztul, E. Basolateral to apical transcytosis in polarized cells is indirect and involves BFA and trimeric G protein sensitive passage through the apical endosome. J. Cell Biol. 124, 83-100 (1994).
    • (1994) J. Cell Biol. , vol.124 , pp. 83-100
    • Barroso, M.1    Sztul, E.2
  • 57
    • 0032951298 scopus 로고    scopus 로고
    • Association of Rab25 and Rab11a with the apical recycling system of polarized Madin-Daroy canine kidney cells
    • Casanova, J. E. et al. Association of Rab25 and Rab11a with the apical recycling system of polarized Madin-Daroy canine kidney cells. Mol. Biol. Cell 10, 47-61 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 47-61
    • Casanova, J.E.1
  • 58
    • 0034666356 scopus 로고    scopus 로고
    • Regulation of vesicle trafficking in Madin-Darby canine kidney cells by Rah 11a and Rab25
    • Wang, X., Kumar, R., Navarre, J., Casanova, J. E. & Goldending, J. R. Regulation of vesicle trafficking in Madin-Darby canine kidney cells by Rah11a and Rab25. J. Biol. Chem 275, 29138-29146 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 29138-29146
    • Wang, X.1    Kumar, R.2    Navarre, J.3    Casanova, J.E.4    Goldending, J.R.5
  • 59
    • 0024374567 scopus 로고
    • Postendocytotic sorting of the ligand for the polymeric immunoglobulin receptor in Madin-Daroy canine kidney cells
    • Breitfeld, P. P., Harris, J. M. & Mostov, K. M. Postendocytotic sorting of the ligand for the polymeric immunoglobulin receptor in Madin-Daroy canine kidney cells. J. Cell Biol. 109, 475-486 (1989).
    • (1989) J. Cell Biol. , vol.109 , pp. 475-486
    • Breitfeld, P.P.1    Harris, J.M.2    Mostov, K.M.3
  • 60
    • 0033034401 scopus 로고    scopus 로고
    • IgG transport across trophoblast-derived BeWo cells: A model system to study IgG transport in the placenta
    • Ellinger, I., Schwab, M., Stefanescu, A., Hunziker, W. & Fuchs, R. IgG transport across trophoblast-derived BeWo cells: A model system to study IgG transport in the placenta. Eur. J. Immunol. 29, 733-744 (1999).
    • (1999) Eur. J. Immunol. , vol.29 , pp. 733-744
    • Ellinger, I.1    Schwab, M.2    Stefanescu, A.3    Hunziker, W.4    Fuchs, R.5
  • 61
    • 0032794645 scopus 로고    scopus 로고
    • Intracellular traffic of the MHC class I-like IgG Fc receptor, FcRn, expressed in epithelial MDCK cells
    • Praetor, A., Ellinger, I. & Hunziker, W. Intracellular traffic of the MHC class I-like IgG Fc receptor, FcRn, expressed in epithelial MDCK cells. J. Cell Sci. 112, 2291-2299 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 2291-2299
    • Praetor, A.1    Ellinger, I.2    Hunziker, W.3
  • 62
    • 0034058526 scopus 로고    scopus 로고
    • Bidirectional transcytosis of IgG by the rat neonatal Fo receptor expressed in a rat kidney cell line: A system to study protein transport across epithelia
    • McCarthy, K. M., Yoong, Y. & Simister, N. E. Bidirectional transcytosis of IgG by the rat neonatal Fo receptor expressed in a rat kidney cell line: A system to study protein transport across epithelia. J. Cell Sci. 113, 1277-1285 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 1277-1285
    • McCarthy, K.M.1    Yoong, Y.2    Simister, N.E.3
  • 63
    • 0035113258 scopus 로고    scopus 로고
    • Expression of functionally active FcRn and the differentiated bidirectional transport of IgG in human placental endothelial cells
    • Antohe, F., Raculescu, L., Gafencu, A., Ghetie, V. Simionescu, M. Expression of functionally active FcRn and the differentiated bidirectional transport of IgG in human placental endothelial cells. Human Immunol. 62, 93-105 (2001).
    • (2001) Human Immunol. , vol.62 , pp. 93-105
    • Antohe, F.1    Raculescu, L.2    Gafencu, A.3    Ghetie, V.4    Simionescu, M.5
  • 64
    • 0019837455 scopus 로고
    • Evidence for the sorting of endocytic vesicle contents during the receptor-mediated transport of IgG across the newborn rat intestine
    • Abrahamson, D. R. & Rodewald, R. Evidence for the sorting of endocytic vesicle contents during the receptor-mediated transport of IgG across the newborn rat intestine. J. Cell Biol. 91, 270-280 (1981).
    • (1981) J. Cell Biol. , vol.91 , pp. 270-280
    • Abrahamson, D.R.1    Rodewald, R.2
  • 66
    • 0025299751 scopus 로고
    • Uptake and intracellular routing of peroxidase-conjugated immunoglobulin-G by the perfused human placenta
    • Leach, L., Eaton, B. M., Firth, J. A. & Contractor, S. F. Uptake and intracellular routing of peroxidase-conjugated immunoglobulin-G by the perfused human placenta. Cell Tissue Res. 261, 383-388 (1990).
    • (1990) Cell Tissue Res. , vol.261 , pp. 383-388
    • Leach, L.1    Eaton, B.M.2    Firth, J.A.3    Contractor, S.F.4
  • 67
    • 0035895939 scopus 로고    scopus 로고
    • Tryptophan- and dileucine-based endocytosis signals in the neonatal Fc receptor
    • Wu, Z. & Simister, N. E. Tryptophan- and dileucine-based endocytosis signals in the neonatal Fc receptor. J. Biol Chem. 276, 5240-5247 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 5240-5247
    • Wu, Z.1    Simister, N.E.2
  • 68
    • 0032482226 scopus 로고    scopus 로고
    • In polarized MDCK cells basolateral vesicles arise from clathrin-gamma-adaptin-coated domains on endosomal tubules
    • Futter, C. E. et al. In polarized MDCK cells basolateral vesicles arise from clathrin-gamma-adaptin-coated domains on endosomal tubules. J. Cell Biol. 141, 611-623 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 611-623
    • Futter, C.E.1
  • 69
    • 0025168710 scopus 로고
    • Differential microtubule requirements for transcytosis in MDCK cells
    • Hunziker, W., Mâe, P. & Mailman, I. Differential microtubule requirements for transcytosis in MDCK cells. EMBO J. 9, 3515-3525 (1990).
    • (1990) EMBO J. , vol.9 , pp. 3515-3525
    • Hunziker, W.1    Mâe, P.2    Mailman, I.3
  • 70
    • 0030889917 scopus 로고    scopus 로고
    • Both microtubules and actin filaments are required for efficient postendocytic traffic of the polymeric immunoglobulin receptor in polarized Madin-Darby canine kidney cells
    • Maples, C. J., Ruiz, W. G. & Apodaca, G. Both microtubules and actin filaments are required for efficient postendocytic traffic of the polymeric immunoglobulin receptor in polarized Madin-Darby canine kidney cells. J. Biol. Chem. 272, 6741-6751 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 6741-6751
    • Maples, C.J.1    Ruiz, W.G.2    Apodaca, G.3
  • 71
    • 0032736748 scopus 로고    scopus 로고
    • Modulation of endocytic traffic in polarized MDCK cells by the small GTPase RhoA
    • Leung, S.-M. et al. Modulation of endocytic traffic in polarized MDCK cells by the small GTPase RhoA. Mol. Biol. Cell 10, 4369-4384 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4369-4384
    • Leung, S.-M.1
  • 72
    • 0033973134 scopus 로고    scopus 로고
    • Selective alterations in biosynthetic and endocytic protein traffic in Madin-Darby canine kidney epithelial cells expressing mutants of the small GTPase Rac 1
    • Jou, T.-S. et al. Selective alterations in biosynthetic and endocytic protein traffic in Madin-Darby canine kidney epithelial cells expressing mutants of the small GTPase Rac1. Mol. Biol. Cell 11, 287-304 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 287-304
    • Jou, T.-S.1
  • 73
    • 0035159369 scopus 로고    scopus 로고
    • Cdc42-dependent modulation of tight junctions and membrane protein traffic in polarized MDCK cells
    • Rojas, R., Ruiz, W. G., Leung, S. M., Jou, T. S. & Apodaca, G. Cdc42-dependent modulation of tight junctions and membrane protein traffic in polarized MDCK cells. Mol. Biol. Cell 12, 2257-2274 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2257-2274
    • Rojas, R.1    Ruiz, W.G.2    Leung, S.M.3    Jou, T.S.4    Apodaca, G.5
  • 74
    • 0036480017 scopus 로고    scopus 로고
    • Direct interactions between Rab3b and the polymeric immunoglobulin receptor controls ligand-stimulated transcytosis in epithelial cells
    • van Ijzandeom, S. C. D., Tuvim, M. J., Weimbs, T., Dickey, B. F. & Mostov, K. E. Direct interactions between Rab3b and the polymeric immunoglobulin receptor controls ligand-stimulated transcytosis in epithelial cells. Dev. Cell 2, 219-228 (2002). Demonstrates that dIgA binding stimulates pIgR transcytosis through the action of the Rab3b GTIPase.
    • (2002) Dev. Cell , vol.2 , pp. 219-228
    • Van Ijzandeom, S.C.D.1    Tuvim, M.J.2    Weimbs, T.3    Dickey, B.F.4    Mostov, K.E.5
  • 75
    • 0027379648 scopus 로고
    • s, in transcytosis of the polymeric immunoglobulin receptor
    • s, in transcytosis of the polymeric immunoglobulin receptor. J. Biol. Chem. 268, 25824-25835 (1993)
    • (1993) J. Biol. Chem. , vol.268 , pp. 25824-25835
    • Bomsel, M.1    Mostov, K.E.2
  • 76
    • 0028167863 scopus 로고
    • α stimulates transcytosis and apical secretion in MDCK cells through cAMP and protein kinase A
    • α stimulates transcytosis and apical secretion in MDCK cells through cAMP and protein kinase A. J. Cell Biol. 126, 677-688 (1994).
    • (1994) J. Cell Biol. , vol.126 , pp. 677-688
    • Hansen, S.H.1    Casanova, J.E.2
  • 77
    • 0028796834 scopus 로고
    • TAP/p 115, a general fusion factor is homologous to yeast US01 and is required for stable binding of vesicles to target membrane
    • Barroso, M. R., Nelson, D. S. & Sztul, E. S. TAP/p115, a general fusion factor is homologous to yeast US01 and is required for stable binding of vesicles to target membrane. Proc. Natl. Acad. Sci. USA 92, 527-531 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 527-531
    • Barroso, M.R.1    Nelson, D.S.2    Sztul, E.S.3
  • 78
    • 0028304457 scopus 로고
    • The calmodulin antagonist, W-13, alters transcytosis, recycling, and the morphology of the endocytic pathway in MDCK cells
    • Apodaca, G., Enrich, C. & Mostov, K. E. The calmodulin antagonist, W-13, alters transcytosis, recycling, and the morphology of the endocytic pathway in MDCK cells. J. Biol. Chem. 269, 19005-19013 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 19005-19013
    • Apodaca, G.1    Enrich, C.2    Mostov, K.E.3
  • 79
    • 0030048098 scopus 로고    scopus 로고
    • Calmodulin binds to the basolateral targeting signal of the polymeric immunoglobulin receptor
    • Chapin, S., Enrich, C., Aroeti, B., Havel, R. & Mostov, K. Calmodulin binds to the basolateral targeting signal of the polymeric immunoglobulin receptor. J. Biol. Chem. 271, 1336-1342 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 1336-1342
    • Chapin, S.1    Enrich, C.2    Aroeti, B.3    Havel, R.4    Mostov, K.5
  • 80
    • 0028862325 scopus 로고
    • Wortmannin, an inhibitor of phosphoinositide 3-kinase, inhibits transcytosis in polarized epithelial cells
    • Hansen, S. H., Olsson, A. & Casanova, J. E. Wortmannin, an inhibitor of phosphoinositide 3-kinase, inhibits transcytosis in polarized epithelial cells. J. Biol. Chem. 270, 28425-28432 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 28425-28432
    • Hansen, S.H.1    Olsson, A.2    Casanova, J.E.3
  • 81
    • 0035904227 scopus 로고    scopus 로고
    • Vps 34p differentially regulates endocytosis from the apical and basolateral domains in polarized hepatic cells
    • Tuma, P. L., Nyasae, L. K., Backer, J. M. & Hubbard, A. L. Vps34p differentially regulates endocytosis from the apical and basolateral domains in polarized hepatic cells. J. Cell Biol. 154, 1197-1208 (2001).
    • (2001) J. Cell Biol. , vol.154 , pp. 1197-1208
    • Tuma, P.L.1    Nyasae, L.K.2    Backer, J.M.3    Hubbard, A.L.4
  • 82
    • 0000777226 scopus 로고    scopus 로고
    • The SNARE machinery is involved in apical plasma membrane trafficking in MDCK cells
    • Low, S. H. et al. The SNARE machinery is involved in apical plasma membrane trafficking in MDCK cells. J. Cell Biol. 141, 1503-1513 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 1503-1513
    • Low, S.H.1
  • 83
    • 0034677896 scopus 로고    scopus 로고
    • Cellubrevin is present in the basolateral endocytic compartment of hepatocytes and follows the transcytotic pathway after IgA internalization
    • Calvo, M. et al. Cellubrevin is present in the basolateral endocytic compartment of hepatocytes and follows the transcytotic pathway after IgA internalization. J. Biol. Chem. 215, 7910-7917 (2000).
    • (2000) J. Biol. Chem. , vol.215 , pp. 7910-7917
    • Calvo, M.1
  • 84
    • 0029990362 scopus 로고    scopus 로고
    • Reconstitution of transcytosis in SLO-permeabilized MDCK cells: Existence of an NSF dependent fusion mechanism with the apical surface of MDCK cells
    • Apodaca, G., Carbone, M. H., Whiteheart, S. W., DasGupta, B. R. & Mostov, K. E. Reconstitution of transcytosis in SLO-permeabilized MDCK cells: Existence of an NSF dependent fusion mechanism with the apical surface of MDCK cells. EMBO J. 15, 1471-1481 (1996).
    • (1996) EMBO J. , vol.15 , pp. 1471-1481
    • Apodaca, G.1    Carbone, M.H.2    Whiteheart, S.W.3    DasGupta, B.R.4    Mostov, K.E.5
  • 85
    • 0029954454 scopus 로고    scopus 로고
    • Signal transduction by the polymeric immunoglobulin receptor suggests a role in regulation of receptor transcytosis
    • Cardone, M. H. et al. Signal transduction by the polymeric immunoglobulin receptor suggests a role in regulation of receptor transcytosis. J. Cell Biol. 133, 1-9 (1996).
    • (1996) J. Cell Biol. , vol.133 , pp. 1-9
    • Cardone, M.H.1
  • 86
    • 0028267096 scopus 로고
    • Phorool myristate acetate-mediated stimulation of transcytosis and apical recycling in MDCK cells
    • Cardone, M. H., Smith, B. L., Song, W., Mochley-Rosen, D. & Mostov, K. E. Phorool myristate acetate-mediated stimulation of transcytosis and apical recycling in MDCK cells. J. Cell Biol. 124, 717-727 (1994).
    • (1994) J. Cell Biol. , vol.124 , pp. 717-727
    • Cardone, M.H.1    Smith, B.L.2    Song, W.3    Mochley-Rosen, D.4    Mostov, K.E.5
  • 88
    • 0031817316 scopus 로고    scopus 로고
    • Role of tyrosine phosphorylation in ligand-induced regulation of transcytosis of the polymeric Ig receptor
    • Luton, F., Carbone, M. H., Zhang, M. & Mostov, K. E. Role of tyrosine phosphorylation in ligand-induced regulation of transcytosis of the polymeric Ig receptor. Mol. Biol. Cell 9, 1787-1802 (1998).
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1787-1802
    • Luton, F.1    Carbone, M.H.2    Zhang, M.3    Mostov, K.E.4
  • 89
    • 0031671085 scopus 로고    scopus 로고
    • Selective perfurbation of apical membrane traffic by expression of influenza M2, an acid-activated channel, in polarized Madin-Darby canine kidney cells
    • Henkel, J. R., Apodaca, G., Atschuler Y., Hardy, S. & Weisz, O. A. Selective perfurbation of apical membrane traffic by expression of influenza M2, an acid-activated channel, in polarized Madin-Darby canine kidney cells. Mol. Biol. Cell 9, 2477-2490 (1998).
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2477-2490
    • Henkel, J.R.1    Apodaca, G.2    Atschuler, Y.3    Hardy, S.4    Weisz, O.A.5
  • 90
    • 0033044626 scopus 로고    scopus 로고
    • Transcytosis of immunoglobulin A in the mouse enterocyte occurs through glycoplipid raft- and Rab17-containing compartments
    • Hansen, G. H., et al. Transcytosis of immunoglobulin A in the mouse enterocyte occurs through glycoplipid raft- and Rab17-containing compartments. Gastroenterol. 116, 610-622 (1999).
    • (1999) Gastroenterol. , vol.116 , pp. 610-622
    • Hansen, G.H.1
  • 91
    • 0000234827 scopus 로고
    • Selective inhibition of transcytosis by Brefeldin A in MDCK cells
    • Hunziker, W., Whitney, J. A. & Mellman, I. Selective inhibition of transcytosis by Brefeldin A in MDCK cells. Cell 57, 1-20 (1991).
    • (1991) Cell , vol.57 , pp. 1-20
    • Hunziker, W.1    Whitney, J.A.2    Mellman, I.3
  • 92
    • 0025358292 scopus 로고
    • Phosphorylation of the polymeric immunoglobulin receptor required for its efficient transcytosis
    • Casanova, J. E., Breitfeld, P. P., Ross, S. A. & Mostov, K. E. Phosphorylation of the polymeric immunoglobulin receptor required for its efficient transcytosis. Science 248, 742-745 (1990).
    • (1990) Science , vol.248 , pp. 742-745
    • Casanova, J.E.1    Breitfeld, P.P.2    Ross, S.A.3    Mostov, K.E.4
  • 93
    • 0031898776 scopus 로고    scopus 로고
    • Dimerization of the polymeric immunoglobulin receptor controls its transcytotic trafficking
    • Singer, K. L. & Mostov, K. E. Dimerization of the polymeric immunoglobulin receptor controls its transcytotic trafficking. Mol. Biol. Cell 9, 901-915 (1998).
    • (1998) Mol. Biol. Cell , vol.9 , pp. 901-915
    • Singer, K.L.1    Mostov, K.E.2
  • 94
  • 95
    • 0031889306 scopus 로고    scopus 로고
    • In vivo stimulation of polymeric Ig receptor transcytosis by circulating polymeric IgA in rat liver
    • Giffroy, D. et al. In vivo stimulation of polymeric Ig receptor transcytosis by circulating polymeric IgA in rat liver. Int. Immunol. 10, 347-354 (1998). Together with reference 94, shows that dlgA stimulates plgR transcytosis both in vitro and in vivo.
    • (1998) Int. Immunol. , vol.10 , pp. 347-354
    • Giffroy, D.1
  • 96
    • 0035150687 scopus 로고    scopus 로고
    • Polymeric IgA binding to the human plgR elicits intracellular signalling, but fails to stimulate plgR-transcytosis
    • Giffroy, D., Courtoy, P. J. & Vaerman, J. P. Polymeric IgA binding to the human plgR elicits intracellular signalling, but fails to stimulate plgR-transcytosis. Scand. J. Immunol. 53, 56-64 (2001).
    • (2001) Scand. J. Immunol. , vol.53 , pp. 56-64
    • Giffroy, D.1    Courtoy, P.J.2    Vaerman, J.P.3
  • 97
    • 0032925764 scopus 로고    scopus 로고
    • Transduction of basolateral-to-apical signals across epithelial cells: Ilgand-stimulated transcytosis of the polymeric immunoglobulin receptor requires two signals
    • Luton, F. & Mostov, K. E. Transduction of basolateral-to-apical signals across epithelial cells: Ilgand-stimulated transcytosis of the polymeric immunoglobulin receptor requires two signals. Mol. Biol. Cell 10, 1409-1427 (1999)
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1409-1427
    • Luton, F.1    Mostov, K.E.2
  • 98
    • 0035010475 scopus 로고    scopus 로고
    • Effects of mutations in potential phosphorylation sites on transcytosis of FcRn
    • McCarthy, K. M. et al. Effects of mutations in potential phosphorylation sites on transcytosis of FcRn. J. Cell Sci. 114, 1591-1598 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 1591-1598
    • McCarthy, K.M.1
  • 99
    • 0035478617 scopus 로고    scopus 로고
    • Apical to basolateral transcytosis and apical recycling of immunoglobulin G in trophoblast-derived BeWo cells: Effects of low temperature, nocodazole, and cychalasin D
    • Ellinger, I., Rothe, A., Grill, M. & Fuchs, R. Apical to basolateral transcytosis and apical recycling of immunoglobulin G in trophoblast-derived BeWo cells: Effects of low temperature, nocodazole, and cychalasin D. Exp. Cell Res. 269, 322-331 (2001).
    • (2001) Exp. Cell Res. , vol.269 , pp. 322-331
    • Ellinger, I.1    Rothe, A.2    Grill, M.3    Fuchs, R.4
  • 100
    • 0033605685 scopus 로고    scopus 로고
    • Nonvectorial surface transport, endocytosis via a di-leucine-based motif, and bidirectional transcytosis of chimera encoding the cytosolic tail of rat FcRn expressed in Madin-Darby canine kidney cells
    • Stefaner, I., Praetor, A. & Hunziker, W. Nonvectorial surface transport, endocytosis via a di-leucine-based motif, and bidirectional transcytosis of chimera encoding the cytosolic tail of rat FcRn expressed in Madin-Darby canine kidney cells. J. Biol. Chem. 274, 8998-9005 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 8998-9005
    • Stefaner, I.1    Praetor, A.2    Hunziker, W.3
  • 101
    • 0344182437 scopus 로고    scopus 로고
    • Secretory immunoglobulin A: From mucosal protection to vaccine development
    • Corthesy, B. & Spertini, F. Secretory immunoglobulin A: From mucosal protection to vaccine development. Biol. Chem. 380, 1251-1262 (1999).
    • (1999) Biol. Chem. , vol.380 , pp. 1251-1262
    • Corthesy, B.1    Spertini, F.2
  • 102
    • 0036467723 scopus 로고    scopus 로고
    • Recombinant immunoglobulin A: Powerful tools for fundamental and applied research
    • Corthésy B. Recombinant immunoglobulin A: Powerful tools for fundamental and applied research. Trends Biotech. 20, 65-71 (2002).
    • (2002) Trends Biotech. , vol.20 , pp. 65-71
    • Corthésy, B.1
  • 103
    • 0028799484 scopus 로고
    • Gene transfer into the airway epithelium of animals by targeting the polymeric immunoglobulin receptor
    • Ferkol, T. etal. Gene transfer into the airway epithelium of animals by targeting the polymeric immunoglobulin receptor. J. Clin. Invest. 95, 493-502 (1995).
    • (1995) J. Clin. Invest. , vol.95 , pp. 493-502
    • Ferkol, T.1
  • 104
    • 0029731813 scopus 로고    scopus 로고
    • Fc receptors and their interactions with immunoglobulins
    • Raghavan, M. & Bjorkman, P. J. Fc receptors and their interactions with immunoglobulins. Annu. Rev. Cell Dev. Biol. 12, 181-220 (1996).
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 181-220
    • Raghavan, M.1    Bjorkman, P.J.2
  • 105
    • 0029035201 scopus 로고
    • Generation and assembly of secretory antibodies in plants
    • Ma, J. K. et al. Generation and assembly of secretory antibodies in plants. Science 268, 716-719 (1995)
    • (1995) Science , vol.268 , pp. 716-719
    • Ma, J.K.1
  • 106
    • 0031835622 scopus 로고    scopus 로고
    • Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans
    • Ma, J K. et al. Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans. Nature Med. 4, 601-606 (1998). Together with reference 105, shows that recombinant slgA can be made in plants, and when orally administered, can decrease bacterial colonization.
    • (1998) Nature Med. , vol.4 , pp. 601-606
    • Ma, J.K.1
  • 107
    • 0036156444 scopus 로고    scopus 로고
    • Actin dependence of polarized receptor recycling in Madin-Darby canine kidney cell endosomes
    • Sheff, D. R., Kroschewski, R. & Mellman, I. Actin dependence of polarized receptor recycling in Madin-Darby canine kidney cell endosomes. Mol. Biol. Cell 13, 262-275 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 262-275
    • Sheff, D.R.1    Kroschewski, R.2    Mellman, I.3
  • 108
    • 15644371370 scopus 로고    scopus 로고
    • Sorting mechanisms regulating membrane protein traffic in the apical transcytotic pathway of polarized MDCK cells
    • Gibson, A. et al. Sorting mechanisms regulating membrane protein traffic in the apical transcytotic pathway of polarized MDCK cells. J. Cell Biol. 143, 81-94 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 81-94
    • Gibson, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.