Regulation of the formation and external transport of secretory immunoglobulins

Critical Reviews in Immunology

Volumn 19, Issue 5-6, 1999, Pages 481-508

  Norderhaug, I N ^a   Johansen, F E ^a   Schjerven, H ^a   Brandtzaeg, P ^a  

^a UNIVERSITY OF OSLO   (Norway)

Author keywords

Gene regulation; IgA; IgM; J chain; Mucosal immunity; Polymeric Ig receptor; Secretory component

Indexed keywords

CYTOKINE; IMMUNOGLOBULIN RECEPTOR; REGULATOR PROTEIN; SECRETORY COMPONENT; SECRETORY IMMUNOGLOBULIN; TRANSCRIPTION FACTOR;

GENE EXPRESSION REGULATION; HUMAN; IMMUNOGLOBULIN PRODUCING CELL; IMMUNOGLOBULIN PRODUCTION; LIGAND BINDING; PLASMA CELL; PRIORITY JOURNAL; PROTEIN TRANSPORT; REVIEW; TRANSCYTOSIS;

ANIMALS; ANTIBODY-PRODUCING CELLS; CYTOKINES; GENE EXPRESSION REGULATION; HUMANS; IMMUNOGLOBULIN A; IMMUNOGLOBULIN A, SECRETORY; IMMUNOGLOBULIN J-CHAINS; IMMUNOGLOBULIN M; RECEPTORS, POLYMERIC IMMUNOGLOBULIN; SECRETORY COMPONENT; TRANSCRIPTION FACTORS;

EID: 0033401533     PISSN: 10408401     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (224)

1. Brandtzaeg, P., Transport models for secretory IgA and secretory IgM, Clin. Exp. Immunol., 44, 221, 1981.
2. Brandtzaeg, P. and Prydz, H., Direct evidence for an integrated function of J chain and secretory component in epithelial transport of immunoglobulins, Nature, 311, 71, 1984.
3. Brandtzaeg, P., Immune functions of human nasal mucosa and tonsils in health and disease, in Immunology of the Lung and Upper Respiratory Tract Bienenstock, J., Ed., McGraw-Hill, 1984, 28.
4. Goldblum, R. M., Hanson, L. Å., and Brandtzaeg P., The mucosal defense system, in Immunologie Disorders in Infants and Children, Stiehm, E. R. Ed., W. B. Saunders Co., Philadelphia, 1996, 159.
5. Russel, M. W., Kilian, M., and Lamm, M. E., Biological activities of IgA, in Mucosal Immunology Ogra, P. L., Mestecky, J., Lamm, M. E., Strober, W. Bienenstock, J., and McGhee, J., Eds., Academic Press, San Diego, 1999, 225.
6. Mazanec, M. B., Nedrud, J. G., and Lamm, M. E., Immunoglobulin A monoclonal antibodies protect against Sendai virus, J. Virol., 61, 2624, 1987.
7. Rasmussen, M. and Silbart, L. K., Peroral administration of specific antibody enhances carcinogen excretion, J. Immunother., 21, 418, 1998.
8. Stokes, C. R., Soothill, J. F., and Turner, M. W., Immune exclusion is a function of IgA, Nature, 255, 745, 1975.
9. Persson, C. G., Gustafsson, B., Erjefalt, J. S., and Sundler, F., Mucosal exudation of plasma is a noninjurious intestinal defense mechanism, Allergy, 48, 581, 1993.
10. Outlaw, M. C. and Dimmock, N. J., Mechanisms of neutralization of influenza virus on mouse tracheal epithelial cells by mouse monoclonal polymeric IgA and polyclonal IgM directed against the viral haemagglutinin, J. Gen. Virol., 71(Pt 1), 69, 1990.
11. Brandtzaeg, P., Mucosal immunity in the female genital tract, J. Reprod. Immunol., 36, 23, 1997.
12. Johansen, F.-E., Pekna, M., Norderhaug, I. N., Haneberg, B., Hietala, M. A., Krajci, P., Betsholtz, C., and Brandtzaeg, P., Absence of epithelial IgA transport, with increased mucosal leakiness, in polymeric immunoglobulin receptor/secretary component-deficient mice, J. Exp. Med., 190, 915, 1999.
13. Brandtzaeg, P., Haraldsen, G., and Rugtveit, J., Immunopathology of human inflammatory bowel disease, Springer Semin. Immunopathol., 18, 555, 1997.
14. Scott, H., Nilsen, E., Sollid, L. M., Lundin, K. E., Rugtveit, J., Molberg, O., Thorsby, E., and Brandtzaeg, P., Immunopathology of gluten-sensitive enteropathy, Springer Semin. Immunopathol., 18, 535, 1997.
15. Duchmann, R., Neurath, M., Marker-Hermann, E., and Meyer, Z. B. K., Immune responses towards intestinal bacteria - current concepts and future perspectives, Z. Gastroenterol., 35, 337, 1997.
16. Bomsel, M., Heyman, M., Hocini, H., Lagaye, S., Belec, L., Dupont, C., and Desgranges, C., Intracellular neutralization of HIV transcytosis across tight epithelial barriers by anti-HIV envelope protein dIgA or IgM, Immunity, 9, 277, 1998.
17. Mazanec, M. B., Kaetzel, C. S., Lamm, M. E., Fletcher, D., and Nedrud, J. G., Intracellular neutralization of virus by immunoglobulin A antibodies, Proc. Natl. Acad. Sci. U.S.A., 89, 6901, 1992.
18. Mazanec M. B., Coudret, C. L., and Fletcher, D. R., Intracellular neutralization of influenza virus by immunoglobulin A anti-hemagglutinin monoclonal antibodies, J. Virol., 69, 1339, 1995
19. Burns, J.W., Siadat-Pajouh, M., Krishnaney, A. A., and Greenberg, H. B., Protective effect of rotavirus VP6-specific IgA monoclonal antibodies that lack neutralizing activity, Science, 212, 104, 1996.
20. Kaetzel, C. S., Robinson, J. K., Chintalacharuvu, K. R., Vaerman, J. P., and Lamm, M. E., The polymeric immunoglobulin receptor (secretory component) mediates transport of immune complexes across epithelial cells: a local defense function for IgA, Proc. Natl. Acad. Sci. U.S.A., 88, 8796, 1991.
21. Brandtzaeg, P., Molecular and cellular aspects of the secretory immunoglobulin system, APMIS, 103, 1, 1995.
22. Brewer, J. W., Randall, T. D., Parkhouse, R. M., and Corley, R. B., IgM hexamers? Immunol. Today, 15, 165, 1994.
23. Sørensen, V., Sundvold, V., Michaelsen, T. E., and Sandlie, I., Polymerization of IgA and IgM: roles of Cys309/Cys414 and the secretory tailpiece, J. Immunol., 162, 3448, 1999.
24. Haneberg, B., Immunoglobulins in feces from infants fed human or bovine milk, Scand. J. Immunol., 3, 191, 1974.
25. Richman, L. K. and Brown, W. R., Immunochemical characterization of IgM in human intestinal fluids, J. Immunol., 119, 1515, 1977.
26. Brandtzaeg, P., Nilssen, D. E., Rognum, T. O., and Thrane, P. S., Ontogeny of the mucosal immune system and IgA deficiency, Gastroenterol. Clin. N. Am. 20, 397, 1991.
27. Girard, J. P. and Kalbermatten, A. D., Antibody activity in human duodenal fluid, Eur. J. Clin. Invest., 1, 188, 1970.
28. Gleeson, M., Cripps, A. W., Clancy, R. L., Husband, A. J., Hensley, M. J., and Leeder, S. R., Ontogeny of the secretory immune system in man, Aust. N. Z. J. Med., 12, 255, 1982.
29. Brandtzaeg, P., Gjeruldsen, S. T., Korsrud, F., Baklien, K., Berdal, P., and Ek, J., The human secretory immune system shows striking heterogeneity with regard to involvement of J chain-positive IgD immunocytes, J. Immunol., 122, 503, 1979.
30. Brandtzaeg, P. and Nilssen, D. E., Mucosal aspects of primary B-cell deficiency and gastrointestinal infections, Curr. Opin. Gastroenterol., 11, 532, 1995.
31. Cunningham-Rundles, C., Disorders of the IgA system, in Immunologic Disorders in Infants and Children, 4th ed., Stiehm, E. R., Ed., Saunders, London, 1996, 423.
32. Cataldo, F., Marino, V., Ventura, A., Bottaro, G., and Corazza, G. R., Prevalence and clinical features of selective immunoglobulin A deficiency in coeliac disease: an Italian multicentre study. Italian Society of Paediatric Gastroenterology and Hepatology (SIGEP) and "Club del Tenue" Working Groups on Coeliac Disease, Gut, 42, 362, 1998.
33. Brandtzaeg, P., Structure, synthesis, and external transfer of mucosal immunoglobulins, Ann. Immunol. (Paris), 124, 417, 1973.
34. Giugliano, L. G., Ribeiro, S. T., Vainstein, M. H., and Ulhoa, C. J., Free secretory component and lactoferrin of human milk inhibit the adhesion of enterotoxigenic Escherichia coli, J. Med. Microbiol., 42, 3, 1995.
35. Dallas, S. D. and Rolfe, R. D., Binding of Clostridium difficile toxin A to human milk secretory component, J. Med. Microbiol., 47, 879, 1998.
36. Hammerschmidt, S., Talay, S. R., Brandtzaeg, P., and Chhatwal, G. S., SpsA, a novel pneumococcal surface protein with specific binding to secretory immunoglobulin A and secretory component, Mol. Microbiol., 25, 1113, 1997.
37. Brandtzaeg, P. and Farstad, I. N., The human mucosal B-cell system, in Mucosal Immunology, Ogra, P. L., Mestecky, J., Lamm, M. E., Strober, W., Bienenstock, J., and McGhee, J., Eds., Academic Press, San Diego, 1999, 439.
38. Brandtzaeg, P., Baekkevold, E. S., Farstad, I. N., Jahnsen, F. L., Johansen, F.-E., Nilsen, E. M., and Yamanaka, T., Regional specialization in the mucosal immune system: what happens in the microcompartments? Immunol. Today, 20, 141, 1999.
39. Brandtzaeg, P., Regionalized immune function of tonsils and adenoids, Immunol. Today, 20, 383, 1999.
40. Brandtzaeg, P., Farstad, I. N., and Haraldsen, G., Regional specialization in the mucosal immune system: primed cells do not always home along the same track, Immunol. Today, 20, 267, 1999.
41. Kelsall, B. and Strober, W., Gut-associated lymphoid tissue: antigen handling and T-lymphocyte responses, in Mucosal Immunology, Mestecky, J., Bienenstock, J., McGhee, J. R., Lamm, M. E., Strober, W., and Ogra, P. L., Eds., Academic Press, San Diego, 1999, 293.
42. McIntyre, T. M. and Strober, W., Gut-associated lymphoid tissue: regulation of IgA B-cell development, in Mucosal Immunology, Mestecky, J., Bienenstock, J., McGhee, J. R., Lamm, M. E., Strober, W., and Ogra, P. L., Eds., Academic Press, San Diego, 1999, 319.
43. Peyer, J. C., Exercitatio anatomico-medica de glandulis intestinorum, Schaffhausen, 1677
44. Hamilton, S. R., Keren, D. F., Yardley, J. H., and Brown, G., No impairment of local intestinal immune response to keyhole limpet haemocyanin in the absence of Peyer's patches, Immunology, 42, 431, 1981.
45. Farstad, I. N., Norstein, J., and Brandtzaeg, P., Phenotypes of B and T cells in human intestinal and mesenteric lymph, Gastroenterology, 112, 163, 1997.
46. Bienenstock, J., Befus, A. D., McDermott, M., Mirski, S., Rosenthal, K., and Tagliabue, A., The mucosal immunological network: compartmentalization of lymphocytes, natural killer cells, and mast cells, Ann. N.Y. Acad. Sci., 409, 164, 1983.
47. Craig, S. W. and Cebra, J. J., Peyer's patches: an enriched source of precursors for IgA-producing immunocytes in the rabbit, J. Exp. Med., 134, 188, 1971.
48. Brandtzaeg, P., Farstad, I. N., Johansen, F.-E., Morton, H. C., Norderhaug, I. N., and Yamanaka, T., The B-cell system of human mucosae and exocrine glands, Immunol. Rev., 171, 45, 1999.
49. Brandtzaeg, P., Karlsson, G., Hansson, G., Petruson, B., Bjorkander, J., and Hanson, L. A., The clinical condition of IgA-deficient patients is related to the proportion of IgD- and IgM-producing cells in their nasal mucosa, Clin. Exp. Immunol., 67, 626, 1987.
50. Drenth, J. P., Goertz, J., Daha, M. R., and van der Meer, J. W., Immunoglobulin D enhances the release of tumor necrosis factor-α, and interleukin-1β as well as interleukin-1 receptor antagonist from human mononuclear cells, Immunology, 88, 355, 1996.
51. Brandtzaeg, P., Presence of J chain in human immunocytes containing various immunoglobulin classes, Nature, 252, 418, 1974.
52. Halpern, M. S. and Koshland, M. E., Novel subunit in secretory IgA, Nature, 228, 1226, 1970.
53. Mestecky, J., Zikan, J., and Butler, W., Immunoglobulin M and secretory immunoglobulin A: evidence for a common polypeptide chain different from light chains, Science, 171, 1163, 1971.
54. Takahashi, T., Iwase, T., Takenouchi, N., Saito M., Kobayashi, K., Moldoveanu, Z., Mestecky, J., and Moro, I., The joining (J) chain is present in invertebrates that do not express immunoglobulin Proc. Natl. Acad. Sci., U.S.A., 95:1886. 1996.
55. Brandtzaeg, P., Immunohistochemical characterization of intracellular J-chain and binding site for secretory component (SC) in human immunoglobulin (Ig)-producing cells, Mol. Immunol., 20, 941, 1983.
56. Brandtzaeg, P., Role of J chain and secretory component in receptor-mediated glandular and hepatic transport of immunoglobulins in man, Scand. J. Immunol., 22, 111, 1985.
57. Vaerman, J. P., Langendries, A., and Vander Maelen, C., Homogenous IgA monomers, dimers, trimers and tetramers from the same IgA myeloma serum, Immunol. Invest., 24, 631, 1995.
58. Bastian, A., Kratzin, H., Eckart, K., and Hilschmann N., Intra- and interchain disulfide bridges of the human J chain in secretory immunoglobulin A, Biol. Chem., Hoppe Seyler, 373, 1255, 1992.
59. Garcia-Pardo, A., Lamm, M. E., Plaut, A. G., and Frangione, B., J chain is covalently bound to both monomer subunits in human secretory IgA, J. Biol. Chem., 256, 11734, 1981.
60. Underdown, B. J. and Schiff, J. M., Immunoglobulin A: strategic defense initiative at the mucosal surface, Annu. Rev. Immunol., 4, 389, 1986.
61. Krugemann, S., Pleass, R. J., Atkin, J. D., and Woof, J. M., Structural requirements for assembley of dimeric IgA probed by site directed mutagenesis of J chain and a cystein residue of the α-chain CH2 domain, J. Immunol., 159, 244, 1997.
62. Eskeland, T. and Brandtzaeg, P., Does J chain mediate the combination of 19S IgM and dimeric IgA with the secretory component rather than being necessary for their polymerization? Immunochemistry, 11, 161, 1974.
63. Cattaneo, A. and Neuberger, M. S., Polymeric immunoglobulin M is secreted by transfectants of non lymphoid cells in the absence of immunoglobulin. J chain, EMBO J., 6, 2753, 1987.
64. Randall, T. D., Brewer, J. W., and Corley, R. B. Direct evidence that J chain regulates the polymeric structure of IgM in antibody-secreting B cells, J. Biol. Chem., 267, 18002, 1992.
65. Brewer, J. W. and Corley, R. B., Late events in assembly determine the polymeric structure and biological activity of secretory IgM, Mol. Immunol., 34, 323, 1997.
66. Wiersma, E. J., Collins, C., Fazel, S., and Shulman, M. J., Structural and functional analysis of J chain-deficient IgM, J. Immunol., 160, 5979, 1998.
67. Erlandsson, L., Andersson, K., Sigvardsson, M., Lycke, N., and Leanderson, T., Mice with an inactivated joining chain locus have perturbed IgM secretion,. Eur. J. Immunol., 28, 2355, 1998.
68. Metzger, H., Structure and function of gamma M macroglobulins, Adv. Immunol., 12, 57, 1970.
69. Parkhouse, R. M., Askonas, B. A., and Dourmashkin, R. R., Electron microscopic studies of mouse immunoglobulin M; structure and reconstitution following reduction, Immunology, 18, 575, 1970.
70. Zikan, J., Mestecky, J., Kulhavy, R., and Bennett, J. C., The stoichiometry of J chain in human secretory dimeric IgA, Mol. Immunol., 23, 541, 1986.
71. Brandtzaeg, P., Immunochemical studies on free and bound J chain of human IgA and IgM, Scand. J. Immunol., 4, 439, 1975.
72. Grubb, A. O., Quantitation of J chain in human biological fluids by a simple immunochemical procedure, Acta Med. Scand., 204, 453, 1978.
73. Brandtzaeg, P., Purification of J chain after mild reduction of human immunoglobulins, Scand. J. Immunol., 4, 309, 1975.
74. Mosmann, T. R., Gravel, Y., Williamson, A. R., and Baumal, R., Modification and fate of J chain in myeloma cells in the presence and absence of polymeric immunoglobulin secretion, Eur. J. Immunol., 8, 94, 1978.
75. Boehm, M. K., Woof, J. M., Kerr, M. A., and Perkins, S. J., The Fab and Fc fragments of IgA1 exhibit a different arrangement from that in IgG: a study by X-ray and neutron solution scattering and homology modelling, J. Mol. Biol., 286, 1421, 1999
76. Feinstein, D. and Franklin, E. C., Two antigenically distinguishable subclasses of human A myeloma proteins differing in their heavy chains, Nature, 212, 1496, 1966.
77. Vaerman, J.-P. and Heremans, J. F., Subclasses of human immunoglobulin A based on differences in the α polypeptide chains, Science, 153, 647, 1966.
78. Kilian, M. and Russel, M. W., Microbial evasion of IgA functions, in Mucosal Immunology, Ogra, P. L., Mestecky, J., Lamm, M. E., Strober, W., Bienenstock, J., and McGhee, J. R., Eds., Academic Press, San Diego, 1999, 241.
79. Brandtzaeg, P., Human secretory component VI. Immunoglobulin-binding properities, Immunochemistry, 14, 179, 1977.
80. Kilian, M., Reinholdt, J., Lomholt, H., Poulsen, K., and Frandsen, E. V., Biological significance of IgA1 proteases in bacterial colonization and pathogenesis: critical evaluation of experimental evidence, APMIS, 104, 321, 1996.
81. Kett, K., Brandtzaeg, P., Radl, J., and Haaijman, J. J., Different subclass distribution of IgA-producing cells in human lymphoid organs and various secretory tissues, J. Immunol., 136, 3631, 1986.
82. Kett, K., Baklien, K., Bakken, A., Kral, J. G., Fausa, O., and Brandtzaeg, P., Intestinal B-cell isotype response in relation to local bacterial load: evidence for immunoglobulin A subclass adaptation, Gastroenterology, 109, 819, 1995.
83. Tomasi, T. B., Tan, E. M., Solomon, A., and Prendergast, R. A., Characteristics of an immune system common to external secretions, J. Exp. Med., 121, 101, 1965.
84. Brandtzaeg, P., History of oral tolerance and mucosal immunity, Ann. N.Y. Acad. Sci., 778, 1, 1996.
85. Brandtzaeg, P., Two types of IgA immunocytes in man, Nature. New Biol., 243, 142, 1973.
86. Brandtzaeg, P., Mucosal and glandular distribution of immunoglobulin components: differential localization of free and bound SC in secretory epithelial cells, J. Immunol., 112, 1553, 1974.
87. Brandtzaeg, P., Mucosal and glandular distribution of immunoglobulin components. Immunohistochemistry with a cold ethanol-fixation technique, Immunology, 26, 1101, 1974.
88. Brandtzaeg, P., Characteristics of SC-Ig complexes formed in vitro, Adv. Exp. Med. Biol., 45, 87, 1974.
89. Brandtzaeg, P., Fjellanger, I., and Gjeruldsen, S. T., Human secretory immunoglobulins. I. Salivary secretions from individuals with normal or low levels of serum immunoglobulins, Scand. J. Haematol. Suppl., 12, 3, 1970.
90. Krajci, P., Grzeschik, K. H., Geurts van Kessel, A. H., Olaisen, B., and Brandtzaeg, P., The human transmembrane secretory component (poly-Ig receptor): molecular cloning, restriction fragment length polymorphism and chromosomal sublocalization, Hum. Genet., 87, 642, 1991.
91. Krajci, P., Kvale, D., Tasken, K., and Brandtzaeg, P., Molecular cloning and exon-intron mapping of the gene encoding human transmembrane secretory component (the poly-Ig receptor), Eur. J. Immunol., 22, 2309, 1992.
92. Krajci, P., Solberg, R., Sandberg, M., Oyen, O., Jahnsen, T., and Brandtzaeg, P., Molecular cloning of the human transmembrane secretory component (poly-Ig receptor) and its mRNA expression in human tissues, Biochem. Biophys. Res. Commun., 158, 783, 1989.
93. Brandtzaeg, P., The secretory immune system of lactating human mammary glands compared with other exocrine organs, Ann. N.Y. Acad. Sci., 409, 353, 1983.
94. Mostov, K. E. and Kaetzel, C. S., Immunoglobulin transport and the polymeric immunoglobulin receptor, in Mucosal Immunology, Academic Press, San Diego, CA, 1999, 181.
95. Vaerman, J. P., Lemaitre-Coelho, I., and Jackson, G. D., Role of the liver in the rat intestinal S-IgA system, Adv. Exp. Med. Biol., 107, 233, 1978.
96. Huling, S., Fournier, G. R., Feren, A., Chuntharapai, A., and Jones, A. L., Ontogeny of the secretory immune system: maturation of a functional polymeric immunoglobulin receptor regulated by gene expression, Proc. Natl. Acad. Sci. U.S.A., 89, 4260, 1992.
97. Sollid, L. M., Kvale, D., Brandtzaeg, P., Markussen, G., and Thorsby, E., Interferon-γ enhances expression of secretory component, the epithelial receptor for polymeric immunoglobulins,. J. Immunol., 138, 4303, 1987.
98. Phillips, J. O., Everson, M. P., Moldoveanu, Z., Lue, C., and Mestecky, J., Synergistic effect of IL-4 and IFN-γ on the expression of polymeric Ig receptor (secretory component) and IgA binding by human epithelial cells, J. Immunol., 145, 1740, 1990.
99. Kvale, D. and Brandtzaeg, P., Constitutive and cytokine induced expression of HLA molecules, secretory component, and intercellular adhesion molecule1 is modulated by butyrate in the colonie epithelial cell line HT-29, Gut, 36, 737, 1995.
100. Hayashi, M., Takenouchi, N., Asano, M., Kato, M., Tsurumachi, T., Saito, T., and Moro, I., The polymeric immunoglobulin receptor (secretory component) in a human intestinal epithelial cell line is upregulated by interleukin-1, Immunology, 92, 220, 1997.
101. Kvale, D., Løvhaug, D., Sollid, L. M., and Brandtzaeg, P., Tumor necrosis factor-α upregulates expression of secretory component, the epithelial receptor for polymeric Ig, J. Immunol., 140, 3086, 1988.
102. Chintalacharuvu, K. R., Piskurich, J. F., Lamm, M. E., and Kaetzel, C. S., Cell polarity regulates the release of secretory component, the epithelial receptor for polymeric immunoglobulins, from the surface of HT-29 colon carcinoma cells, J. Cell. Physiol., 148, 35, 1991.
103. Hirata, M., Bamba, T., and Hosoda, S., The human colon cancer cell line CaCo-2 produces secretory components during enterocytic differentiation, Gastroenterol. Jpn., 28, 528, 1993.
104. Loman, S., Radl, J., Jansen, H. M., Out, T. A., and Lutter, R., Vectorial transcytosis of dimeric IgA by the Calu-3 human lung epithelial cell line: upregulation by IFN-γ. Am. J. Physiol., 272, L951, 1997.
105. Loman, S., Jansen, H. M., Out, T. A., and Lutter, R., Interleukin-4 and interferon-γ synergistically increase secretory component gene expression, but are additive in stimulating secretory immunoglobulin A release by Calu-3 airway epithelial cells, Immunology, 96, 537, 1999.
106. Brandtzaeg, P., Halstensen, T. S., Huitfeldt, H. S., Krajci, P., Kvale, D., Scott, H., and Thrane, P. S., Epithelial expression of HLA, secretory component (poly-Ig receptor), and adhesion molecules in the human alimentary tract, Ann. N.Y. Acad. Sci., 664, 157, 1992.
107. Krajci, P., Tasken, K., Kvale, D., and Brandtzaeg, P., Interferon-γ stimulation of messenger RNA for human secretory component (poly-Ig receptor) depends on continuous intermediate protein synthesis, Scand. J. Immunol., 37, 251, 1993.
108. Nilsen, E. M., Johansen, F. E., Kvale, D., Krajci, P., and Brandtzaeg, P., Different regulatory pathways employed in cytokine-enhanced expression of secretory component and epithelial HLA class I genes. Eur. J. Immunol., 29, 168, 1999.
109. Piskurich, J. F., France, J. A., Tamer, C. M. Willmer, C. A., Kaetzel, C. S., and Kaetzel, D. M Interferon-γ induces polymeric immunoglobulin receptor mRNA in human intestinal epithelial cells by a protein synthesis dependent mechanism, Mol. Immunol., 30, 413, 1993.
110. Johansen, F. E., Bosloven, B. A., Krajci, P., and Brandtzaeg, P., A composite DNA element in the promoter of the polymeric immunoglobulin receptor regulates its constitutive expression, Eur. J. Immunol. 28, 1161, 1998.
111. Piskurich, J. F., Youngman, K. R., Phillips, K. M., Hempen, P. M., Blanchard, M. H., France, J. A., and Kaetzel, C. S., Transcriptional regulation of the human polymeric immunoglobulin receptor gene by interferon-γ, Mol. Immunol., 34, 75, 1997.
112. Martin, M. G., Wang, J., Li, T. W., Lam, J. T., Gutierrez, E. M., Solorzano-Vargas, R. S., and Tsai, A. H., Characterization of the 5′-flanking region of the murine polymeric IgA receptor gene, Am. J. Physiol., 275, G778, 1998.
113. Verrijdt, G., Swinnen, J., Peeters, B., Verhoeven G., Rombauts, W., and Ciaessens, F., Characterization of the human secretory component gene promoter, Biochim. Biophys. Acta, 1350, 147, 1997.
114. Haelens, A., Verrijdt, G., Schoenmakers, E., Alen, P., Peeters, B., Rombauts, W., and Claessens, F., The first exon of the human SC gene contains an androgen recponsive unit and an interferon regulatory factor element, Mol. Cell Endocrinol., 153, 91, 1999.
115. Kaetzel, C. S., Blanch, V. J., Hempen, P. M., Phillips, K. M., Piskurich, J. F., and Youngman, K. R., The polymeric immunoglobulin receptor: structure and synthesis, Biochem. Soc. Transact., 25, 475, 1997.
116. Blanch, V. J., Piskurich, J. F., and Kaetzel, C. S., Cutting edge: coordinate regulation of IFN regulatory factor-1 and the polymeric Ig receptor by proinflammatory cytokines, J. Immunol., 162, 1232, 1999.
117. Lohoff, M., Ferrick, D., Mittrucker, H. W., Duncan, G. S., Bischof, S., Rollinghoff, M., and Mak, T. W., Interferon regulatory factor-1 is required for a T helper 1 immune response in vivo, Immunity, 6, 681, 1997.
118. Taki, S., Sato, T., Ogasawara, K., Fukuda, T., Sato M., Hida, S., Suzuki, G., Mitsuyama, M., Shin, E., H., Kojima, S., Taniguchi, T., and Asano, Y., Multistage regulation of Th1-type immune responses by the transcription factor IRF-1, Immunity, 6, 673, 1997.
119. Nilsen, E. M., Lundin, K. E., Krajci, P., Scott, H., Sollid, L. M., and Brandtzaeg, P., Gluten specific, HLA-DQ restricted T cells from coeliac mucosa produce cytokines with Th1 or Th0 profile dominated by interferon J, Gut, 37, 766, 1995.
120. Schjerven, H., Nilsen, E. M., Brandtzaeg, P., and Johansen, F.-E., IL-4 and TNF-α enhance the expression of human pig-receptor through DNA elements in the first intron, Scand. J. Immunol., (Abstract No. 36), 47, 623, 1999.
121. Denning, G. M., IL-4 and IFN-γ synergistically increase total polymeric IgA receptor levels in human intestinal epithelial cells. Role of protein tyrosine kinases, J. Immunol., 156, 4807, 1996.
122. Menge, A. C. and Mestecky, J., Surface expression of secretory component and HLA class II DR antigen on glandular epithelial cells from human endometrium and two endometrial adenocarcinoma cell lines, J. Clin. Immunol., 13, 259, 1993.
123. Rosato, R., Jammes, H., Belair, L., Puissant, C., Kraehenbuhl, J. P., and Djiane, J., Polymeric-Ig receptor gene expression in rabbit mammary gland during pregnancy and lactation: evolution and hormonal regulation, Mol. Cell Endocrinol., 110, 81, 1995.
124. Gao, J., Lambert, R. W., Wickham, L. A., Banting, G., and Sullivan, D. A., Androgen control of secretory component mRNA levels in the rat lacrimal gland, J. Steroid Biochem. Mol. Biol., 52, 239, 1995.
125. Sarkar, J., Gangopadhyay, N. N., Moldoveanu, Z., Mestecky, J., and Stephensen, C. B., Vitamin A is required for regulation of polymeric immunoglobulin receptor (pIgR) expression by interleukin-4 and interferon-γ in a human intestinal epithelial cell line, J. Nutr., 128, 1063, 1998.
126. Ha, C. L. and Woodward, B., Depression in the quantity of intestinal secretory IgA and in the expression of the polymeric immunoglobulin receptor in caloric deficiency of the weanling mouse, Lab. Invest., 78, 1255, 1998.
127. Rice, J. C., Spence, J. S., Megyesi, J., Safirstein, R. L., and Goldblum, R. M., Regulation of the polymeric immunoglobulin receptor by water intake and vasopressin in the rat kidney, Am. J. Physiol., 274, F966, 1998.
128. Carpenter, G. H., Garrett, J. R., Hartley, R. H., and Proctor, G. B., The influence of nerves on the secretion of immunoglobulin A into submandibular saliva in rats, J. Physiol. (Lond.), 512(Pt. 2), 567, 1998.
129. Brandtzaeg, P., Johansen, F.-E., Krajci, P., and Natvig, I. B., Secretory component (the polymeric Ig receptor), in Encyclopedia of Immunology, 2nd ed., Roitt, I. M. and Delves, P.-J., Eds., Academic Press, London, 1998, 2153.
130. Mostov, K. E., Transepithelial transport of immunoglobulins, Annu. Rev. Immunol., 12, 63, 1994.
131. Mostov, K. E., Friedlander, M., and Blobel, G., The receptor for transepithelial transport of IgA and IgM contains multiple immunoglobulin-like domains, Nature, 308, 37, 1984.
132. Banting, G., Brake, B., Braghetta, P., Luzio, J. P., and Stanley, K. K., Intracellular targetting signals of polymeric immunoglobulin receptors are highly conserved between species, FEBS Lett., 254, 177, 1989.
133. Kulseth, M. A., Krajci, P., Myklebust, O., and Rogne, S., Cloning and characterization of two forms of the bovine polymeric immunoglobulin receptor, DNA Cell Biol., 14, 251, 1995.
134. Verbeet, M. P., Vermeer, H., Warmerdam, G. C., de Boer, H. A., and Lee, S. H., Cloning and characterization of the bovine polymeric immunoglobulin receptor-encoding cDNA, Gene, 164, 329, 1995.
135. Piskurich, J. F., Blanchard, M. H., Youngman, K. R., France, J. A., and Kaetzel, C. S., Molecular cloning of the mouse polymeric Ig receptor. Functional regions of the molecule are conserved among five mammalian species, J. Immunol., 154, 1735, 1995.
136. Adamski, F. M. and Demmer, J., Two stages of increased IgA transfer during lactation in the marsupial, trichosurus vulpecula (Brushtail possum), J. Immunol., 162, 6009, 1999
137. Deitcher, D. L. and Mostov, K. E., Alternate splicing of rabbit polymeric immunoglobulin receptor, Mol. Cell Biol., 6, 2712, 1986.
138. Coyne, R. S., Siebrecht, M., Peitsch, M. C., and Casanova, J. E., Mutational analysis of polymeric immunoglobulin receptor/ligand interactions. Evidence for the involvement of multiple complementarity determining region (CDR)-like loops in receptor domain I, J. Biol. Chem., 269, 31620, 1994.
139. Kuhn, L. C. and Kraehenbuhl, J. P., The membrane receptor for polymeric immunoglobulin is structurally related to secretory component. Isolation and characterization of membrane secretory component from rabbit liver and mammary gland, J. Biol. Chem., 256, 12490, 1981.
140. Schaerer, E., Verrey, F., Racine, L., Tallichet, C., Reinhardt, M., and Kraehenbuhl, J. P., Polarized transport of the polymeric immunoglobulin receptor in transfected rabbit mammary epithelial cells, J. Cell Biol., 110, 987, 1990.
141. Pumphrey, R. S. H., Computer models of the human immunoglobulins, Immunol. Today, 7, 206, 1986.
142. Hughes, G. J., Frutiger, S., Savoy, L. A., Reason, A. J., Morris, H. R., and Jaton, J. C., Human free secretory component is composed of the first 585 amino acid residues of the polymeric immunoglobulin receptor, FEBS Lett., 410, 443, 1997.
143. Sletten, K., Christensen, T. B., and Brandtzaeg, P., Human secretory component. III. Carbohydrates, amino acids and N-terminal sequence, Immunochemistry, 12, 783, 1975.
144. Bakos, M. A., Kurosky, A., and Goldblum, R. M., Characterization of a critical binding site for human polymeric Ig on secretory component, J. Immunol., 147, 3419, 1991.
145. Nagura, H., Nakane, P. K., and Brown, W. R., Secretory component in immmunoglobulin deficiency: an immunoelectron microscopic study of intestinal epithelium, Scand. J. Immunol., 12, 359, 1980.
146. Okamoto, C. T., Shia, S. P., Bird, C., Mostov, K. E., and 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, 1992.
147. Apodaca, G., Katz, L. A., and Mostov, K. E., Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes, J. Cell Biol., 125, 67, 1994.
148. Breitfeld, P. P., Harris, J. M., and Mostov, K. E., Postendocytotic sorting of the ligand for the polymeric immunoglobulin receptor in Madin-Darby canine kidney cells, J. Cell Biol., 109, 475, 1989.
149. Hunziker, W., Male, P., and Mellman, I., Differential microtubule requirements for transcytosis in MDCK cells, EMBO J., 9, 3515, 1990.
150. Casanova, J. E., Breitfeld, P. P., Ross, S. A., and Mostov, K. E., Phosphorylation of the polymeric immunoglobulin receptor required for its efficient transcytosis, Science, 248, 742, 1990.
151. Hirt, R. P., Hughes, G. J., Frutiger, S., Michetti, P., Perregaux, C., Poulain-Godefroy, O., Jeanguenat, N., Neutra, M. R., and Kraehenbuhl, J. P., Transcytosis of the polymeric Ig receptor requires phosphorylation of serine 664 in the absence but not the presence of dimeric IgA, Cell, 74, 245, 1993.
152. Song, W., Apodaca, G., and Mostov, K., Transcytosis of the polymeric immunoglobulin receptor is regulated in multiple intracellular compartments, J. Biol. Chem., 269, 29474, 1994.
153. Musil, L. S. and Baenziger, J. U., Cleavage of membrane secretory component to soluble secretory component occurs on the cell surface of rat hepatocyte monolayers, J. Cell Biol., 104, 1725, 1987.
154. Ferkol, T., Kaetzel, C. S., and Davis, P. B., Gene transfer into respiratory epithelial cells by targeting the polymeric immunoglobulin receptor, J. Clin. Invest., 92, 2394, 1993.
155. Ferkol, T., Perales, J. C., Eckman, E., Kaetzel, C. S., Hanson, R. W., and Davis, P. B., Gene transfer into the airway epithelium of animals by targeting the polymeric immunoglobulin receptor, J. Clin. Invest., 95, 493, 1995.
156. Brandtzaeg, P., Human secretory immunoglobulin M. An immunochemical and immunohistochemical study, Immunology, 29, 559, 1975.
157. Fallgreen-Gebauer, E., Gebauer, W., Bastian, A., Kratzin, H. D., Eiffert, H., Zimmermann, B., Karas, M., and Hilschmann, N., The covalent linkage of secretory component to IgA. Structure of sIgA, Biol. Chem. Hoppe Seyler, 374, 1023, 1993.
158. Lamm, M. E., Cellular aspects of immunoglobulin A, Adv. Immunol., 22, 223, 1976.
159. Crottet, P. and Corthesy, B., Secretory component delays the conversion of secretory IgA into antigen-binding competent F(ab′)2: a possible implication for mucosal defense, J. Immunol., 161, 5445, 1998.
160. Lindh, E., Increased resistance of immunoglobulin A dimers to proteolytic degradation after binding of secretory component, J. Immunol., 114, 284, 1975.
161. Renegar, K. B., Jackson, G. D., and Mestecky, J., In vitro comparison of the biologic activities of monoclonal monomeric IgA, polymeric IgA, and secretory IgA, J. Immunol., 160, 1219, 1998.
162. Berdoz, J., Blanc, C. T., Reinhardt, M., Kraehenbuhl, J.-P., and Corthesy, B., In vitro comparison of the antigen-binding and stability properties of the various molecular forms of IgA antibodies assembled and produced in CHO cells, Proc. Natl. Acad. Sci. U.S.A., 96, 3034, 1999.
163. Chintalacharuvu, K. R. and Morrison, S. L., Production of secretory immunoglobulin A by a single mammalian cell, Proc. Natl. Acad. Sci. U.S.A., 94, 6364, 1997.
164. Chintalacharuvu, K. R., Tavill, A. S., Louis, L. N., Vaerman, J. P., Lamm, M. E., and Kaetzel, C. S., Disulfide bond formation between dimeric immunoglobulin A and the polymeric immunoglobulin receptor during hepatic transcytosis, Hepatology, 19, 162, 1994.
165. Knight, K. L., Vetter, M. L., and Malek, T. R. Distribution of covalently bound and non-covalently bound secretory component on subclasses of rabbit secretory IgA, J. Immunol., 115, 595, 1975.
166. Tamer, C. M., Lamm, M. E., Robinson, J. K., Piskurich, J. F., and Kaetzel, C. S., Comparative studies of transcytosis and assembly of secretory IgA in Madin-Darby canine kidney cells expressing human polymeric Ig receptor, J. Immunol., 155, 707, 1995.
167. Radl, J., Klein, F., Berg, P. V. D., Bruyn, A. M., and Hijmans, W., Binding of secretory piece to polymeric IgA and IgM paraproteins in vitro, Immunol. ogy, 20, 843, 1971.
168. Brandtzaeg, P., Complex formation between secretory component and human immunoglobulins related to their content of J chain, Scand. J. Immunol., 5., 411, 1976.
169. Vaerman, J. P., Langendries, A., Giffroy, D., Brandtzaeg, P., and Kobayashi, K., Lack of SC/ pIgR-mediated epithelial transport of a human polymeric IgA devoid of J chain: in vitro and in vivo studies, Immunology, 95, 90, 1998.
170. Brandtzaeg, P., Blocking effect of J chain and J-chain antibody on the binding of secretory component to human IgA and IgM, Scand. J. Immunol., 4, 837, 1975
171. Vaerman, J. P., Langendries, A. E., Giffroy, D. A. Kaetzel, C. S., Fiani, C. M., Moro, I., Brandtzaeg, P., and Kobayashi, K., Antibody against the human J chain inhibits polymeric Ig receptor-mediated biliary and epithelial transport of human polymeric IgA Eur. J. Immunol., 28, 171, 1998.
172. Geneste, C., Iscaki, S., Mangalo, R., and Pillot, J. Both Fcα domains of human IgA are involved in in vitro interaction between secretory component and dimeric IgA, Immunol. Lett., 13, 221, 1986.
173. Hexham, J. M., White, K. D., Carayannopoulos, L. N., Mandecki, W., Brisette, R., Yang, Y. S., and Capra, J. D., A human immunoglobulin (Ig)A Cα3 domain motif directs polymeric Ig receptor-mediated secretion, J. Exp.
174. Socken, D. J. and Underdown, B. J., Comparison of human, bovine and rabbit secretory component- immunoglobulin interactions, Immunochemistry, 15, 499, 1978.
175. Natvig, I. B., Johansen, F. E., Norderng, T. W., Haraldsen, G., and Brandtzaeg, P., Mechanism for enhanced external transfer of dimeric IgA over pentameric IgM. Studies of diffusion, binding to the human polymeric Ig receptor and epithelial transcytosis, J. Immunol., 15, 4330, 1997.
176. Røe, M., Norderhaug, I. N., Brandtzaeg, P., and Johansen, F.-E., Fine specificity of ligand-binding domain 1 in the polymeric Ig receptor: importance of the CDR2-containing region for IgM interaction, J. Immunol., 15, 6046, 1999.
177. Brandtzaeg, P., Hidden antigenic determinant in secretory immunoglobulin A, Nature, 220, 292, 1968.
178. Brandtzaeg, P., Unfolding of human secretory immunoglobulin A, Immunochemistry, 7, 127, 1970.
179. Beale, D. and Hopley, J. G., Fragmentation and reduction of bovine secretory component. Preparation of a biologically active fragment and some evidence for a multiple-domain structure, Biochem. J., 226, 661, 1985.
180. Frutiger, S., Hughes, G. J., Hanly, W. C., Kingzette, M., and Jaton, J. C., The amino-terminal domain of rabbit secretory component is responsible for noncovalent binding to immunoglobulin A dimers, J. Biol. Chem., 261, 16673, 1986.
181. Brandtzaeg, P., Human secretory component. IV. Aggregation and fragmentation of free secretory component, Immunochemistry, 12, 877, 1975.
182. Bakos, M. A., Widen, S. G., and Goldblum, R. M., Expression and purification of biologically active domain I of the human polymeric immunoglobulin receptor, Mol. Immunol., 31, 165, 1994.
183. Bakos, M. A., Kurosky, A., Czerwinski, E. W., and Goldblum, R. M., A conserved binding site on the receptor for polymeric Ig is homologous to CDR1 of Ig V kappa domains, J. Immunol., 151, 1346, 1993.
184. Underdown, B. J., Switzer, I., and Jackson, G. D., Rat secretory component binds poorly to rodent IgM, J. Immunol., 149, 487, 1992.
185. Norderhaug, I. N., Johansen, F.-E., Krajci, P., and Brandtzaeg, P., Domain deletions in the human polymeric Ig receptor disclose differences between its dimeric IgA and pentameric IgM interaction, Eur. J. Immunol., 29, 3401, 1999.
186. Bakos, M. A., Kurosky, A., Woodard, C. S., Denney, R. M., and Goldblum, R. M., Probing the topography of free and polymeric Ig-bound human secretory component with monoclonal antibodies, J. Immunol., 146, 162, 1991.
187. Zikan, J., Novotny, J., Trapane, T. L., Koshland, M. E., Urry, D. W., Bennett, J. C., and Mestecky, J., Secondary structure of the immunoglobulin J chain, Proc. Natl. Acad. Sci. U.S.A., 82, 5905, 1985.
188. Frutiger, S., Hughes, G. J., Paquet, N., Luthy, R., and Jaton, J. C., Disulfide bond assignment in human J chain and its covalent pairing with immunoglobulin M, Biochemistry, 31, 12643, 1992.
189. Guyton, A. C., Interstitial fluid pressure and dynamics of lymph formation, Fedn. Proc., 35, 1861, 1975.
190. Brown, W. R., Smith, P. D., Lee, E., McCalmon, R. T., and Nagura, H., A search for an enriched source of polymeric IgA in human thoracic duct lymph, portal vein blood, and aortic blood, Clin. Exp. Immunol., 48, 85, 1982.
191. Conley, M. E. and Delacroix, D. L., Intravascular and mucosal immunoglobulin A: two separate but related systems of immune defense? Ann. Intern. Med., 106, 892, 1987.
192. Davis, A. C., Roux, K. H., Pursey, J., and Shulman, M. J., Intermolecular disulfide bonding in IgM: effects of replacing cysteine residues in the μ heavy chain, EMBO J., 8:2519, 1989.
193. Inoue, S., Basic structure of basement membranes is a fine network of "cords," irregular anastomosing strands, Microsc. Res. Tech., 28, 29, 1994.
194. Song, W., Bomsel, M., Casanova, J., Vaerman, J. P., and Mostov, K., Stimulation of transcytosis of the polymeric immunoglobulin receptor by dimeric IgA. Proc. Natl. Acad. Sci. U.S.A., 91, 163, 1994.
195. Richardson, J. M., Kaushic, C., and Wira, C. R., Polymeric immunoglobin (Ig) receptor production and IgA transcytosis in polarized primary cultures of mature rat uterine epithelial cells, Biol. Reprod., 53, 488, 1995.
196. Song, W., Vaerman, J. P., and Mostov, K. E., Dimeric and tetrameric IgA are transcytosed equally by the polymeric Ig receptor, J. Immunol., 155, 715, 1995.
197. Giffroy, D., Langendries, A., Maurice, M., Daniel, F., Lardeux, B., Courtoy, P. J., and Vaerman, J. P., In vivo stimulation of polymeric Ig receptor transcytosis by circulating polymeric IgA in rat liver, Int. Immunol., 10, 347, 1998.
198. Luton F. and Mostov, K. E., Transduction of basolateral-to-apical signals across epithelial cells: ligand-stimulated transcytosis of the polymeric immunoglobulin receptor requires two signals, Mol. Biol. Cell, 10, 1409, 1999.
199. Singer, K. L. and Mostov, K. E., Dimerization of the polymeric immunoglobulin receptor controls its transcytotic trafficking, Mol. Biol. Cell, 9, 901, 1998.
200. Luton, F., Cardone, M. H., Zhang, M., and Mostov, K. E., Role of tyrosine phosphorylation in ligand-induced regulation of transcytosis of the polymeric Ig receptor, Mol. Biol. Cell, 9, 1787, 1998.
201. Lamm, M. E., Interaction of antigens and antibodies at mucosal surfaces, Annu. Rev. Microbiol., 51, 311, 1997.
202. Fujioka, H., Emancipator, S. N., Aikawa, M., Huang, D. S., Blatnik, F., Karban, T., DeFife, K., and Mazanec, M. B., Immunocytochemical colocalization of specific immunoglobulin A with sendai virus protein in infected polarized epithelium, J. Exp. Med., 188, 1223, 1998.
203. Brandtzaeg, P. and Baklien, K., Intestinal secretion of IgA and IgM: a hypothetical model, Ciba. Found. Symp., 77, 1977.
204. Phillips, A. D., Mechansim of mucosal injury: human studies, in Viruses and the Gut, Farthing, M. J. G., Ed., Smith Kline & French Laboratories Limited, 1992, 30.
205. Savidge, T. C., Walker-Smith, J. A., and Phillips, A. D., Novel insights into human intestinal epithelial cell proliferation in health and disease using confocal microscopy, Gut, 36, 369, 1995.
206. Renegar, K. B. and Small, P. A., Passive immunization: sysetmic and mucosal, in Mucosal Immunology, Ogra, P. L., Mestecky, J., Lamm, M. E., Strober, W., Bienenstock, J., and McGhee, J., Eds., Academic Press, San Diego, CA, 1999, 729.
207. Hammarström, L., Gardulf, A., Hammarström, V., Janson, A., Lindberg, K., and Smith, C. I., Systemic and topical immunoglobulin treatment in immunocompromised patients, Immunol. Rev., 139, 43, 1994.
208. Ma, J. K., Hikmat, B. Y., Wycoff, K., Vine, N. D., Chargelegue, D., Yu, L., Hein, M. B., and Lehner, T., Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans, Nat. Med., 4, 601, 1998.
209. Johansen, F.-E., Norderhaug, I. N., Røe, M., Sandlie, L, and Brandtzaeg, P., Recombinant expression of polymeric IgA: incorporation of J chain and secretroy component of human origin, Eur. J. Immunol., 29, 1701, 1999.
210. Ma, J. K., Hiatt, A., Hein, M., Vine, N. D., Wang, F., Stabila, P., van Dolleweerd, C., Mostov, K., and Lehner, T., Generation and assembly of secretory antibodies in plants, Science, 268, 716, 1995.
211. Gan, Y. J., Chodosh, J., Morgan, A., and Sixbey, J. W., Epithelial cell polarization is a determinant in the infectious outcome of immunoglobulin A-mediated entry by Epstein-Barr virus, J. Virol., 71, 519, 1997.
212. Schroten, H., Stapper, C., Plogmann, R., Kohler, H., Hacker, J., and Hanisch, F. G., Fab-independent antiadhesion effects of secretory immunoglobulin A on S-fimbriated Escherichia coli are mediated by sialyloligosaccharides, Infect. Immun., 66, 3971, 1998.
213. Brandtzaeg, P., Humoral immune response patterns of human mucosae: Induction and relation to bacterial respiratory tract infections, J. Infect. Dis., 165, S167, 1992.
214. Brandtzaeg, P., Synthesis and secretion of human salivary immunoglobulins, In Glandular Mechanisms of Salivary Secretion, Garret, J. R., Ekström, J., and Anderson, L. C., Eds., Front Oral Biol., Karger, Basel 1998, 10, 167.
215. Haneberg, B., Human milk immunoglobulins and agglutinins to rabbit erythrocytes, Int. Arch. Allerg Appl. Immunol., 47, 716, 1974.
216. Fullard, R. J., Protein levels in nonstimulated and stimulated tears of normal human subjects, Invest. Ophthalmol., 31, 1119, 1990.
217. Mygind, N., Quantitative determination of immunoglobulins in nasal secretion, Int. Arch. Allergy Appl. Immunol., 49, 99, 1975.
218. Peebles, R., IgA. IgG, and IgM quantification in bronchoalveolar lavage fluids from allergic rhinitics allergic asthmatics, and normal subjects by monoclonal antibody-based immunoenzymetric assays, J. Immunol. Methods, 179, 77, 1995.
219. Girard, J. P. and de Kalbermatten, A., Antibody activity in human duodenal fluid, Eur. J. Clin. Invest., 1, 188, 1970.
220. Bull, D. M., Bienenstock, J., Tomasi, T. B., Jr. Studies on human intestinal immunoglobulin A, Gastroenterology, 60, 370, 1971.
221. Feltelius, N., Hvatum, M., Brandtzaeg, P., Knutson, L., and Hallgren, R., Increased jejunal secretory IgM and IgM in ankylosing spondylitis: normalization after treatment with sulfasalazine, J. Rheumatol., 21, 2076, 1994.
222. Kutteh, W. H., Hatch, K. D., Blackwell, R. E., and Mestecky, J., Secretory immune system of the female reproductive tract. I. Immunoglobulin and secretory component-containing cells, Obstet. Gynecol., 71, 56, 1988.
223. Hordnes, K., Tynning, T., Kvam, A. I., Jonsson, R., and Haneberg, B., Colonization in the rectum and uterine cervix with group B streptococci may induce specific antibody responses in cervical secretions of pregnant women, Infect. Immun., 64, 1643, 1996.
224. James-Ellison M. Y., Roberts, R., Verrier-Jones, K., Williams, J. D., and Topley, N., Mucosal immunity in the urinary tract: changes in sIgA, FSC, and total IgA with age and in urinary tract infection, Clin. Nephrol., 48, 69, 1997.