Drug – bio-affecting and body treating compositions – Immunoglobulin – antiserum – antibody – or antibody fragment,... – Structurally-modified antibody – immunoglobulin – or fragment...
Reexamination Certificate
2007-12-25
2007-12-25
Romeo, David S. (Department: 1647)
Drug, bio-affecting and body treating compositions
Immunoglobulin, antiserum, antibody, or antibody fragment,...
Structurally-modified antibody, immunoglobulin, or fragment...
C424S804000, C424S806000, C514S012200, C530S300000, C530S387300, C530S861000, C530S863000
Reexamination Certificate
active
09005318
ABSTRACT:
Targeting molecules for use in delivering biological agents to epithelial tissue are disclosed. Upon delivery, the biological agent(s) may remain within an epithelial cell or may undergo transepithelial transport via transcytosis. The targeting molecules may be used, for example, for the delivery of therapeutic agents.
REFERENCES:
patent: 4350764 (1982-09-01), Baxter et al.
patent: 4897384 (1990-01-01), Janoff et al.
patent: 5169627 (1992-12-01), Cunningham-Rundles
patent: 5202422 (1993-04-01), Hiatt et al.
patent: 5254342 (1993-10-01), Shen et al.
patent: 5284931 (1994-02-01), Springer et al.
patent: 5366958 (1994-11-01), Weiner et al.
patent: 5639947 (1997-06-01), Hiatt et al.
patent: 5670626 (1997-09-01), Chang
patent: 5814507 (1998-09-01), Cheng et al.
patent: 6063905 (2000-05-01), Capra et al.
patent: 58-134032 (1983-08-01), None
patent: WO 92/16622 (1992-10-01), None
Creighton TE. (1984) Proteins: Structures and Molecular Properties. W.H. Freeman, New York, p. 2.
Weissleder et al. Quantitation of slow drug release from an implantable and degradable gentamicin conjugate by in vivo magnetic resonance imaging. Antimicrob Agents Chemother Apr. 1995;39(4):839-45.
Bowie et al. Deciphering the message in protein sequences: tolerance to amino acid substitutions. Science, (Mar. 16, 1990) 247 (4948) 1306-10.
Ngo et al., in The Protein Folding Problem and Tertiary Structure Prediction, Merz and Le Grand (Eds), Aug. 1994, Springer Verlag, pp. 433 and 492-495.
Pierce Chemical Company. ImmunoTechnology Catalog and Handbook. 1992-93, pp. E-8, E-15, E-21, E-58.
Carayannopoulos et al. Recombinant human IgA expressed in insect cells. Proc Natl Acad Sci U S A. Aug. 30, 1994;91(18):8348-52.
Carayannopoulos et al. Localization of the binding site for the monocyte immunoglobulin (Ig) A-Fc receptor (CD89) to the domain boundary between Calpha2 and Calpha3 in human IgA1. J Exp Med Apr. 1, 1996;183(4):1579-86.
Morton et al. Purification and characterization of chimeric human IgA1 and IgA2 expressed in COS and Chinese hamster ovary cells. J Immunol Nov. 1, 1993;151(9):4743-52.
Lemaitre-Coelho et al. In vivo experiments involving secretory component in the rat hepatic transfer of polymeric IgA. Immunology Jun. 1981;43(2):261-70.
Koshland ME. The coming of age of the immunoglobulin J chain. Annu Rev Immunol. 1985;3:425-53.
Brandtzaeg et al. Intestinal secretion of IgA and IgM: a hypothetical model. Ciba Found Symp. Apr. 26-28, 1977;(46):77-113.
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. 1975;4(8):837-42.
Bowie et al. Deciphering the message in protein sequences: tolerance to amino acid substitutions. Science, (Mar. 16, 1990) 247 (4948) 1306-10.
Ngo et al., in The Protein Folding Problem and Tertiary Structure Prediction, Merz and Le Grand (Eds), Aug. 1994, Springer Verlag, pp. 433 and 492-495.
Marston FA. The purification of eukaryotic polypeptides synthesized inEscherichia coli.Biochem J. Nov. 15, 1986;240(1):1-12.
Janknecht et al. Affinity purification of histidine-tagged proteins transiently produced in HeLa cells. Gene. Nov. 16, 1992;121(2):321-4.
Chamow SM, Ashkenazi A. Immunoadhesins: principles and applications. Trends Biotechnol. Feb. 1996;14(2):52-60.
Martin et al. Efficient neutralization and disruption of rhinovirus by chimeric ICAM-1/immunoglobulin molecules. J Virol. Jun. 1993;67(6):3561-8.
Ferkol et al., “Gene Transfer into Respiratory Epithelial Cells by Targeting the Polymeric Immunoglobulin Receptor,”J. Clin. Invest. 92: 2394-2400, 1993.
Terskikh et al., “Dimeric Recombinant IgA Directed Against Carcino-Embryonic Antigen, A Novel Tool For Carcinoma Localization,”Molecular Immunology 31(17): 1313-1319, 1994.
Hendrickson et al., “Altered Hepatic Transport of Immunoglobulin A in Mice Lacking the J Chain,”J. Exp. Med. 182: 1905-1911, 1995.
Max and Korsmeyer, “Human J Chain Gene. Structure and Expression in B Lymphoid Cells,”Journal of Experimental Medicine 161: 832-849, 1985.
Frutiger et al., “Disulfide Bond Assignment in Human J Chain and Its Covalent Pairing with Immunoglobulin M,”Biochemistry 31: 12643-12647, 1992.
Allen et al., “An immunoperoxidase study of epithelial marker antigens in ulcerative colitis with dysplasia and carcinoma,”J. Clin. Pathol. 38: 18-29, 1985.
Brown and Koshland, “Evidence for a long-range conformational change induced by antigen binding to IgM antibody,”Proc. Natl. Acad. Sci. USA 74(12): 5682-5686, 1977.
Brandtzaeg and Baklien, “Immunohistochemical studies of the immunoglobulin-producing cell systems of the human intestinal mucosa,”Acta Histochemica Suppl. 21: 105-119, 1980.
Burns et al., “Protective Effect of Rotavirus VP6-Specific IgA Monoclonal Antibodies That Lack Neutralizing Activity,”Science 272: 104-107, 1996.
Emancipator and Lamm, “IgA Nephropathy: Overproduction of Decreased Clearance of Immune Complexes?”Laboratory Investigation 61(4): 365-367, 1989.
Kaetzel et al., “Epithelial Transcytosis of Monomeric IgA and IgG Cross-linked Through Antigen to Polymeric IgA. A Role for Monomeric Antibodies in the Mucosal Immune System,”Journal of Immunology 152: 72-76, 1994.
Kaetzel et al., “The polymeric immunoglobulin receptor (secretory component) mediates transport of immune complexes across epithelial cells: A local defense function for IgA,”Proc. Natl. Acad. Sci. 88: 8796-8800, 1991.
Kulseth and Rogne, “Cloning and Characterization of the Bovine Immunoglobulin J Chain cDNA and Its Promoter Region,”DNA and Cell Biology 13(1): 37-42, 1994.
Mannik and Arend, “Fate of Preformed Immune Complexes in Rabbits and Rhesus Monkeys,”Journal of Experimental Medicine 134(3 pt. 2): 19s-31s, 1971.
Mazanec et al., “Intracellular Neutralization of Influenza Virus by Immunoglobulin A Anti-Hemagglutinin Monoclonal Antibodies,”Journal of Virology 69(2): 1339-1343, 1995.
Mestecky et al., “The Role of the Liver in Catabolism of Mouse and Human IgA,”Immunological Investigations 18(1-4): 313-324, 1989.
Nagura et al., “Translocation of Dimeric IgA Through Neoplastic Colon Cells In Vitro,”Journal of Immunology 123(5): 2359-2368, 1979.
Rifai and Mannik, “Clearance Kinetics and Fate of Mouse IgA Immune Complexes Prepared with Monomeric or Dimeric IgA,”Journal of Immunology 130(4): 1826-1832, 1983.
Rifai et al., “Clearance Kinetics and Fate of Macromolecular IgA in Patients with IgA Nephropathy,”Laboratory Investigation 61(4): 381-388, 1989.
Sheldrake et al., “Selective Transport of Serum-Derived IgA Into Mucosal Secretions,”Journal of Immunology 132(1): 363-368, 1984.
Verma and Somia, “Gene therapy—promises, problems and prospects,”Nature 389: 239-242, 1997.
Wells, James A., “Perspectives in Biochemistry. Additivity of Mutational Effects in Proteins,”Biochemistry 29(37): 8509-8517, 1990.
Youngman et al., “Inhibition of IFN-γ Activity in Supernatants from Stimulated Human Intestinal Mononuclear Cells Prevents Up-Regulation of the Polymeric Ig Receptor in an Intestinal Epithelial Cell Line,”Journal of Immunology 153: 675-681, 1994.
Hexham, J., et al., “A Human Immunoglobulin (Ig)A Cα3 Domain Motif Directs Polymeric Ig Receptor-Mediated Secretion,”J. Exp. Med.,1999, pp. 747-751, vol. 189(4), The Rockefeller University Press.
Johansen, F., et al., “The J Chain is Essential for Polymeric Ig Receptor-Mediated Epithelial Transport of IgA,”Journal of Immunology, 2001, pp. 5185-5192, The American Association of Immunologists.
Vaerman, J., et al., “Antibody Against the Human J Chain Inhibits Polymeric Ig Receptor-Mediated Biliary and Epithelial Transport of Human Polymeric IgA,”Eur. J. Immunol., 1998, pp. 171-182, vol. 28, WILEY-VCH Verlag GmbH, Weinheim, Germany.
White, K.D. and J.D. Capra, “Targeting Mucosal Si
Fitchen John H.
Hein Mich B.
Hiatt Andrew C.
Alston & Bird LLP
Plantbodies Corporation
Romeo David S.
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