Drug – bio-affecting and body treating compositions – Immunoglobulin – antiserum – antibody – or antibody fragment,... – Binds expression product or fragment thereof of...
Reexamination Certificate
2005-06-14
2005-06-14
Andres, Janet (Department: 1646)
Drug, bio-affecting and body treating compositions
Immunoglobulin, antiserum, antibody, or antibody fragment,...
Binds expression product or fragment thereof of...
C530S387100, C530S388100, C530S202000, C530S350000, C424S139100
Reexamination Certificate
active
06905685
ABSTRACT:
Disclosed herein are the methods of using the H4-1BB protein, ligands to this protein, and various mAbs either directed against H4-1BB or other molecules that can be used therapeutically. The nature and importance of the H4-1BB molecule provides the ligands and related co-stimulatory molecules the ability to enhance or suppress T-cell activation and proliferation. By treating T-cells that have expressed receptor protein H4-1BB with one of the four anti-H4-1BB monoclonal antibodies disclosed herein activation or inhibition of the immune response is seen. Also disclosed herein is cDNA for the human receptor H4-1BB. The cDNA of the human receptor H4-1BB is about 65% homologous to the mouse cDNA 4-1BB and was isolated by using probes derived from murine cDNA 4-1BB. A fusion protein for detecting cell membrane ligands to human receptor protein H4-1BB was developed. It comprises the extracellular portion of the receptor protein H4-1BB and a detection protein, alkaline phosphatase, bound to the portion of the receptor protein H4-1BB. B-cells that have expressed a ligand to receptor protein H4-1BB can be treated with cells that have expressed receptor protein H4-1BB and B-cell proliferation may be induced. The use of H4-1BB to block H4-1BB ligand binding has practical application in the suppression of the immune system during organ transplantation or against autoimmune diseases including diabetes, rheumatoid arthritis, and lupus. Other applications of this technology include the development of therapeutic methods for the treatment of HIV-1 infected individuals, and the treatment of cancerous tumors.
REFERENCES:
patent: 5674704 (1997-10-01), Goodwin et al.
patent: 5928893 (1999-07-01), Kang et al.
patent: 96/29348 (1996-09-01), None
patent: 97/33898 (1997-09-01), None
Bressler et al., “Anti-CD2 Receptor Antibodies Activate the HIV Long Terminal Repeat in T Lymphocytes”, J. Immunology 1991 174(7) :2290-2294.
Carthew et al., “seven in absentia, a Gene Required for Specificaiton of R7 Cell Fate in the Drosophila Eye”, Cell 1990 63:561-577.
Defrance et al., “Interleukin 10 and Transforming Growth Factor β Cooperate to Induce Anti-CD40-activated Naive Human B Cells to Secrete Immunoglobulin A”, J. Exp. Med. 1992 175:671-682.
Haskins et al., “The Major Histocompatibility Complex-Restricted Antigen Receptor on T Cells”, J. Exp, Med. 1983 157:1149-1169.
Kwon et al., “Isolation and initial characterization of multiple species of T-lymphocyte subset cDNA clones”, Proc. Natl. Acad. Sci. USA 1987 84:2896-2900.
Mallett et al., “A new superfamily of cell surface proteins related to the nerve growth factor receptor”, Immunology Today 1991 12(7) :220-223.
Maraskovsky et al., “Co-engagement of CD3 with LFA-1 or 1CAM-1 adhesion molecules enhances the frequency of activation of single murine CD4+ and CD8+ T cells and induces synthesis of IL-3 and IFN-γ but not IL-4 or IL-6”, International Immunology 1992 4(4):475-485.
Mueller et al., “Clonal Expansion Versus Functional Clonal Inactivation: A Costimulatory Signalling Pathway Determines the Outcome of T Cell Antigen Receptor Occupancy1”, Ann. Rev. Immunol. 1989 7:445-480.
Noelle et al., “Cognate interactions between helper T cells and B Cells”, Immunology Today 1990 11(10):361-368.
Van Lier et al., “Tissue Distribution and Biochemical and Functional Properties of Tp55 (CD27), A Novel T Cell Differentiation Antigen”, J. Immunology 1987 139(5):1589-1596.
Debenedette et al., “Costimulation of CD38-T Lymphocytes by 4-1BB Ligand”, J. Immunology 1997 158(2):551-559.
Kwon et al., “cDNA sequences of two inducible T-cells genes”, Proceedings of the National Academy of Sciences 1989 86(6):1963-1967.
Melero et al., “Monoclonal Antibodies Against the 4-1BB T-cell Activation Molecule Eradicate Established Tumors”, Nature Medicine 1997 3(6):682-685.
Schwartz et al., “A receptor induced by lymphocyte activation (ILA) :a new member of the human nerve-growth-factor/tumor-necrosis-factor receptor family”, Gene 1993 134:295-298.
Shuford et al., “4-1BB Costimulatory Signals Preferentially Induce CD8+ T Cells Proliferation and Lead to the Amplification In Vivo of Cytotoxic T Cell Responses”, J. Experimental Medicine 1997 186(1):47-55.
Alderson, M.R., et al., “Molecular and Biological Characterization of Human 4-1BB and its Ligand”,Eur. J. Immunol., 24, pp. 2219-2227, (1994).
Debenedette, M.A., et al., “Costimulation of CD28-T Lymphocytes by 4-1BB Ligand”,The Journal of Immunology, 158(2), pp. 551-559, (1997).
Melero, I., et al., “Monoclonal Antibodies Against the 4-1BB T-cell Activation Molecule Eradicate Established Tumors”,Nature Medicine, 3(6), pp. 682-685, (Jun. 1997).
Pollok, K.E., et al., “Inducible T Cell Antigen 4-1BB”,J. Immunol., 150(3), pp. 771-781, (1993).
Shuford, W.W., et al., “4-1BB Costimulatory Signals Preferentially Induce CD8+ T Cells Proliferation and Lead to the Amplification In Vivo of Cytotoxic T Cell Responses”,The Journal of Experimental Medicine, 186(1), pp. 47-55, (1997).
LandOfFree
Methods of using antibodies to human receptor protein 4-1BB does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Methods of using antibodies to human receptor protein 4-1BB, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Methods of using antibodies to human receptor protein 4-1BB will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3516304