Drug – bio-affecting and body treating compositions – Immunoglobulin – antiserum – antibody – or antibody fragment,... – Monoclonal antibody or fragment thereof
Reexamination Certificate
2006-10-17
2006-10-17
Gambel, Phillip (Department: 1644)
Drug, bio-affecting and body treating compositions
Immunoglobulin, antiserum, antibody, or antibody fragment,...
Monoclonal antibody or fragment thereof
C424S130100, C424S133100, C424S141100, C424S143100, C424S144100, C424S153100, C424S173100, C530S387100, C530S387300, C530S388100, C530S388200, C530S388220, C530S388700, C530S388730, C530S387700
Reexamination Certificate
active
07122187
ABSTRACT:
The present invention is directed to humanized antibodies which bind human gp39 and their use as therapeutic agents. These humanized antibodies are especially useful for treatment of autoimmune diseases; and an immunosuppressant during transplantation of heterologous cells, tissues or organs, cell therapy, and gene therapy.
REFERENCES:
patent: 4816397 (1989-03-01), Boss
patent: 4816567 (1989-03-01), Cabilly
patent: 4975369 (1990-12-01), Beavers
patent: 4978745 (1990-12-01), Schoemaker
patent: 5474771 (1995-12-01), Lederman
patent: 5683693 (1997-11-01), Noelle
patent: 5747037 (1998-05-01), Noelle
patent: 5833987 (1998-11-01), Noelle
patent: 5876718 (1999-03-01), Noelle
patent: 5902585 (1999-05-01), Noelle
patent: 6001358 (1999-12-01), Black et al.
patent: 6136310 (2000-10-01), Hanna et al.
patent: 6440418 (2002-08-01), Black et al.
patent: 6506383 (2003-01-01), Black et al.
patent: 0 451 216 (1991-10-01), None
patent: 0 519 596 (1992-12-01), None
patent: 0 555 880 (1993-08-01), None
patent: 0 555 880 (1993-08-01), None
patent: 0 585 943 (1994-03-01), None
patent: 0 682 040 (1995-11-01), None
patent: WO93/08207 (1993-04-01), None
patent: WO93/09812 (1993-05-01), None
patent: WO94/04570 (1994-03-01), None
patent: WO95/06480 (1995-03-01), None
patent: WO95/06666 (1995-03-01), None
patent: WO95/28957 (1995-11-01), None
patent: WO96/23071 (1996-08-01), None
patent: WO97/17446 (1997-05-01), None
patent: WO98/08541 (1998-03-01), None
patent: WO99/12566 (1999-03-01), None
Duncan et al. Nature 332: 563-564, 1988.
Alderson MR, et al., “CD40 expression by human monocytes: regulation by cytokines and activation of monocytes by the ligand for CD40,”J Exp Med,1993, 178: 669-74.
Alexander-Miller, et al., “Alloreactive cytotoxic T lymphocytes generated in the presence of viral-derived peptides show exquisite peptide and MHC specificity,” J. Immunol., 1993, 151:1-10.
Allen RC, et al., “CD40 ligand gene defects responsible for X-linked hyper-IgM syndrome,”Science,1993, 259: 990-3.
Andersson J, et al., “T-cell-dependent B-cell stimulation is H-2 restricted and antigen dependent only at the resting B-cell level,”Proc Natl Acad Sci U S A,1980, 77: 1612-6.
Armitage RJ, et al., “Molecular and biological characterization of a murine ligand for CD40,”Nature,1992, 357: 80-2.
Aruffo A, et al., “The CD40 ligand, gp39, is defective in activated T cells from patients with X-linked hyper-IgM syndrome,”Cell,1993, 72: 291-300.
Bach JF, “Immunosuppressive therapy of autoimmune diseases,”Trends Pharmacol Sci.,1993, 14(5):213-6.
Bartlett WC, et al., “Cognate interactions between helpher T cells and B cells. II. Dissection of cognate help by using a class II-restricted, antigen-specific, IL-2-dependent helper T cell clone,”J Immunol,1989, 143:1745-54.
Bartlett WC, et al., “Cognate interactions between helper T cells and B cells. IV. Requirements for the expression of effector phase activity by helper T cells,”J Immunol,1990, 145: 3956-62.
Bebbington CR, et al., “High-level expression of a recombinant antibody from myeloma cells using a glutamine synthetase gene as an amplifiable selectable marker,”Biol. Technology,1992, 10:169.
Benhar et al., “Rapid humanization of the Fv of monoclonal antibody B3 by using framework exchange of the recombinant immunotoxin B3(Fv)-PE38,”Proc. Natl. Acad. Sci. USA,1994, 91:12051-5.
Bhatia S., et al., “In vivo administration of anti-CD40 ligand (gp39) blocks the rejection of MHC class II disparate skin allografts,” 9thIntl. Congress of Immunology, Jul. 23-29, 1995, San Francisco, CA, p. 311.
Biancone L. et al., “Inhibition of the CD40-CD40ligand pathway prevents murine membranous glomerulonephritis,”Kidney Int.,1995, 48(2):458-68.
Blair P. et al., “CD40 ligand (CD154) triggers a short-term CD4+ T cell activation response that results in secretion of immunomodulatory cytokines and apoptosis,”The Journal of Experimental Medicine,2000, 191(4):651-60.
Brennan FM, et al., “Enhanced expression of tumor necrosis factor receptor mRNA and protein in mononuclear isolated from rheumatoid arthritis synovial joints,”Eur J Immunol,1992, 22: 1907-12.
Brian AA, “Stimulation of B-cell proliferation by membrane-associated molecules from activated T cells,”Proc Natl Acad Sci U S A,1988, 85: 564-8.
Bulens et al., “Construction and characterization of a functional chimeric murine-human antibody directed against human fibrin fragment-D dimer,”Eur. J. Biochem.,1991, 195:235-42.
Burns C, et al., “Anti-CD40 Ligand antibody treatment of NZB/NZW murine lupus-like nephritis,” Arthritis and Rheumatism, 1994, 37(Suppl):S390 (Poster 1371).
Carlsson et al., “Human peripheral blood lymphocytes transplanted into SCID mice constitute in vivo culture system exhibiting several parameters found in a normal humoral immune response and are a source of immunocytes for the production of human monoclonal antibodies,”J. Immunol.1992, 148:1065.
Caron et al., “Biological and immunological features of humanized M195 (Anti-CD33) monoclonal antibodies,”Cancer Res.,1992, 32:67671-7.
Carroll et al., “Hybridoma fusion cell lines contain an aberrant kappa transcript,”Mol. Immunol.,1988, 10:991.
Cathcart ES, et al., “Experimental arthritis in a nonhuman primate. I. Induction by bovine type II collagen,”Lab Invest,1986, 54: 26-31.
Chambers-Slater K, et al., “A humanized anti-human primate,”The FASEB Journal,Mar. 15, 1999, 13(5):2, p. A988.
Chaudhary VK, et al., “A recombinant immunotoxin consisting of two antibody variable domains fused toPseudomonas exotoxin,” Nature,1989, 339:394-7.
Chu CQ, et al., “Localization of tumor necrosis factor alpha in synovial tissues and at the cartilage-pannus junction in patients with rheumatoid arthritis,”Arthritis Rheum,1991, 34: 1125-32.
Claman HN and Chaperon, “Immunologic complementation between thymus and marrow cells-a model for the two-cell theory of immunocompetence,”Transplant Rev,1969, 1: 92-113.
Clark EA, et al., “CD40: a cytokine receptor in search of a ligand,”Tissue Antigens,1990, 36: 33-6.
Clark EA et al., “How B and T cells talk to each other,”Nature,1994, 367(6462):425-8.
Clement LT, et al., “Small, resting B cells can be induced to proliferate by direct signals from activated helper T cells,”J Immunol,1984, 132: 740-4.
Cobbold SP, et al., Monoclonal antibodies to promote marrow engraftment and tissue graft tolerance,Nature,1986, 323(6084):164-6.
Colcher et al., “Characterization and biodistribution of recombinant/chimeric constructs of monoclonal antibody B72.3,”Cancer Res.,1989, 49:1738-45.
Coloma, et al., “Novel vectors for the expressilon of antibody molecules using variable regiions generated by polymerase chain reaction,”J. Immunol. Meth.,1992, 152:89-104.
Courtenay et al., “Immunisation against heterologous type II collagen induces arthritis in mice,”Nature,1980, 283(5748):666-8.
Couto et al., “Humanization of KC4G3, an antihuman carcinoma antibody,”Hybridoma,1994, 13(3):215-9.
Cox et al., “A directory of human germ-line Vx segments reveals a strong bias in their usage,”Eur. J. Immunol.,1994, 24:827-36.
Crow et al., “Direct T Helper-B cell interactions Induce an early B cell activation antigen,”J Exp Med.,1986, 164:1760-72.
Crow et al., “Human peripheral blood T helper cell-induced B cell activation results in B cell surface expression of the CD23 (BLAST-2) antigen,”Cell Immunol.1989, 121(1):99-112.
De Waele et al., “Expression in non-lymphoid cells of mouse recombinant immunoglobulin directed against the tumour marker human placental alkaline phosphatase,”Eur. J. Biochem.,1988, 176:287-95.
DiGiovane et al., “tumour necrosis factor in synovial exudates,”Ann.
Black Amelia
Hanna Nabil
Newman Roland A.
Padian Eduardo A.
Biogen IDEC Inc.
Gambel Phillip
Pillsbury Winthrop Shaw & Pittman LLP
LandOfFree
Treating autoimmune diseases with humanized anti-CD40L antibody does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Treating autoimmune diseases with humanized anti-CD40L antibody, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Treating autoimmune diseases with humanized anti-CD40L antibody will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3642306