Anti-hydroxylase antibodies and uses thereof

Details Anti-hydroxylase antibodies and uses thereof Anti-hydroxylase antibodies and uses thereof

2004-11-15

2008-08-19

Canella, Karen A. (Department: 1643)

Drug, bio-affecting and body treating compositions

Immunoglobulin, antiserum, antibody, or antibody fragment,...

Monoclonal antibody or fragment thereof

C424S152100, C424S155100, C530S387300, C530S387700, C530S388150, C530S388800

Reexamination Certificate

active

07413737

ABSTRACT:
Antibodies, or antigen-binding portions thereof, to aspartyl (asparaginyl) β-hydroxylase are provided. The anti-aspartyl (asparaginyl) β-hydroxylase antibodies, or antigen-binding portions thereof, can modulate activity of aspartyl (asparaginyl) β-hydroxylase.

REFERENCES:
patent: 4946778 (1990-08-01), Ladner et al.
patent: 5565332 (1996-10-01), Hoogenboom et al.
patent: 6166176 (2000-12-01), Radosevich
patent: 6727080 (2004-04-01), Radosevich
patent: 6783758 (2004-08-01), Wands et al.
patent: 6797696 (2004-09-01), Wands et al.
patent: 6812206 (2004-11-01), Wands et al.
patent: 6815415 (2004-11-01), Wands et al.
patent: 6835370 (2004-12-01), Wands et al.
patent: 7094556 (2006-08-01), Wands et al.
patent: WO 82/01461 (1982-05-01), None
patent: WO 01/35102 (2001-05-01), None
patent: WO 02/092782 (2002-11-01), None
patent: WO 03/100087 (2003-12-01), None
patent: WO 2005/003302 (2005-01-01), None
patent: WO 2005/016381 (2005-02-01), None
Gura (1997, Science 278:1041-1042).
White et al. (2001, Ann. Rev. Med. 52:125-145).
Bowie et al, Science, 247:1306-1310, 1990, p. 1306, col.2.
Gussow et al. (1991, Methods in Enzymology 203:99-121).
Rudikoff et al. (PNAS, USA, 1982, 79: 1979).
Lavaissiere et al. (1996, J. Clin. Invest. 98(6):1313-1323).
Daugherty et al. (2000, Proc. Natl. Acad. Sci. USA 97(5):2029-2034).
D'Amico et al., “Use of anti-HAAH antibodies in cancer therapy:specific delivery of cytotoxic agents”, AACR Annual Meeting, Apr. 14-18, 2007, Los Angeles, CA.
De la Monte, et al., “Aspartyl (Asparaginyl) β-Hydroxylase regulates hepatocellular carcinoma invasiveness”, J. of Hepatology, 44:971-983 (2006).
Finney et al., “Anti-Proliferative and Anti-Metastatic Activities of Monoclonal Antibodies to Human Aspartyl (Asparaginyl) β-Hydroxylase”, Abstract and Poster presented at the AACR Meeting of Nov. 17-21, 2003, Boston, MA.
Finney, et al, “Surface Expressed HAAH in Cancer Cells is an Internalizing Antigen”, Abstract and Poster presented at the 97th Annual Meeting of AACR, Apr. 1-5, 2006, Washington, DC.
Gores, Gregory J., “Cholangiocarcinoma:preventing invasion as anti-cancer strategy”, J. of Hepatology, 38:671-673 (2003).
Lebowitz et al., “Inhibition of cancer cell proliferation, motility and invasiveness by monoclonal antibodies specific for human aspartyl (asparaginyl) β-hydroxylase (HAAH)” Abstract published for the AACR-NCI-EORTC International Conference (Oct. 29-Nov. 2, 2001 (Miami Beach, Florida).
Palumbo et al., “Human Aspartyl (Asparaginyl) β-Hydroxlase Monoclonal Antibodies: Potential Biomarkers for Pancreatic Carcinoma”, Pancreas, 25(1):39-44 (2002).
Xian et al., “Expression of aspartyl beta-hydroxylase and its clinicopathological significance in hepatocellular carcinoma”, Modern Pathology.19:280-286 (2006).
Yeung et al, “Isolation and Engineering of Biologically Active Human Single-Chain Antibody Fragments (scFv) against Human Aspartyl (Asparaginyl) β-Hydroxylase”, Abstract published for the AACR Meeting of Nov. 17-21, 2003, Boston, MA.
Boder et al., “Optimal Screening of Surface-Displayed Polypeptide Libraries,”Biotechnol. Prog., 14(1):55-62 (1998).
Boder et al., “Yeast surface display for screening combinatorial polypeptide libraries,”Nat. Biotechnol., 15(6):553-557 (1997).
Copeland et al., “Transfection by Exogenous and Endogenous Murine Retrovirus DNAs,”Cell, 16(2):347-356 (1979).
Feldhaus et al., “Flow-cytometric isolation of human antibodies from a nonimmuneSaccharomyces cerevisiaesurface display library,”Nature Biotech., 21:163-170 (2003).
Gronke et al., “Aspartyl β-hydroxylase: In vitro hydroxylation of a synthetic peptide based on the structure of the first growth factor-like domain of human factor IX,”Proc. Natl. Acad. Sci. USA, 86(10):3609-3613 (1989).
Gronke et al., “Partial Purification and Characterization of Bovine Liver Aspartyl β-Hydroxylase,”J. Biol. Chem., 265(15):8558-8565 (1990).
Jia et al., “A fully active catalytic domain of bovine aspartyl (asparaginyl) β-hydroxylase expressed inEscherichia coli: Characterization and evidence for the identification of an active-site region in vertebrate α-ketoglutarate-dependent dioxygenases,”Proc. Natl. Acad. Sci. USA, 91(15):7227-7231 (1994).
Jia et al., “cDNA Cloning and Expression of Bovine Aspartyl (Asparaginyl) β-Hydroxylase,”J. Biol. Chem., 267(20):14322-14327 (1992).
Lavaissiere et al., “Overexpression of Human Aspartyl(Asparaginyl)β-Hydroxylase in Hepatocellular Carcinoma and Cholangiocarcinoma,”J. Clin. Invest., 98(6):1313-1323 (1996).
Sepe et al., “Role of the Aspartyl-Asparaginyl-β-Hydroxylase Gene in Neuroblastoma Cell Motility,”Lab. Investig., 82(7):881-891 (2002).
Swers et al., “Shuffled antibody libraries created by in vivo homologous recombination and yeast surface diaplay,”Nucl. Acids Res., 32(3):e36 (2004).
Vaickus et al., “Immune markers in hematologic malignancies,”Crit. Rev. in Oncol./Hematol., 11:267-297 (1991).
Wang et al., “Bovine Liver Aspartyl β-Hydroxylase,”J. Biol. Chem., 266(21):14004-14010 (1991).
Zaccolo et al., “An Approach to Random Mutagenesis of DNA Using Mixtures of Triphosphate Derivatives of Nucleoside Analogues,”J. Mol. Biol., 255:589-603 (1996).
Zaccolo et al., “The Effect of High-frequency Random Mutagenesis on in Vitro Protein Evolution: A Study of TEM-1 β-Lactamase,”J. Mol. Biol., 285:775-783 (1999).
Zhang et al., “Development of a Carbon Dioxide-Capture Assay in Microtiter Plate for Aspartyl-β-hydroxylase,”Anal. Biochem., 271:137-142 (1999).
Dinchuk et al., “Aspartyl beta-hydroxylase (Asph) and an evolutionary conserved isoform of Asph missing the catalytic domain share exons with junction,” J. Biol. Chem., 275:39543-54 (2000).
Korioth et al., “Cloning and characterization of the human gene encoding aspartyyl beta-hydroxylase,” Gene, 150:395-399 (1994).
Maeda et al., “Antisense oligodeoxynucleptides directed against aspartyl (asparaginyl) beta-hydroxylase suppress migration of cholangiocarcinoma cells,” J. Hepatol., 38:615-622 (2003).
Yeung et al., “Quantitative screening of yeast surface-displayed polypeptide libraries by magnetic bead capture,” Biotechnol. Prog., 18:212-220 (2002).
Yeung, “Antibody Engineering for Cancer Therapy,” [Online thesis, retrieved from http://dspace.mit.edu/bitstream/1721.1/32325/1/61368509.pdf on Jul. 19, 2007] pp. 1-144 (2005).

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