Antibodies to mitogenic oxygenases

Details Antibodies to mitogenic oxygenases Antibodies to mitogenic oxygenases

2006-05-23

2006-05-23

Siew, Jeffrey (Department: 1642)

Drug, bio-affecting and body treating compositions

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

Structurally-modified antibody, immunoglobulin, or fragment...

C424S130100, C424S133100, C530S388100, C530S378000, C530S388800

Reexamination Certificate

active

07048923

ABSTRACT:
The present invention relates to new genes encoding for the production of novel proteins involved in generation of reactive oxygen intermediates that affect cell division. The present invention also provides vectors containing these genes, cells transfected with these vectors, antibodies raised against these novel proteins, kits for detection, localization and measurement of these genes and proteins, and methods to determine the activity of drugs to affect the activity of the proteins of the present invention.

REFERENCES:
patent: 4340535 (1982-07-01), Voisin et al.
patent: 4690914 (1987-09-01), Callut et al.
patent: 5191066 (1993-03-01), Bieniarz et al.
patent: 5585103 (1996-12-01), Raychaudhuri et al.
patent: 5593966 (1997-01-01), Malech et al.
patent: 5733748 (1998-03-01), Yu et al.
patent: 5929033 (1999-07-01), Tang et al.
patent: 5985270 (1999-11-01), Srivastava
patent: 6620603 (2003-09-01), Lambeth et al.
patent: 6858386 (2005-02-01), Macina et al.
patent: 2003/0044783 (2003-03-01), Williams et al.
patent: 2003/0109690 (2003-06-01), Ruben et al.
patent: WO 96/39419 (1996-12-01), None
patent: WO 97/42506 (1997-11-01), None
patent: WO 98/44159 (1998-08-01), None
patent: WO 98/44133 (1998-10-01), None
patent: WO 99/01020 (1999-01-01), None
patent: WO 99/24463 (1999-05-01), None
patent: WO 99/25828 (1999-05-01), None
patent: WO 99/47658 (1999-09-01), None
patent: WO 99/53051 (1999-10-01), None
patent: WO 99/55858 (1999-11-01), None
patent: WO 99/60161 (1999-11-01), None
patent: WO 99/63088 (1999-12-01), None
patent: WO 00/07632 (2000-02-01), None
patent: WO 00/12708 (2000-03-01), None
patent: WO 00/28031 (2000-05-01), None
patent: WO 00/32221 (2000-06-01), None
patent: WO 00/37643 (2000-06-01), None
patent: WO 01/96388 (2001-12-01), None
patent: WO 01/096388 (2001-12-01), None
Batot et al. Eur. J. Biochem. 1995, 234, 208-215.
Candia et al. (Int. J. Dev. Biol. 1996; 40 (6): 1179-84).
Harlow et al. teach (Antibodies, A Laboratory Manual, Chapter 5, p. 76, 1988).
Abdelrahim, M., et al., “Liquid chromatographic assay of dityrosin in human cerebrospinal fluid,” J. Chromatogr. B. Biomed. Sci. Appl., vol. 696, pp. 175-182 (1997).
Anderson, S.O., “Covalent cross-links in a structural protein, resilin,” Acta Physiol. Scand., vol. 66 Suppl. 263, pp. 1-81 (1966).
Burdon, R.H., “Superoxide and hydrogen peroxide in relation to mammalian cell proliferation,” Free Radical Biol. Med., vol. 18, No. 4, pp. 775-794 (1995).
Church, S.L., et al., “Increased managanese superoxide dismutase expression suppresses the malignant phenotype of human melanoma cells,” Proc. Natl. Acad. Sci. USA, vol. 90, pp. 3113-3117 (1993).
Emmendörffer, A., et al., “Production of oxygen radicals by fibroblasts and neutrophils from a patient with x-linked chronic granulomatous disease,” Eur. J. Haematol, vol. 51, pp. 223-227 (1993).
Fernandez-Pol, J.A., et al., “Correlation between the loss of the transformed phenotype and an increase in superoxide dismutase activity in a revertant subclone of sarcoma virus-infected mammalian cells,” Can. Res., vol. 42, pp. 609-617 (1982).
Fire, A., et al., “Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans,” Nature, vol. 391, No. 6669, pp. 806-811 (1998).
Frohman, M.A., et al., “Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer, ” Proc. Natl. Acad. Sci. USA, vol. 85, pp. 8998-9002 (1988).
Fukui, T., et al., “p22phox mRNA expression and NADPH oxidase activity are increased in aortas from hypertensive rats, ” Cir. Res., vol. 80, No. 1, pp. 45-51 (1997).
Gardner, P.R., et al., “Superoxide radical and iron modulate aconitase activity in mammalian cells,” J. Biol. Chem., vol. 270, No. 22, pp. 13399-13405 (1995).
Griendling, K. K., et al., “Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells, ” Cir. Res., vol. 74, No. 6, pp. 1141-1148 (1994).
Irani, K., et al., “Mitogenic signaling mediated by oxidants in ras-transformed fibroblasts,” Science, vol. 275, No. 5306, pp. 1649-1652 (1997).
Li, Y., et al., “Validation of lucigenin (Bis-N-methylacridinium) as a chemilumigenic probe for detecting superoxide anion radical production by enzymatic and cellular systems, ” J. Biol. Chem., vol. 273, No. 4, pp. 2015-2023 (1998).
Mastsubara, T., et al. “Increased superoxide anion release from human endothelial cells in response to cytokines,” J. Immun., vol. 137, No. 10, pp. 3295-3298 (1986).
Meier, B., et al., “Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumor necrosis factor-α, ” Biochem. J., vol. 263, No. 2, pp. 539-545 (1989).
Pagano, P. J., et al., “Localization of a constitutively active, phagocyte-like NADPH oxidase in rabbit aortic adventitia: Enhancement by angiotensin II,” Proc. Natl. Acad. Sci. USA, vol. 94, No. 26, pp. 14483-14488 (1997).
Schmidt, K. N., et al. “The roles of hyrdogen peroxide and superoxide as messengers in the activation of transcription factor NF-κB,” Chem. & Bio., vol. 2, No. 1, pp. 13-22 (1995).
Schreck, R., et al., “Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1, ” EMBO J., vol. 10, No. 8, pp. 2247-2258 (1991).
Suh, Y., et al., “Cell transformation by the superoxide-generating oxidase Mox1, ” Nature, vol. 401, No. 6748, pp. 79-82 (1999).
Sundaresan, M., et al., “Requirement for generation of H2O2for platelet-derived growth factor signal transduction,” Science, vol. 270, pp. 296-299 (1995).
Szatroski, T.P., et al., “Production of large amounts of hydrogen peroxide by human tumor cells,” Canc. Res., vol. 51, No. 3, pp. 794-798 (1991).
Uhlinger, D.J., “Nucleoside triphosphate requirements for superoxide generation and phosphorylation in a cell-free system from human neutrophils,” vol. 266, No. 31, pp. 20990-20997 (1991).
Ushio-Fukai M., et al., “p22phoxis a critical component of the superoxide-generating NADH/NADPH oxidase system and regulates angiotensin II-induced hypertrophy in vascular smooth muscle cells,” J. Biol. Chem., vol. 271, No. 38, pp. 23317-23321 (1996).
Yan, T., et al., “Manganese-containing superoxide dismutase overexpression causes phenotypic reversion in SV40-transformed human lung fibroblasts,” Canc. Res., vol. 56, pp. 2864-2871 (1996).
Yu, L., et al., Biosynthesis of the phagocyte NADPH oxidase cytochrome b558, J. Biol. Chem., vol. 272, No. 43, pp. 27288-27294 (1997).
U.S. Appl. No. 60/086,266, filed May 21, 1998, Macina et al.
Adams, M.D., et al., EMBL Accession No. AA305700, Mar. 8, 2000.
Adams, M.D., et al., EMBL Accession No. AA305700, Apr. 18, 1997.
Arbiser, Jack L., et al., “Reactive Oxygen Generated by Nox1 Triggers the Angiogenic Switch, ”PNAS, vol. 99, No. 2, pp 715-720, Jan. 22, 2002.
Banfi, Botond, et al., “A Mammalian H+Channel Generated Through Alternative Splicing of the NADPH Oxidase HomologNOH-1,” Science, vol. 287, pp 138-142, Jan. 7, 2000.
Bayraktutan, Ulvi, et al., “Molecular Characterization and Localization of the NAD(P)H Oxidase Components gp91-phoxand p22-phoxin Endothelial Cells,”Arterioscler Thromb Vasc Biol., vol. 20, pp 1903-1911, Aug. 2000.
Davis, A. R., et al., Genbank Accession No. 046522, May 30, 2000.
Dupuy, C., et al., EMBL Accession No. AF181972, Dec. 29, 1999.
Dupy, Corinne et al., “Purifucation of a Novel Flavoprotein Involved in the Thyroid NADPH Oxidase —Cloning of the Porcine and Human cDNAs, ”The Journal of Biological Chemistry, vol. 274, No. 52, pp 37265-37269, 1999.
Griffin, Thomas W., et al., “Initial Clinical Study of Indium-111-Labeled Clone 110 Anticarcinoembryonic Antigen Antibody in Patients with Colore

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