Chemistry: molecular biology and microbiology – Animal cell – per se ; composition thereof; process of...
Reexamination Certificate
2006-05-16
2006-05-16
Slobodyansky, Elizabeth (Department: 1652)
Chemistry: molecular biology and microbiology
Animal cell, per se ; composition thereof; process of...
C435S189000, C435S192000, C435S252300, C435S320100, C536S023200
Reexamination Certificate
active
07045351
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: 4690914 (1987-09-01), Callut 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 99/60161 (1999-11-01), None
Edens et al. (2001) J. Cell Biology, vol. 154(4), pp. 879-891.
U.S. Appl. No. 60/086,266, filed May 21, 1998, Macina et al.
International Search Report dated Aug. 16, 2000 for PCT/US 99/26592.
Li, F. et al.: “CD34+Peripheral Blood Progenitors as a Target for Genetic Correction of the Two Flavocytochrome B558 Defective Forms of Chronic Granulomatous Disease,” Blood, US, W.B. Saunders, Philadelphia, VA, vol. 84, No. 1, Jul. 1, 1994, pp. 53-58, XP000674233 ISSN: 0006-4971, p. 54, col. 2, figures 1, 2.
Strausberg et al., “National cancer institute, cancer genome anatomy project (CGAP),” EMBL Database Acc No.: AA493362, Jun. 28, 1997, XP002137597.
Lloyd: “Human DNA sequence from clone 146h21 on chromosome Xq22,” EMBL Database Acc No.: Z83819, Jan. 10, 1997, XP002137598.
Adams et al.: “Initial assessment of human gene diversity and expression patterns based upon 83 million basepairs of cDNA sequence,” EMBL Database Acc No.: AA305700, Apr. 18, 1997, XP002137621 cited in the application.
Palmer: “Human DNA sequence from clone 257I9 on chromosome 6q25.1-26 contains gene similar to Cytochrome B, CA repeat, GSS” EMBL Database Acc. No.: AL031773, Sep. 29, 1998, XP002144975.
Hillier et al.: “Generation and analysis of 280,000 human expressed sequence tags,” EMBL Database Acc. No.: W52750, Jun. 4, 1996, XP002144976.
Strausberg: “National cancer institute, cancer genome anatomy project (CGAP)” EMBL Database Acc. No.: AA641653, Nov. 1, 1997, XP002144977.
Wilson et al.: “f53g12.3” EMBL Database Acc. No.: AF003139, Jul. 1, 1997, XP002144978, abstract.
Suh et al.: “Cell transformation by the superoxide-generating oxidase Mox1” Nature, vol. 401, Sep. 2, 1999, pp. 79-82, XP002137599.
Dupuy et al.: “Purification of a novel flavoprotein involved in the thyroid NADPH oxidase,” The Journal of Biological Chemistry, vol. 274, No. 52, Dec. 24, 1999, pp. 37265-37269, XP002144979.
Dupuy et al.: EMBL Database Acc. No.: AF181972, Dec. 29, 1999, XP002144980.
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 hydrogen 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).
Szatrowski, 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).
Zhou et al., “Interleukin-4 Suppresses the Expression of Macrophage NADPH Oxidase Heavy Chain Subunit (gp91-phox),”Biochimica et Biophysica Acta,
Arnold Rebecca S.
Cheng Guangie
Griendling Kathy K.
Lambeth J. David
Lassegue Bernard P.
Emory University
Klarquist & Sparkman, LLP
Slobodyansky Elizabeth
LandOfFree
Mitogenic oxygenases does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Mitogenic oxygenases, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Mitogenic oxygenases will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3612995