Mitogenic oxygenase regulators

Details Mitogenic oxygenase regulators Mitogenic oxygenase regulators

2007-04-10

2007-04-10

Nashed, Nashaat T. (Department: 1656)

Chemistry: molecular biology and microbiology

Measuring or testing process involving enzymes or...

Involving oxidoreductase

C435S168000, C435S189000

Reexamination Certificate

active

10850060

ABSTRACT:
The present invention relates to new genes encoding for the production of novel nox enzyme 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: 2002/0022022 (2002-02-01), Shi et al.
patent: WO 00/28031 (2000-05-01), None
patent: WO 01/53312 (2001-07-01), None
patent: WO 01/79467 (2001-10-01), None
Banfi, B. et al. “A Ca(2+)-Activated NADPH Oxidase in Testis, Spleen, and Lymph Nodes”, Journal of Biological Chemistry, United States, Oct. 5, 2001, vol. 276, No. 40, pp. 37594-37601.
Biberstine-Kinkade, K., et al., “Mutagenesis of an Arginine- and Lysine-rich Domain in the gp91phoxSubunit of the Phagocyte NADPH-oxidase Flavocytochrome b558,”J. Biol. Chem.,vol. 274, No. 15, pp. 10451-10457 (1999).
Bjiorgvinsdottir et al., “Cloning of murine gp91 (phox) and functional expression in a human X-liked . . . ” Blood, 87 (5), 2005-2010 (1996).
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).
Cheng Guangjie et al. Homologs of Gp91phox: Cloning and Tissue Expression of Nox3, Nox4 and Nox5, Gene (Amsterdam), vol. 269, No. 1-2, 23001, pp. 131-140.
Church, S. L., et al., “Increased Manganese 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).
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).
Geiszt, M., et al., “Identification of Renox, an NAD(P)H Oxidase in Kidney,”PNAS, vol. 97, No. 14, pp. 8010-8014 (2000).
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).
Isogai, Y., “Superoxide-producing Cytochrome b: Enzymatic and Electron Paramagnetic Resonance Properties of Cytochrome b558Purified from Neutrophhils,”J. Biol. Chem.,vol. 268, No. 6, pp. 4025-4031 (1993).
Kikuchi, H. et al., “NADPH Oxidase Subunit, pg91phoxHomologue, Preferentially Expressed in Human Colon Epithelial Cells,”Gene,vol. 254, pp. 237-243 (2000).
Lambeth, J.D., et al., “Novel Homologs of gp91phox,” Trends in Biochemical Sciences,vol. 25, pp. 459-461 (2000).
Lambeth, J.D., “Regulation of the Phagocyte Respiratory Burst Oxidase by Protein Interactions,”Journal of Biochemistry and Molecular Biology,vol. 33, No. 6, pp. 427-439 (2000).
Lloyd, D., “Human DNA Sequence from Clone 146H21 on Chromosome Xq22”, Jan. 10, 1997.
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 on Interleukin-1 or Tumor Necrosis Factor-α,”Biochem. J.,vol. 263, No. 2, pp. 539-545 (1989).
Merta, A. et al., “The Rat S-Adenosylhomocysteine Hydrolase Promoter”, Biochemical and Biophysical Research Communications, United States, Nov. 26, 1997, vol. 240, No. 3, pp. 580-585.
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).
Pepe, G.J. et al. “Cloning of the 11Beta Hydroxysteroid Dehydrogenase (11Beta-HSD)-2 Gene in the Baboon: Effects of Estradiol on Promoter Activity of 11Beta-HSD-1 and -2 in Placental JEG-3 Cells”, U.S. National Library of Medicine, Jan. 18, 1999.
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).
Shiose, A., et al., “A Novel Superoxidases-producing NAD(P)H Oxidase in Kidney”,J. Biol. Chem.,vol. 276, No. 2, pp. 1417-1423 (2001).
Suh, Y., et al., “Cell Transformation by the Superoxide-Generating Oxidase Mox1,”Nature,vol. 401, No. 6748, pp. 79-82 (1999).
Sudaresan, 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,”J. Biol. Chem.,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-Inducted 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 Pheontypic 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 b588: Role of Heme Incorporation and Heterodimer Formation in Maturation and Stability of gp91phoxand p22phoxSubunits,”J. Biol. Chem,vol. 272, No. 43, pp. 27288-27294 (1997).
Geiszt et al., GenBank Accession No. AF261944, Jul. 25, 2000.
Cheng et al.., GenBank Accession No. AF254621, May 9, 2000.
da Silva et al., GenBank Accession No. AAM40338, May 23, 2002 (SWISSPROT online Oct. 22, 2001).
da Silva et al., GenBank Accession No. AAM403389, May 23, 2002 (SWISSPROT online Oct. 22, 2001).
Hillier et al., GenBank Accession No. AA159494, Dec. 16, 1996 (EMBL online Oct. 22, 2001).
Geiszt et al., EMBL-EBI Accession No. AF261943 (EMBL Online Sep. 21, 2006).
Kawabata et al., NCBI Accession No. BAB15319 (NCBI Online Sep. 21, 2006).
Kawahara et al., EMBL-EBA Database Accession No. AF317889 (EMBL Online Sep. 21, 2006).
Lambeth and Cheng, NCBI Accession No. AAG33638 (NCBI Online Sep. 21, 2006).
Sugano et al., EMBL-EBI Database Accession No. AK026011 (EMBL Online Sep. 21, 2006).

Affiliated with

Also associated with

Rating

Mitogenic oxygenase regulators 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 oxygenase regulators, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Mitogenic oxygenase regulators will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3756820