Recombinant human T2 RNase and uses thereof

Details Recombinant human T2 RNase and uses thereof Recombinant human T2 RNase and uses thereof

2005-09-28

2011-10-18

Ramirez, Delia (Department: 1652)

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Hydrolase

C424S094600, C435S199000, C435S019000, C530S350000

Reexamination Certificate

active

08039240

ABSTRACT:
The cloning and heterologous expression of human T2 RNase6PL are disclosed. Further disclosed are methods for preventing, inhibiting and/or reversing cell motility, actin filament assembly or disassembly, proliferation, colonization, differentiation, accumulation and/or development of abnormal cells in a subject is disclosed. The methods are effected by administering to the subject a therapeutically effective amount of a RNase6PL ribonuclease or close homologues thereof.

REFERENCES:
patent: 3791932 (1974-02-01), Schuurs et al.
patent: 3839153 (1974-10-01), Schuurs et al.
patent: 3850578 (1974-11-01), McConnell
patent: 3850752 (1974-11-01), Schuurs et al.
patent: 3853987 (1974-12-01), Dreyer
patent: 3867517 (1975-02-01), Ling
patent: 3879262 (1975-04-01), Schuurs et al.
patent: 3901654 (1975-08-01), Gross
patent: 3935074 (1976-01-01), Rubenstein et al.
patent: 3984533 (1976-10-01), Uzgiris
patent: 3996345 (1976-12-01), Ullman et al.
patent: 4034074 (1977-07-01), Miles
patent: 4098876 (1978-07-01), Piasio et al.
patent: 4879219 (1989-11-01), Wands et al.
patent: 5011771 (1991-04-01), Bellet et al.
patent: 5281521 (1994-01-01), Trojanowski et al.
patent: 5786457 (1998-07-01), Nett et al.
patent: 6590075 (2003-07-01), Ruben et al.
patent: 7101839 (2006-09-01), Roiz et al.
patent: 2005/0113327 (2005-05-01), Roiz et al.
patent: 2008/0013419 (2008-01-01), Lee et al.
patent: 769011 (2001-03-01), None
patent: 1207755 (2002-05-01), None
patent: WO 99/33981 (1999-07-01), None
patent: WO 01/15531 (2001-08-01), None
Smirnoff et al., Cancer 107(12):2760-2769; 2006.
Garret et al., European Journal of Cancer 35(14):2010-2030, 1999.
Deshpande et al., Critical Reviews in Microbiology 28(2):79-122, 2002.
Branden et al. , Introduction to Protein Structure, Garland Publishing Inc., New York, p. 247, 1991.
Seffernick et al., J. Bacteriol. 183(8):2405-2410, 2001.
Witkowski et al, Biochemistry 38:11643-11650, 1999.
Guo et al., PNAS 101(25):9205-9210, 2004.
Trubia et al., GenBank accession No. NP—003721, Jun. 28, 1999.
Roiz et al. “Stigmatic RNase in Self-Compatible Peach (Prunus persica)”, International Journal of Plant Sciences, 156:(1): 37-41, 1995.
Zhu et al. “Escherichia coliRNA Gene Encoding RNase I: Cloning, Overexpression, Subcellular Distribution of the Enzyme, and Use of an RNA Deletion to Identify Additional RNases”, Journal of Bacteriology, 172(6): 3146-3151, 1990.
Ye et al. “Isolation and Characterization of cDNAs Encoding Zylogenesis-Associated and Wounding-Induced Ribonucleases inZinnia elegans”, Plant Molecular Biology, 30: 697-709, 1996.
Irie et al. “Role of Histidine 46 in the Hydrolysis and the Reverse Transphosphorylation Reaction of RNase Rh FromRhizopus niveus”, Journal of Biochemistry, 121: 849-853, 1997.
Laemmli “Relevant Page on Gel Electrophoresis”, Nature, 227: 681, 1970. Abstract.
Broothaerts et al. “Petunia Hybrida S-Proteins: Ribonuclease Activity and the Role of Their Glycan Side Chains in Self-Incompatibility”, Sexual Plant Reproduction, 4: 258-266, 1991.
Bradford “A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding”, Analytical Biochemistry, 72: 248-254, 1976.
Yokota et al. “Isolation and Characterization of Plant Myosin From Pollen Tubes of Lily”, Protoplasma, 177: 153-162, 1994.
Lin et al. “Characterization of the Mechanism of Cellular and Cell Free Protein Synthesis Inhibition by an Anti-Tumor Ribonuclease”, Biochemical and Biophysical Research Communications, 204(1): 156-162, 1994.
Brown et al. “Barley Aleurone Layers Secrete a Nuclease in Response to Gibberellic Acid”, Plant Physiology, 82: 801-806, 1986.
Heslop-Harrison et al. “Dynamic Aspects of Apical Zonation in the Angiosperm Pollen Tube”, Sexual Plant Reproduction, 3: 187-194, 1990.
Irie et al. “Site of Alkylation of the Major Ribonuclease FromAspergillus saitoiWith Lodoacetate”, Journal of Biochemistry, 99(3): 627-633, 1986.
Simm et al. “On the Interaction of Bovine Seminal Rnase With Actin in Vitro”, European Journal of Biochemistry, 166: 49-54, 1987.
Kawata et al. “Amino-Acid Sequence of Ribonuclease T2 FromAspergillus oryzae”, European Journal of Biochemistry, 176: 683-697, 1988. p. 688, Claims 15, 20.
Ohgi et al. “Expression of Rnase Rh FromRhizopus niveusin Yeast and Characterization of the Secreted Proteins”, Journal of Biochemistry, 109: 776-785, 1991. p. 777, Claims 21, 26.
Irie et al. “Structure-Function Relationships of Acid Ribonucleases: Lysosomal, Vacuolar and Periplasmic Enzymes”, Pharmacological Therapy, 81(2): 77-89, 1999. p. 79, Claims 15, 20.
Roiz et al. “Characterization ofAspergillus nigerB-1 RNase and Its Inhibitory Effect on Pollen Germination and Pollen Tube Growth in Selected Tree Fruit”, Journal of the American Society of Horticulture Sciences, 125(1): 9-14, 2000. Abstract.
Nomachi et al. “Purification and Some Properties of 2 Acid RNase Fractions EC-3.1.27.1 EC-3.1.27.3 From the Mycelia ofAspergillus niger”, Journal of General and Applied Microbiology, 26(6): 375-386, 1980.
Hu et al. “Technology to Obtain Sustained Release Characteristics of Drugs After Delivered to the Colon”, Journal of Drug Targeting, 6(6): 439-448, 1999. Abstract.
Ishibashi et al. “Evaluation of Colonic Absorbability of Drugs in Dogs Using a Novel Colon-Targeted Delivery Capsule (CTDC)”, Journal of Control Release, 59(3): 361-376, 1999. Abstract.
Matsuda et al. “Effect of Food Intake on the Delivery of Fluorescein as a Model Drug in Colon Delivery Capsule After Oral Administration to Beagle Dogs”, Journal of Drug Targeting, 4(2): 59-67, 1996. Abstract.
Takaya et al. “Development of a Colon Delivery Capsule and the Pharmacological Activity of Recombinant Human Granulocyte Colony-Stimulating Factor (RhG-CSF) in Beagle Dogs”, Journal of Pharmacy and Pharmacology, 47(6):474-478, 1995. Abstract.
Tozaki et al. “Chitosan Capsules for Colon-Specific Drug Delivery: Improvement of Insulin Absorption From the Rat Colon”, Journal of Pharmaceutical Sciences, 86(9): 1016-1021, 1997. Abstract.
Tozaki et al. “Colon-Specific Delivery of R68070, A New Thromboxane Synthase Inhibitor, Using Chitosan Capsules: Therapeutic Effects Against 2,4,6-Trinitrobenzene Sulfonic Acid-Induced Ulcerative Colitis in Rats”, Life Science, 64(13): 1155-1162, 1999. Abstract.
Hu et al. “An Angiogenin-Binding Protein From Endothelial Cells”, Proc. Natl. Acad. Sci. USA, 88: 2227-2231, 1991.
Hu et al. “Actin Is a Binding for Angiogenin”, Proc. Natl. Acad. Sci. USA, 90: 1217-1221, 1993.
Kao et al. “A Small-Molecule Inhibitor of the Ribonucleolytic Activity of Human Angiogenin That Possesses Antitumor Activity”, Proc. Natl. Acad. Sci. USA, 99: 10066-10071, 2002.
Eck et al. “Gene-Based Therapy”, Goodman & Gilman's The Pharmacological Basis of Therapeutics, 9(Chap.5): 77-101, 1996.
Rudinger “Characteristics of the Amino Acids as Components of a Peptide Hormone Sequence”, University Park Press, Baltimore, p. 1-7, 1976.
Kaye et al. “A Single Amino Acid Substitution Results in a Retinoblastoma Protein Defective in Phosphorylation and Oncoprotein Binding”, Proc. Natl. Acad. Sci. USA, 87: 6922-6926, 1990.
Skolnick et al. “From Genes to Protein Structure and Function: Novel Applications of Computational Approaches in the Genomic Era”, Trends in Biotechnology (TIBTECH), 18: 34-39, 2000.
Kawata et al. “Identification of Two Essential Histidine Residues of RNase T-2 FromAspergillus oryzae”, European Journal of Biochemistry, 187(1): 255-262, 1990.
Roiz et al. “Stigmatic Rnase in Calamondin (Citrus reticulataVar. Austera x Fortunella Sp.)”, Physiologia Plantarum, 94: 585-590, 1995.
Laccetti et al. “Seminal Ribonuclea

Affiliated with

Also associated with

Rating

Recombinant human T2 RNase and uses thereof does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Recombinant human T2 RNase and uses thereof, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Recombinant human T2 RNase and uses thereof will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-4257413