Human proteases and polynucleotides encoding the same

Details Human proteases and polynucleotides encoding the same Human proteases and polynucleotides encoding the same

2002-07-22

2004-08-17

Saidha, Tekchand (Department: 1652)

Chemistry: molecular biology and microbiology

Micro-organism, per se ; compositions thereof; proces of...

Bacteria or actinomycetales; media therefor

C435S320100, C435S212000, C536S023200

Reexamination Certificate

active

06777221

ABSTRACT:

1. INTRODUCTION
The present invention relates to the discovery, identification, and characterization of novel human polynucleotides encoding proteins that share sequence similarity with animal proteases. The invention encompasses the described polynucleotides, host cell expression systems, the encoded proteins, fusion proteins, polypeptides and peptides, antibodies to the encoded proteins and peptides, and genetically engineered animals that either lack or over express the disclosed genes, antagonists and agonists of the proteins, and other compounds that modulate the expression or activity of the proteins encoded by the disclosed genes that can be used for diagnosis, drug screening, clinical trial monitoring and the treatment of physiological disorders.
2. BACKGROUND OF THE INVENTION
Proteases are enzymes that cleave polypeptide sequences. In particular, carboxypeptidases hydrolyze the peptide bonds at the carboxy-terminal end of an amino acid chain, and have been identified in a wide variety of cells and animals. Peptidases have been implicated in a wide variety of cellular functions including, but not limited to, digestion, coagulation, diabetes, prostate cancer, gynecological disorders, neurological disorders, and obesity. Accordingly, peptidases represent key targets/players for the regulation of a variety of physiological processes and pathways.
3. SUMMARY OF THE INVENTION
The present invention relates to the discovery, identification, and characterization of nucleotides that encode novel human proteins, and the corresponding amino acid sequences of these proteins. The novel human proteins (NHPs) described for the first time herein share structural similarity with animal proteases, and especially carboxypeptidases. As such, the described NHPs represent a new family of protease-related proteins with a range of homologues and orthologs that transcend phyla and a broad range of species.
The novel human nucleic acid sequences described herein, encode proteins/open reading frames (ORFs) of 351, 314, 436, 399, 351, 314, and 69 amino acids in length (see SEQ ID NOS: 2, 4, 6, 8, 10, 12 and 14 respectively).
The invention also encompasses agonists and antagonists of the described NHPs, including small molecules, large molecules, mutant NHPs, or portions thereof, that compete with native NHP, peptides, and antibodies, as well as nucleotide sequences that can be used to inhibit the expression of the described NHPs (e.g., antisense and ribozyme molecules, and gene or regulatory sequence replacement constructs) or to enhance the expression of the described NHP genes (e.g., expression constructs that place the described gene under the control of a strong promoter system), and transgenic animals that express a NHP transgene, or “knock-outs” (which can be conditional) that do not express a functional NHP.
Further, the present invention also relates to processes of identifying compounds that modulate, i.e., act as agonists or antagonists, of NHP expression and/or NHP product activity that utilize purified preparations of the described NHPs and/or NHP product, or cells expressing the same. Such compounds can be used as therapeutic agents for the treatment of any of a wide variety of symptoms associated with biological disorders or imbalances.
4. DESCRIPTION OF THE SEQUENCE LISTING AND FIGURES
The Sequence Listing provides the sequences of several protease ORFs that encode the described NHP amino acid sequences.


REFERENCES:
patent: 4215051 (1980-07-01), Schroeder et al.
patent: 4376110 (1983-03-01), David et al.
patent: 4594595 (1986-06-01), Struckman
patent: 4946778 (1990-08-01), Ladner et al.
patent: 5459127 (1995-10-01), Felgner et al.
patent: 5474901 (1995-12-01), Drayna et al.
patent: 5593674 (1997-01-01), Drayna et al.
patent: 5837458 (1998-11-01), Minshull et al.
patent: 5869336 (1999-02-01), Meyer et al.
patent: 5877397 (1999-03-01), Lonberg et al.
patent: 5948767 (1999-09-01), Scheule et al.
patent: 6075181 (2000-06-01), Kucherlapati et al.
patent: 6110490 (2000-08-01), Thierry
Bird et al, 1988, “Single-Chain Antigen-Binding Proteins”, Science 242:423-426.
Bitter et al, 1987, “Expression and Secretion Vectors for Yeast”, Methods in Enzymology 153:516-544.
Colbere-Garapin et al, 1981, “A New Dominant Hybrid Selective Marker for Higher Eukaryotic Cells”, J. Mol. Biol. 150:1-14.
Gautier et al, 1987, “&agr;-DNA IV:&agr;-anomeric and &bgr;-anomeric tetrathymidylates covalently linked to intercalating oxazolopyridocarbazole. Synthesis, physiochemical properties and poly (rA) binding”, Nucleic Acids Research 15(16):6625-6641.
Greenspan et al, 1993, “Idiotypes: structure and immunogenicity”, FASEB Journal 7:437-444.
Huse et al, 1989, “Generation of a Large Combinatorial Library of the Immunoglobulin Repertoire in Phage Lambda”, Science 246:1275-1281.
Huston et al, 1988, “Protein engineering of antibody binding sites: Recovery of specific activity in an anti-digoxin single-chain Fv analogue produced inEscherichia coli”, Proc. Natl. Acad. Sci. USA 85:5879-5883.
Inoue et al, 1987, “Sequence-dependent hydrolysis of RNA using modified oligonucleotide splints and R Nase H”, FEBS Letters 215(2):327-330.
Inoue et al, 1987, “Synthesis and hybridization studies on two complementary nona(2′-O-methyl)ribonucleotides”, Nucleic Acids Research 15(15):6131-6149.
Inouye & Inouye, 1985, “Up-promoter mutations in the Ipp gene ofEscherichia coli”, Nucleic Acids Research 13(9):3101-3110.
Janknecht et al, 1991, “Rapid and efficient purification of native histidine-tagged protein expressed by recombinant vaccinia virus”, PNAS USA 88:8972-8976.
Kohler & Milstein, 1975, “Continuous cultures of fused cells secreting antibody of predefined specificity”, Nature 256:495-497.
Logan et al, 1984, “Adenovirus tripartite leader sequence enhances translation of mRNAs late after infection”, Proc. Natl. Acad. Sci. USA 81:3655-3659.
Lowy et al, 1980, “Isolation of Transforming DNA: Cloning the Hamster aprt Gene”, Cell 22:817-823.
Morrison et al, 1984, “Chimeric human antibody molecules: Mouse antigen-binding domains with human constant region domains”, Proc. Natl. Acad. Sci. USA 81:6851-6855.
Mulligan & Berg. 1981, “Selection for animal cells that express theEscherichia collgene coding for xanthine-guanine phosphoribosyltransferase”, Proc. Natl. Acad. Sci. USA 78(4):2072-2078.
Nauberger et al, 1984, “Recombinant antibodies possessing novel effector functions”, Nature 312:604-608.
Nisonoff, 1991, “Idiotypes: Concepts and Applications”, J. of Immunology 147:2429-2438.
O'Hare et al, 1981, “Transformation of mouse fibroblasts to methotrexate resistance by a recombinant plasmid expressing a prokaryotic dihydrololate reductase”, Proc. Natl. Acad. Sci. USA 78(3):1527-1531.
Ruther et al, 1983, “Easy identification of cDNA clones”, EMBO Journal 2(10):1791-1794.
Santerre et al, 1984, “Expression of prokaryotic genes for hygromycin B and G418 resistance as dominant-selection markers in mouse L cells”, Gene 30:147-156.
Sarin et al, 1988, “Inhibition of acquired immunodeficiency syndrome virus by oligodeoxynucleoside methylphosphonates”, Proc. Natl. Acad. Sci. USA 85:7448-7451.
Smith et al, 1983, “Molecular Engineering of the Autographa californica Nuclear Polyhedrosis Virus Genome: Deletion Mutations within the Polyhedrin Gene”, J. Virol. 46(2):584-593.
Stein et al, 1988, “Physiochemical properties of phosphorothioate oligodeoxynucleotides”, Nucleic Acids Research 16(8):3209-3221.
Szybalska & Szybalski, 1962, “Genetics of Human Cell Lines, IV. DNA-Mediated Heritable Transformation of a Biochemical Trait”, Proc. Natl. Acad. Sci. USA 48:2026-2034.
Takeda et al, 1985, “Construction of chimaeric processed immunoglobulin genes containing mouse variable and human constant region sequences”, Nature 314:452-454.
Van Heeke et al, 1989, “Expression of Human Asparagine Synthetase inEscherichia coli”, J. Biol. Chemistry 264(10):5503-5509.
Ward et al, 1989, “Binding activities of a repertoire of single immunoglobulin variable domains secreted fromEscherichia coli”, Nature 341:544-546.
Wigler et al, 1980, “Transformation of mammalian cel

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