Metalloprotease highly expressed in the testis, MMP-29

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues

Reexamination Certificate

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Reexamination Certificate

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11313356

ABSTRACT:
The present invention provides novel polynucleotides encoding MMP-29 polypeptides, fragments and homologues thereof. Also provided are vectors, host cells, antibodies, and recombinant and synthetic methods for producing said polypeptides. The invention further relates to diagnostic and therapeutic methods for applying these novel MMP-29 polypeptides to the diagnosis, treatment, and/or prevention of various diseases and/or disorders related to these polypeptides. The invention further relates to screening methods for identifying agonists and antagonists of the polynucleotides and polypeptides of the present invention.

REFERENCES:
patent: 2003/0235581 (2003-12-01), Pieczenik
patent: 2369363 (2002-05-01), None
patent: WO 00/12708 (2000-03-01), None
patent: WO0179454 (2001-10-01), None
patent: WO0183782 (2001-11-01), None
patent: WO0198468 (2001-12-01), None
patent: WO 03/054178 (2003-07-01), None
NCBI Entrez Accession No. gi|17453852, NCBI Annotation Project, Aug. 1, 2002.
NCBI Entrez Accession No. gi|21693575, Marchenko, G.N. et al., Jul. 4, 2002.
NCBI Entrez Accession No. gi|21928002, Marchenko, G.N. et al., Jul. 22, 2002.
NCBI Entrez Accession No. gi|22218341, Brinckerhoff, C.E. et al., Oct. 22, 2002.
Brinckerhoff, C.E. et al., “Matrix metalloproteinases: a tail of a frog that became a prince”, Nature Reviews, Molecular Cell Biology, vol. 3 (3), pp. 207-214 (2002).
Marchenko, G.N. et al., “MMP-28, a new human matrix metalloproteinase with an unusual cysteine-switch sequence is widely expressed in tumors”, Gene, vol. 265 (1-2), pp. 87-93 (2001).
Pieczenik, G. “Are the universes of antibodies and antigens symmetrical?”, Reproductive BioMedicine, vol. 6, pp. 154-156 (2003).
Swiss -Prot/Trembl Accession No.: Q8N119, Oct. 2002.
Ahokas, et al., “Matrix metalloproteinase-21, the human orthologue for XMMP, is expressed during fetal development and in cancer”, Gene, vol. 301, pp. 31-41 (2002).
Marchenko, et al. “MMP-28, a new human matrix metalloproteinase with an unusual cysteine-switch sequence is widely expressed in tumors”, Gene, vol. 265, pp. 87-93 (2001).
NCBI Entrez Accession No. 1FBL (gi:1310872), Lloyd, L.F. et al., Sep. 4, 1998.
NCBI Entrez Accession No. 1SLM (gi:1942848), Marcy, A.I. et al., Aug. 3, 1995.
NCBI Entrez Accession No. AAC21447 (gi:3211705), Yang, M. et al., Jun. 10, 1998.
NCBI Entrez Accession No. AAG33131 (gi:11228711), Llano, E. et al., Nov. 20, 2000.
NCBI Entrez Accession No. AAM92903 (gi:22134532), Ahokas, K. et al., Dec. 20, 2002.
NCBI Entrez Accession No. AC012488 (gi:16756328), Sulston, J.E. et al., Nov. 7, 2001.
NCBI Entrez Accession No. AC013468 (gi:13493155), Sulston, J.E. et al., Nov. 7, 2001.
NCBI Entrez Accession No. AC023065 (gi:7684439), Birren, B. et al., May 3, 2000.
NCBI Entrez Accession No. AF331526 (gi:22134531), Ahokas, K. et al., Dec. 20, 2002.
NCBI Entrez Accession No. AF520613 (gi:21693574), Marchenko, G.N. et al., Jul. 4, 2002.
NCBI Entrez Accession No. AL158835 (gi:16416159), Tromans, A., Oct. 23, 2001.
NCBI Entrez Accession No. AL360176 (gi:15391100), Williams, S., Aug. 30, 2001.
NCBI Entrez Accession No. AW665196 (gi:7457742), Apr. 6, 2000.
NCBI Entrez Accession No. BG234242 (gi:12748089), Feb. 12, 2001.
NCBI Entrez Accession No. NP—671724 (gi:22218341), Shagisultanova, E.I. et al., Oct. 27, 2004.
Swiss-Prot Accession No. Q10739, Release 34, Oct. 1996.
Swiss-Prot Accession No. Q9NPA2, Release 40, Oct. 2001.
Swiss-Prot Accession No. Q9ULZ9, Release 40, Oct. 2001.
Adams, M.D. et al., “The Genome Sequence ofDrosophila melanogaster”, Science, vol. 287, pp. 2185-2195 (2000).
Altschul, S.F. et al., “Basic Local Alignment Search Tool”, J. Mol. Biol., vol. 215, pp. 403-410 (1990).
Arnold, D. et al., “Substrate specificity of cathepsins D and E determined by N-terminal and C-terminal sequencing of peptide pools”, Eur. J. Biochem., vol. 249, pp. 171-179 (1997).
Backes, B.J. et al., “Synthesis of positional-scanning libraries of fluorogenic peptide substrates to define the extended substrate specificity of plasmin and thrombin”, Nature Biotechnology, vol. 18, pp. 187-193 (2000).
Balasubramanian, N. et al., “Active Site-Directed Synthetic Thrombin Inhibitors: Synthesis, in Vitro and in Vivo Activity Profile of BMY 44621 and Analogs. An Examination of the Role of the Amino Group in the D-Phe-Pro-Arg-H Series”, J. Med. Chem., vol. 36, No. 2, pp. 300-303 (1993).
Bartlett, P.A. et al., “CAVEAT: A Program to Facilitate the Structure-derived Design of Biologically Active Molecules”, Molecular Recognition: Chemical and Biochemical Problems, The Proceedings of an International Symposium, University of Exeter, Special Publication No. 78, The Royal Society of Chemistry, publ., Roberts, S.M., ed., pp. 182-196 (1989).
Bateman, A. et al., “The Pfam Protein Families Database”, Nucleic Acids Research, vol. 28, No. 1, pp. 263-266 (2000).
Becker, J.W. et al., “Stromelysin-1: Three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme”, Protein Science, vol. 4, pp. 1966-1976 (1995).
Bernstein, F.C. et al., “The Protein Data Bank: A Computer-based Archival File for Macromolecular Structures”, J. Mol. Biol., vol. 112, pp. 535-542 (1977).
Biemond, B.J. et al., “Thrombolysis and Reocclusion in Experimental Jugular Vein and Coronary Artery Thrombosis: Effects of a Plasminogen Activator Inhibitor Type 1-Neutralizing Monoclonal Antibody”, Circulation, vol. 91, No. 4, pp. 1175-1181 (1995).
Birney, E. et al., “Using GeneWise in theDrosophilaAnnotation Experiment”, Genome Research, vol. 10, pp. 547-548 (2000).
Blinder, M.A. et al., “Heparin Cofactor IIOslo: Mutation of ARG-189 to His Decreases the Affinity for Dermatan Sulfate”, The Journal of Biological Chemistry, vol. 264, No. 9, pp. 5128-5133 (1989).
Blinder, M.A. et al., “Site-directed Mutagenesis of Arginine 103 and Lysine 185 in the Proposed Glycosaminoglycan-binding Site of Heparin Cofactor II”, The Journal of Biological Chemistry, vol. 265, No. 1, pp. 286-291 (1990).
Bode, W. et al., “Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the ‘metzincins’”, FEBS Letters, vol. 331, No. 1,2, pp. 134-140 (1993).
Bode, W. et al., “The metzincins: A superfamily of structurally related metalloproteinases”, Zoology, vol. 99, No. 4, pp. 237-246 (1996).
Böhm, H.-J., “The computer program LUDI: A new method for the de novo design of enzyme inhibitors”, Journal of Computer-Aided Molecular Design, vol. 6, pp. 61-78 (1992).
Cardozo, T. et al., “Homology Modeling by the ICM Method”, Proteins: Structure, Function, and Genetics, vol. 23, pp. 403-414 (1995).
Cerretti, D.P. et al., “Isolation of Two Novel Metalloproteinase-Disintegrin (ADAM) cDNAs That Show Testis-Specific Gene Expression”, Biochemical and Biophysical Research Communications, vol. 263, No. 3, pp. 810-815 (1999).
Chai, K.X. et al., “Kallistatin: A Novel Human Serine Proteinase Inhibitor”, The Journal of Biological Chemistry, vol. 268, No. 32, pp. 24498-24505 (1993).
Chandra, T. et al., “Sequence Homology between Human α1-Antichymotrypsin, α1-Antitrypsin, and Antithrombin III”, Biochemistry, vol. 22, No. 22, pp. 5055-5061 (1983).
Combrink, K.D. et al., “1,2-Benzisothiazol-3-one 1,1-Dioxide Inhibitors of Human Mast Cell Tryptase”, J. Med. Chem., vol. 41, No. 24, pp. 4854-4860 (1998).
Cooper, J.A. et al., “Phosphorylation Sites in Enolase and Lactate Dehydrogenase Utilized by Tyrosine Protein Kinases in Vivo and in Vitro”, The Journal of Biological Chemistry, vol. 259, No. 12, pp. 7835-7841 (1984).
Cossins, J. et al., “Identification of MMP-18, a Putative Novel Human Matrix Metallopr

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