Chemistry: analytical and immunological testing – Food or dairy products – Dairy product
Reexamination Certificate
2007-03-06
2007-03-06
Nashed, Nashaat T. (Department: 1656)
Chemistry: analytical and immunological testing
Food or dairy products
Dairy product
C435S069100, C435S226000, C435S252300, C435S320100
Reexamination Certificate
active
10116519
ABSTRACT:
The present invention provides novel polynucleotides encoding CAN-12 polypeptides, fragments and homologues thereof. The present invention also provides polynucleotides encoding variants of CAN-12 polypeptides, CAN-12v1 and CAN-12v2. 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 CAN-12, CAN-12v1, and CAN-12v2 polypeptides to the diagnosis, treatment, and/or prevention of various diseases and/or disorders related to these polypeptides, particularly neuro- and musculo-degenerative conditions. The invention further relates to screening methods for identifying agonists and antagonists of the polynucleotides and polypeptides of the present invention.
REFERENCES:
patent: 6943241 (2005-09-01), Isogai et al.
patent: 2003/0204070 (2003-10-01), Chen et al.
patent: 2004/0014093 (2004-01-01), Duclos et al.
patent: 2004/0029249 (2004-02-01), Lee et al.
patent: 2004/0063107 (2004-04-01), Plowman et al.
patent: 1308459 (2003-05-01), None
patent: WO 96/14067 (1996-05-01), None
patent: WO 96/25403 (1996-08-01), None
patent: WO 98/11134 (1998-03-01), None
patent: WO0175067 (2001-10-01), None
patent: WO0183782 (2001-11-01), None
patent: WO0238744 (2002-05-01), None
Busquets, et al. “Calpain-3 gene expression is decreased during experimental cancer cachexia”, Biochimica et Biophysica Acta, vol. 1475, pp. 5-9 (2000).
Huang, et al. “The calpin family and human disease”, TRENDS in Mol. Med., vol. 7, No. 8, pp. 355-362 (2001).
NCBI Entrez Accession No. AC015980 (gi:17647083), Sulston, et al., Jan. 10, 2002.
NCBI Entrez Accession No. 1CFZF (gi:7546423), Fritsche, E. et al., Mar. 23, 1999.
NCBI Entrez Accession No. AAC61764 (gi:3661585), Ma, H. et al., Sep. 29, 1998.
NCBI Entrez Accession No. AL133246 (gi:7594587), Hazan, J. et al., Apr. 18, 2002.
NCBI Entrez Accession No. AL540944 (gi:45716538), Li, W.B. et al., Mar. 24, 2004.
NCBI Entrez Accession No. BM554389 (gi:18793945), NIH-MGC, Feb. 20, 2002.
NCBI Entrez Accession No. NP13000061 (gi:4557405), Diaz, B.G. et al., Oct. 26, 2004.
NCBI Entrez Accession No. NP13001739 (gi:4502563), Alexa, A. et al., Oct. 26, 2004.
NCBI Entrez Accession No. NP13004046 (gi:37577157), Waghray, A. et al., Mar. 2, 2005.
NCBI Entrez Accession No. NP13005177 (gi:12408656), Kulkarni, S. et al., Oct. 26, 2004.
NCBI Entrez Accession No. NP13006606 (gi:5729758), Huang, Y. et al., Mar. 2, 2005.
NCBI Entrez Accession No. NP13008989 (gi:5901916), Dear, T.N. et al., Jan. 26, 2005.
NCBI Entrez Accession No. NP13075571 (gi:13186302), Carlsson, E. et al., Oct. 26, 2004.
NCBI Entrez Accession No. NP13075574 (gi:13186308), Carlsson, E. et al., Mar. 2, 2005.
NCBI Entrez Accession No. O35350 (gi:12643550), Poirier, C. et al., May 1, 2005.
NCBI Entrez Accession No. XP13351430 (gi:37546876), Oct. 17, 2003.
Swiss-Prot Accession No. Q64698, Release 01, Nov. 1996.
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).
Arora, A.S. et al., “Hepatocellular Carcinoma Cells Resist Necrosis During Anoxia by Preventing Phospholipase-Mediated Calpain Activation”, Journal of Cellular Physiology, vol. 167, pp. 434-442 (1996).
Azuma, M. et al., “Cysteine protease inhibitor E64 reduces the rate of formation of selenite cataract in the whole animal”, Current Eye Research, vol. 10, No. 7, pp. 657-666 (1991).
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).
Baier, L.J. et al., “A calpain-10 gene polymorphism is associated with reduced muscle mRNA levels and insulin resistance”, The Journal of Clinical Investigation, vol. 106, pp. R69-R73 (2000).
Bairoch, A. et al., “EF-hand mofits in inositol phospholipid-specific phospholipase C”, FEBS Letters, vol. 269, No. 2, pp. 454-456 (1990).
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).
Banik, N.L. et al., “Role of Calpain and Its Inhibitors in Tissue Degeneration and Neuroprotection in Spinal Cord Injury”, Annals New York Academy of Sciences, vol. 825, pp. 120-127 (1997).
Banik, N.L. et al., “Role of Calpain in Spinal Cord Injury: Effects of Calpain and Free Radical Inhibitors”, Annals New York Academy of Sciences, vol. 844, pp. 131-137 (1998).
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).
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).
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).
Bradbury, A.F. et al., “Biosynthesis of the C-Terminal Amide in Peptide Hormones”, Bioscience Reports, vol. 7, No. 12, pp. 907-916 (1987).
Carafoli, E. et al., “Calpain: A Protease in Search of a Function?”, Biochemical and Biophysical Research Communications, vol. 247, No. 2, pp. 193-203 (1998).
Cardozo, T. et al., “Homology Modeling by the ICM Method”, Proteins: Structure, Function, and Genetics, vol. 23, pp. 403-414 (1995).
Chapot-Cartier, M.-P. et al., “Cloning and Sequencing ofPepC, a Cysteine Aminopeptidase Gene fromLactococcus lactissubsp.cremorisAM2”, Applied and Environmental Microbiology, vol. 59, No. 1, pp. 330-333 (1993).
Chauvaux, S. et al., “Calcium-binding affinity and calcium-enhanced activity ofClostridium thermocellumendoglucanase D”, Biochem. J., vol. 265, pp. 261-265 (1990).
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).
Cuzzocrea, S. et al., “Calpain Inhibitor I Reduces the Development of Acute and Chronic Inflammation”, American Journal of Pathology, vol. 157, No. 6, pp. 2065-2079 (2000).
David, L.L. et al., “Buthionine sulfoximine induced cataracts in mice contain insolubilized crystallins with calpain II cleavage sites”, Exp. Eye Res., vol. 59, pp. 501-504 (1994).
DeBiasi, R.L. et al., “Calpain Inhibition Protects against Virus-Induced Apoptotic Myocardial Injury”, Journal of Virology, vol. 75, No. 1, pp. 351-361 (2001).
D'Souza, S.E. et al., “Arginyl-glycyl-aspartic acid (RGD): a cell adhesion motif”, Trends in Biochemical Sciences, vol. 16, pp. 246-250 (1991).
Dufour, E., “Sequence homologies, hydrophobic profiles and secondary structures of cathepsins B, H and L: comparison with papain and actinidin”, Biochimie, vol. 70, pp. 1335-1342 (1988).
Ebers, G.C. et al., “A full genome search in multiple sclerosis”, Nature Genetics, vol. 13, pp. 472-476 (1996).
Elce, J.S., ed., Methods in Molecular Biology: Calpain Methods and Protocols, Humana Press Inc., publ., pp. ix-xii (table of contents) (2000).
Fox, J.E.B., “On the Role of Calpain and Rho Proteins in Regulating Integrin-induced Signaling”, Thrombosis and Haemostasis, vol. 82, No. 2, pp. 385-3
Chen Jian
Duclos Franck
Nelson Thomas C.
Vaz Roy J.
Bristol--Myers Squibb Company
D'Amico Stephen C.
Moore William W.
Nashed Nashaat T.
LandOfFree
Polynucleotides encoding novel cysteine proteases of the... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Polynucleotides encoding novel cysteine proteases of the..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Polynucleotides encoding novel cysteine proteases of the... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3747385