Drug – bio-affecting and body treating compositions – Enzyme or coenzyme containing – Transferases
Reexamination Certificate
2011-06-28
2011-06-28
Prouty, Rebecca E. (Department: 1652)
Drug, bio-affecting and body treating compositions
Enzyme or coenzyme containing
Transferases
C435S232000, C536S023200
Reexamination Certificate
active
07968089
ABSTRACT:
The present disclosure relates to the preparation and deletion mutants of chondroitinase proteins and their use in methods for promoting the diffusion of therapeutic composition into tissues and their use for neurological functional recovery after central nervous system (“CNS”) injury or disease.
REFERENCES:
patent: 5498536 (1996-03-01), Khandke
patent: 5578480 (1996-11-01), Khandke
patent: 6007810 (1999-12-01), Ishikawa et al.
patent: 7008783 (2006-03-01), Sato et al.
patent: 2005/0233419 (2005-10-01), Pojasek et al.
patent: 2006/0078959 (2006-04-01), Prabhakar et al.
patent: 2006/0233782 (2006-10-01), Gruskin et al.
patent: 2007/0104703 (2007-05-01), Caggiano et al.
patent: WO 94/25567 (1994-11-01), None
patent: WO 00/62067 (2000-10-01), None
patent: 02/08285 (2002-01-01), None
patent: 02/065136 (2002-08-01), None
patent: 03/022882 (2003-03-01), None
patent: 03/031578 (2003-04-01), None
patent: WO 03/074080 (2003-09-01), None
patent: WO 03/100031 (2003-12-01), None
patent: WO 03/102160 (2003-12-01), None
patent: 2004/103299 (2004-12-01), None
patent: 2004/110359 (2004-12-01), None
patent: WO 2004/110360 (2004-12-01), None
patent: 2005/087920 (2005-09-01), None
patent: 2005/112986 (2005-12-01), None
patent: 2007/038548 (2007-04-01), None
Sato et al., Subunit Structure of Chondroitinase ABC from Proteus vulgaris, 1986, Agric. Biol. Chem. 50(4):1057-1059.
Fethiere et al., Crystal Structure of Chondroitin AC Lyase, a Representative of a family of Glycosaminoglycan Degrading Enzymes, 1999, J. Mol. Biol. 288:635-647.
Pojasek et al., Recombinant Expression, Purification, and Kinetic Characterization of Chondroitinase AC and Chondroitinase B from Flavobacterium heparinum, 2001, Biochem. Biophys. Res. Commun. 286:343-351.
Huang et al., Crystal Structure of Chondroitinase B from Flavobacterium heparinum and its Complex with a Disaccharide Product at 107 A Resolution, 1999, J. Mol. Biol. 294:1257-1269.
Miura et al,, Analysis of Glycosaminoglycan-Degrading Enzymes by Substrate Gel Electrophoresis (Zymography), 1995, Anal. Biochem. 225:333-340.
Saito et al., Enzymatic Methods for the Determination of Small Quantities of Isomeric Chondroitin Sulfates, 1968, J. Biol. Chem. 243(7):1536-1542.
Sato et al., Cloning and expression inEscherichia coliof the gene encoding the Proteus vulgaris chondroitin ABC-lyase, 1994, Appl. Microbiol. Biotechnol. 41:39-46.
Frankel et al., Tat Protein from Human Immunodeficiency Virus Forms a Metal-Linked Dimer, 1988, Science 240:70-73.
Zuo et al., Regeneration of Axons After Nerve Transection Repair is Enhanced by Degradation of Chondroitin Sulfate Proteoglycan, 2002, Exp. Neurology 176:221-228.
Yamagata et al., Purification and Properties of Bacterial Chondroitinases and Chondrosulfatases, 1968, J. Biol. Chem. 243(7):1523-1535.
Bradbury et al., Chondroitinase ABC Promotes Functional Recovery After Spinal Cord Injury, Apr. 11, 2002, Nature 416:636-640.
Huang et al., Active Site of Chondroitin AC Lyase Revealed by the Structure of Enzyme-Oligosaccharide Complexes and Mutagenesis, Jan. 1, 2001, Biochemistry, 40(8):2359-2372.
Pojasek et al., Biochemical Characterization of the Chondroitinase B Active Site, Aug. 23, 2002, J. Biol. Chem., 277(34):31179-31186.
Roy et al., Generation of Substantially Smaller Deletion Mutants of Chondroitinase AC and B Those are Biologically Active, Society for Neuroscience Abstract Viewer and Itinerary Planner, 33rdAnnual Meeting of the Society of Neuroscience, New Orleans, LA, Nov. 8-12, 2003, Database Biosis, (Abstract).
Accession P59807, Aug. 15, 2003UniProtKB/Swiss-Prot.
Banker et al. “Modern Pharmaceutics” 1979,Marcel Dekker, Inc. (TOC).
Banker et al. “Modern Pharmaceutics” 4th Ed., 2002,Informa Healthcare, New York (TOC).
Ben-Bassat et al. “Processing of the Initiation Methionine from Proteins: Properties of theEscherichia coliMethionine Aminopeptidase and Its Gene Structure” 1987,J. Bacteriol. 169(2):751-757.
Blight et al. “Animal models of spinal cord injury” 2002,Top Spinal Cord Inj. Rehabi. 6(2):1-13.
Broach et al. “Experimental Manipulation of Gene Expression” M. Inouye ed.,Academic Press, New York, pp. 83-117.
Caggiano et al. “Chondroitinase ABCI Improves Locomotion and Bladder Function following Contusion Injury of the Rat Spinal Cord” 2005,J. Neurotrauma22(2):226-239.
Fawcett et al. “The glial scar and central nervous system repair” 1999,Brain Res. Bull. 49(6):377-391.
Goodman et al. “The Pharmacological Basis of Therapeutics” 10th ed., 2001,McGraw Hill, New York(TOC).
Goodman et al. “The Pharmacological Basis of Therapeutics” 6th ed. 1980,MacMillan Pub., New York(TOC).
Hamai et al. “Two Distinct Chondroitin Sulfate ABC Lyases” 1997,J. Biol. Chem. 272(14):9123-9130.
Hirschberg et al. “Inflammation after axonal injury has conflicting consequences for recovery of function: rescue of spared axons is impaired but regeneration is supported” 1994,J. Neuroimmunol. 50(1):9-16(ABSTRACT).
Hoffman et al. “Chondroitin Sulfates” 1958,Federation Proc. 17:1078-1082.
Hou et al. “Endotoxin Removal by Anion-Exchange Polymeric Matrix” 1990,Biotech. Appl. Biochem. 12:315-324.
Huang et al. “Crystal Structure of Proteus vulgaris Chondroitin Sulfate ABC Lyase I at 1.9 A Resolution” 2003,J. Mol. Biol. 328:623-634.
Korn “The Degradation of Heparin by Bacterial Enzymes” 1957,J. Biol. Chem. 226:841-844.
Krekoski et al. “Axonal Regeneration into Acellular Nerve Grafts is Enhanced by Degradation of Chondroitin Sulfate Proteoglycan” 2001,J. Neurosci. 15:21(16):6206-6213.
Kwon et al. “Animal Models Used in Spinal Cord Regeneration Research” 2002,Spine27(14):1504-1510.
Martinez et al. “Purification and Properties of the Enzyme Chondroitinase” 1959,J. Biol. Chem. 234(9):2236-2239.
Michelacci et al. “Chondroitinase C from Flavobacterium haparinum” 1976,J. Biol. Chem. 251(4):1154-1158.
Michelacci et al. “Isolation and characterization of an induced Chondroitinase ABC” 1987,Biochem. Biophys. Acta923:291-301.
Michelacci et al., A Comparative Study Between a Chondroitinase B and a Chondroitinase AC from Flavobacterium heparinum, 1975,Biochem. J. 151:121-129.
Miller et al. “N-terminal methionine-specific peptidase inSalmonella typhimurium” 1987,PNAS84:2718-2722.
Prabhakar et al. “Biochemical Characterization of the Chondroitinase ABC I Active Site” Aug. 23, 2005,Biochem. J. pp. 395-405.
Reich et al. “Small interfering RNA (siRNA) targeting VEGF effectively inhibits ocular neovascularization in a mouse model” 2003,Molecular Vision9:210-216.
Sambrook et al. “Molecular Cloning” 2nd ed., 1989,Cold Spring Harbor Laboratory Press, Ch. 16 and 17.
Zuo et al. “Degradation of Chondroitin Sulfate Proteoglycan Enhances the Neurite-Promoting Potential of Spinal Cord Tissue” 1998,Exp. Neurol. 154(2):654-662.
Caggiano Anthony O.
D'Souza Rohini
Gruskin Elliott A.
Roy Gargi
Acorda Therapeutics, Inc.
Pepper Hamilton LLP
Prouty Rebecca E.
LandOfFree
Proteoglycan degrading mutants for the treatment of CNS does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Proteoglycan degrading mutants for the treatment of CNS, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Proteoglycan degrading mutants for the treatment of CNS will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-2724728