Methods of inhibiting amyloid toxicity

Details Methods of inhibiting amyloid toxicity Methods of inhibiting amyloid toxicity

2011-03-08

2011-03-08

Kolker, Daniel E. (Department: 1649)

Drug, bio-affecting and body treating compositions

Immunoglobulin, antiserum, antibody, or antibody fragment,...

Monoclonal antibody or fragment thereof

C424S133100, C424S141100, C424S152100

Reexamination Certificate

active

07901683

ABSTRACT:
The present invention features methods and compositions for inhibiting amyloidogenic protein toxicity, inhibiting formation of an amyloidogenic protein deposit and/or treating amyloidogenic diseases by administering a pharmaceutically effective amount of one or more agents that bind an integrin or an integrin subunit.

REFERENCES:
patent: 5612486 (1997-03-01), McConlogue et al.
patent: 5753230 (1998-05-01), Brooks et al.
patent: 5849865 (1998-12-01), Cheng et al.
patent: 5985278 (1999-11-01), Mitjans et al.
patent: 6469024 (2002-10-01), Li et al.
patent: 6743427 (2004-06-01), Schenk
patent: 7517525 (2009-04-01), Prenner et al.
patent: 2002/0160954 (2002-10-01), Hageman et al.
patent: 2003/0040044 (2003-02-01), Heavner et al.
patent: 2003/0202977 (2003-10-01), Amin et al.
patent: 2004/0259152 (2004-12-01), Murray et al.
patent: 2008/0193444 (2008-08-01), Wright et al.
patent: 0 719 859 (1996-07-01), None
patent: WO 98/15179 (1998-04-01), None
patent: WO 99/27944 (1999-06-01), None
patent: WO 99/37683 (1999-07-01), None
patent: WO 00/44404 (2000-08-01), None
patent: WO 00/66730 (2000-11-01), None
patent: WO 03/006893 (2003-01-01), None
patent: WO 2008/116100 (2008-08-01), None
U.S. Appl. No. 11/723,745, filed Mar. 21, 2007.
U.S. Appl. No. 60/341,772, filed Dec. 17, 2001.
U.S. Appl. No. 60/304,315, filed Jul. 9, 2001.
Adams, “Collagen Gene Expression,” Am. J. Respir. Cell. Molec. Biol., 1:161-168 (1989).
Alberts et al.,Molecular Biology of the Cell, 3rdEdition, pp. 129-130 (1994).
Akiyama et al, Immunohistochemical localization of vitronectin, its receptor and beta-3 integrin in Alzheimer brain tissue,J. Neuroimmunol., 32(1):19-28 (1991).
ATTC Accession HB-8448, L230 Monoclonal antibody (accessed 2006).
Bamberger et al., A cell surface receptor complex for fibrillar beta-amyloid mediates microglial activation,J. Neurosci., 23:(7):2665-2674 (2003).
Bard, F. et al.,Nature Medicine, 6(8):916-919(2000).
Basler et al., “Scrapie and Cellular PrP Isoforms Are Encoded by the Same Chromosomal Gene,”Cell, 46:417-428 (1986).
Batt et al., “Disubstituted Indazoles as Potent Antagonists oflntegrin alphaVbeta3,”Journal of Medicinal Chemistry, 43:41-58 (2000).
BOLTONet al., “Identification of a Protein That Purifies with the Scrapie Prion”,Science, 218:1309-1311(1982).
Borchelt et al., “Accelerated Amyloid Deposition in the Brains of Transgenic Mice Coexpressing Mutant Presenilin 1 and Amyloid Precursor Proteins,”Neuron, 19:939-945 (1997).
Bronfman et al., “Laminin Blocks the Assembly of Wild-Type AP and the Dutch Variant Peptide into Alzheimer's Fibrils,”Amyloid: Int. J. Exp. Clin. Invest. 5, 5:16-23 (1998).
Chartier-Harlin et al., “Early-Onset Alzheimer's Disease Caused by Mutations at Codon 717 of the p- Amyloid Precursor Protein Gene,”Nature, 353:844-846 (1991).
Castillo et al., “Laminin Inhibition of p-Amyloid Protein (AP) Fibrillogenesis and Identification of An AP Binding Site Localized to the Globular Domain Repeats on the Laminin A Chain,”J. Neurosci. Res., 62:451-462 (2000).
Chemicon Antibody Information Sheet, Mouse Anti-Human Integrin αV Monoclonal Antibody, dated Aug. 1998.
Cheresh et al, “Human Endothelial Cells Synthesize and Express an Arg-Gly-Asp-directed Adhesion Receptor Involved in Attachment of Fibrinogen and Von Willebran Factor,,”PNAS, 84:6471-6475 (1987).
Chesebro et al., “Identification of Scrapie Prion Protein-Specific mRNA in Scrapie-Infected and Uninfected Brain,”Nature, 315:331-333 (1985).
Choh, “β-Endorphin Omission Analogs: Dissociation of Immunoreactivity From Other Biological Activates,”PNAS, 77(6):3211-3214 (1990).
Chung et al., “Parkin Ubiquitinates the a-Synuclein-lnteracting Protein, Synphilin-1: Implications for Lewy-Body Formation in Parkinson Disease,”Nature Medicine, 7:1144 1150 (2001).
Cooper et al., “Amylin Found in Amyloid Deposits in Human Type 2 Diabetes Mellitus May be a Hormone that Regulates Glycogen Metabolism in Skeletal Muscle.”Proc. Natl. Acad. Sci. USA, 85:7763-7766 (1988).
Coulson et al., Down-regulation of the amyloid protein precursor of Alzheimer's disease by antisense oligonucleotides reduces neuronal adhesion to specific substrata,Brain Res., 770(1-2):72-80 (1997).
Eikelenboom et al., Cellular and substrate adhesion molecules (integrins) and their ligands in cerebral amyloid plaques in Alzheimer's disease,Virchows Arch., 424(4): 421-427 (1994).
El Khoury et a/., “Scavenger Receptor-Mediated Adhesion of Microglia to p-Amyloid Fibrils,”Nature, 382:716-719 (1996).
Friedlander et al., “Migration of Brain Tumor Cells on Extracellular Matrix Proteins in Vitro Correlates with Tumor Type and Grade and Involves αvand β1Integrins1,”Cancer Research, 56:1939-1947 (1996).
Ghiso et al., “A 109-Amino-Acid C-Terminal Fragment of Alzheimer's-Disease Amyloid Precursor Protein Contains a Sequence, -RHDS-, that Promotes Cell Adhesion,”Biochem. J., 288:1053-1059 (1992).
Giese et al., “Prion-Induced Neuronal Damage—The Mechanisms of Neuronal Destruction in the Subacute Spongiform Encephalopathies in the Mechanisms of Neuronal Damage in Virus Infections of the Nervous System (Gosztony, 6.ed.),”Springer-Verlag, pp. 204-27 (2001).
Goate et al., “Segregation of a Missense Mutation in the Amyloid Precursor Protein Gene with Familial Alzheimer's Disease,”Nature, 349:704-706 (1991).
Hardy, “Amyloid, the Presenilins and Alzheimer's Disease,”Trends Neurosci., 20:154-159 (1997).
Harlow et al., Antibodies: A laboratory Manual, 7-10 (1988).
Henthorn et al., “Active Transport of Fentanyl by the Blood-Brain Barrier1,”Journal of Pharmacology and Experimental Therapeutics, 289:1084-1089 (1999).
Hsiao et a/., “Correlative Memory Deficits, AfJ Elevation, and Amyloid Plaques in Transgenic Mice”,Science, 274:99-102 (1996).
Hund et a/., “Transthyretin-Associated Neuropathic Amyloidosis,”Neurology, 56:431-435 (2001).
Hynes, “Integrins: Versatility, Modulation, and Signaling in Cell Adhesion,”Cell, 69: 11-25 (1992).
Johnson et al., “Islet Amyloid Polypeptide: Mechanisms of Amyloidogenesis in the Pancreatic Islets and Potential Roles in Diabetes Mellitus”,Laboratory Investigation, 66:522-535 (1992).
Kahn et a/., “Islet Amyloid: A Long-Recognized but Underappreciated Pathological Feature of Type 2 Diabetes,”Diabetes, 48:241-253 (1999).
Kang et a/., “The Precursor of Alzheimer's Disease Amyloid A4 Protein Resembles a Cell-Surface Receptor,”Nature, 325:733-736 (1987).
Kawahara, E. et al.,American Journal of Pathology, 134(6):1305-1314 (1989).
Kellings et al., “Further Analysis of Nucleic Acids in Purified Scrapie Prion Preparations by Improved Return Refocusing Gel Electrophoresis,”Journal of General Virology, 73:1025-1029 (1992).
Kitaguchi et al., “Novel Precursor of Alzheimer's Disease Amyloid Protein Shows Protease Inhibitory Activity,”Nature, 331:530-532 (1988).
Kuby et al., Immunology, 3rdEdition: p. 123 (1997).
Leighton et al., “Pancreatic Amylin and Calcitonin Gene-Related Peptide Cause Resistance to Insulin in Skeletal Muscle In Vitro,”Nature, 335:632-635 (1988).
Matsubara et al., Association between diabetic retinopathy and genetic variations in α1β2 integrin, a platelet receptor for collagen,Blood, 95(5):1560-1564 (2000).
Matter et al., “The a5p1 Integrin Mediates Elimination of Amyloid-P Peptide and Protects Against Apoptosis,”The Journal of Cell Biology, 141:1019-1030 (1998).
McGeer et al., “Innate Inflammatory Reaction of the Brain in Alzheimer Disease,”MJM, 3:134-141 (1997).
Monning et al., “Extracellular matrix influences the biogenesis of amyloid precursor protein in microglial cells,”J. Bioi Chem., 270(13):7104-7110 (1995).
Mullan et al., “A Pathogenic Mutation for Probable Alzhe

Affiliated with

Also associated with

Rating

Methods of inhibiting amyloid toxicity does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Methods of inhibiting amyloid toxicity, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Methods of inhibiting amyloid toxicity will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-2664849