Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving viable micro-organism
Patent
1995-05-12
1997-02-25
Gitomer, Ralph
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving viable micro-organism
435 23, 435 692, 424 92, C12Q 102
Patent
active
056058110
ABSTRACT:
The present invention provides methods for identifying beta amyloid production inhibitors, wherein cells are cultured under conditions which result in secretion of a soluble fragment of beta amyloid precursor protein. The amino acid sequence of the fragment extends from the amino terminus of beta APP to the amino terminus of the beta amyloid peptide. The cultured cells are exposed to test compounds which cause a change in the secreted amount of the soluble fragment of beta APP which is determined.
REFERENCES:
patent: 4666829 (1987-05-01), Glenner et al.
patent: 5134062 (1992-07-01), Blass
patent: 5200339 (1993-04-01), Abraham
patent: 5223482 (1993-06-01), Schilling, Jr. et al.
patent: 5234814 (1993-08-01), Card et al.
patent: 5385915 (1995-01-01), Buxbaum et al.
patent: 5387742 (1995-02-01), Cordell
patent: 5441870 (1995-08-01), Seubert et al.
Higgins et al. (1994) Annals of Neurology 35:598-607. Transgenic Mouse Brain Histopathology Resembles Early Alzheimer's Disease.
Higgins et al. (1993) Annals New York Academy of Sciences 695:224-227. Transgenic Mice Expressing Human .beta.-APP751, But Not Mice Expressing .beta.-APP695, Display Early Alzheimer's Disease-like Histopathology.
Robakis et al. Soc. Neurosci. Oct. 26, 1993, Abstract No. 15.4, Anaheim, CA. An Alternative Secretase Cleavage Produces Soluble Alzheimer Amyloid Precursor Protein Containing a Potentially Amyloidogenic Sequence.
Seubert et al. (1993) Nature 362:260-263. Secretion of .beta.-amyloid precursor protein cleaved at the amino terminus of the .beta.-amyloid peptide.
Estus et al. (1992) Science 255:726-728. Potentially Amyloidogenic, Carboxyl-Terminal Derivatives of the Amyloid Protein Precursor.
Golde et al. (1992) Science 255:728-730. Processing of the Amyloid Protein Precursor to Potentially Amyloidogenic Derivatives.
Haass et al. (1992) Nature 359:322-325. Amyloid .beta.-peptide is produced by cultured cells during normal metabolism.
Hyman et al. (1992) J. Neuropath. Exp. Neurol. 51:76. Kunitz Protease Inhibitor-Containing Amyloid .beta. Protein Precursor Immunoreactivity in Alzheimer's Disease.
Kennedy et al. (1992) Neurodegeneration 1:59-64. Only Kunitz-Inhibitor-Containing Isoforms of Secreted Alzheimer Amyloid Precursor Protein Show Amyloid Immunoreactivity in Normal Cerebrospinal Fluid.
Mullan et al. (1992) Nature Genet 1:345-347. A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of .beta.-amyloid.
Seubert et al. (1992) Nature 359:325-327. Isolation and quantification of soluble Alzheimer's .beta.-peptide from biological fluids.
Abraham et al. (1991) Biochem. Biophys. Res. Comm. 174:790-796. A Calcium-Activated Protease From Alzheimer's Disease Brain Cleaves At The N-Terminus Of The Amyloid .beta.-Protein.
Chartier Harlan et al. (1991) Nature 353:844-846. Early-onset Alzheimer's disease caused by mutations at codon 717 of the .beta.-amyloid precursor protein gene.
Goate et al. (1991) Nature 349:704-706. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease.
Murrell et al. (1991) Science 254:97-99. A Mutation in the Amyloid Precursor Protein Associated with Hereditary Alzheimer's Disease.
Quon et al. (1991) Nature 352:239-241. Formation of .beta.-amyloid protein deposits in brains of transgenic mice.
Esch et al. (1990) Science 248:1122-1124. Cleavage of Amyloid .beta. Peptide During Constitutive Processing of Its Precursor.
Forss-Petter et al. (1990) Neuron 5:187-197. Transgenic Mice Expressing .beta.-Galactosidase in Mature Neurons under Neuron-Specific Enolase Promoter Control.
Oltersdorf et al. (1990) J. Biol. Chem. 265:4492-4497. The Alzheimer's Amyloid Precursor Protein.
Oltersdorf et al. (1989) Nature 341:144. The secreted form of the Alzheimer's amyloid precursor protein with the Kunitz domain is protease nexin-II.
Palmert et al. (1989) Biochem. Biophys. Res. Comm. 165:182-188. Soluble Derivatives Of The .beta. Amyloid Protein Precursor Of Alzheimer's Disease Are Labeled By Antisera To The .beta. Amyloid Protein.
Palmert et al. (1989) Proc. Natl. Acad. Sci USA 86:6338-6342. The .beta.-amyloid protein precursor of Alzheimer disease has soluble derivatives found in human brain and cerebrospinal fluid.
Weidemann et al. (1989) Cell 57:115-126. Identification, Biogenesis, and Localization of Precursors of Alzheimer's Disease A4 Amyloid Protein.
Kitaguchi et al. (1988) Nature 331:530-532. Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity.
Ponte et al. (1988) Nature 331:525-527. A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors.
Selkoe et al. (1988) Proc. Natl. Acad. Sci. USA 85:7341. .beta.-Amyloid precursor protein of Alzheimer disease occurs as 110-to 135-kilodalton membrane-associated proteins in neural and nonneural tissues.
Kang et al. (1987) Nature 325:733-736. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor.
Glenner and Wong (1984) Biochem. Biophys. Res. Commun. 120:885-890. Alzheimer's Disease: Initial Report Of The Purification And Characterization Of A Novel Cerebrovascular Amyloid Protein.
Glenner and Wong (1984) Biochem. Biophys. Res. Commun. 122:1131-1135. Alzheimer's Disease And Down's Syndrome: Sharing Of A Unique Cerebrovascular Amyloid Fibril Protein.
Pulliam et al. (1984) J. Virol. Met. 9:301. Use Of Aggregating Brain Cultures To Study The Replication Of Herpes Simplex Virus Types 1 and 2 In Central Nervous System Tissue.
J. W. Goding (1983) Academic Press (London) pp. 56-75. Monoclonal Antibodies: Principles and Practice.
Fritz Lawrence C.
Schenk Dale B.
Seubert Peter A.
Athena Neurosciences, Inc.
Duvall Jean M.
Eli Lilly and Company
Gitomer Ralph
Storella John R.
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