Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues
Patent
1997-05-01
2000-01-25
Russel, Jeffrey E.
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
C07K 200, C07K 1447
Patent
active
060180242
ABSTRACT:
Processing of .beta.-amyloid precursor protein (.beta.APP) is monitored by detecting the secretion of a soluble .beta.APP fragment resulting from cleavage of .beta.APP at the amino-terminus of .beta.-amyloid peptide. In vivo monitoring of secretion of the .beta.APP fragment may be monitored for diagnosis and prognosis of Alzheimer's disease and other .beta.-amyloid-related diseases, while in vitro monitoring of such secretion from cultured cells may be monitored to identify inhibitors of .beta.-amyloid production. The .beta.APP fragment may be detected using antibodies and other specific binding substances which recognize a carboxy-terminal residue on the fragment.
REFERENCES:
patent: 4666829 (1987-05-01), Glenner et al.
patent: 5134062 (1992-07-01), Blass
patent: 5200339 (1993-04-01), Abraham
patent: 5213962 (1993-05-01), Van Nostrand et al.
patent: 5223482 (1993-06-01), Schilling 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
Higgins et al. (1994) Ann. Neurol. 35:598-607. Transgenic mouse brain histopathology resembles early Alzheimer's disease.
Higgins et al. (1993) Ann. New York Acad. Sci. 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. (1992) Abstr. 22nd Ann. Meet. Soc. Neurosci. 18(Pt. 1):19. Oct. 25-30, 1992, Anaheim, CA. Abstract No. 15.5. An alternative secretase cleavage produces soluble Alzheimer amyloid precursor protein containing a potentially amyloidogenic sequence.
Seubert et al. (1993) Nature 361:260-263. 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. (1922) 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. 51:76-83. Kunitz protease inhibitor-containing amyloid .beta.protein precursor immunoreactivity in Alzheimer
Kennedy et al. (1992) Neurodegeneration 1:59-64. Only Kunitz-inhibitor-containing isoforms of secreted Alzheimer's disease. 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 in 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-Harlin 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.
Gote et al. (1991) Nature 349:704-706. Segregation of a missense mutation in the amyloid precursor protein gene woth familial Alsheimer's disease.
Murrell et al. (1991) Science 254:97-99. A mutation in 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 amyloid precursor protein. Identification of a stable intermediate in the biosynthetic/degradative pathway.
Osltersdorf et al. (1989) Nature 341:144-147. 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. Commun. 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 homologus to serine proteinase inhibitors.
Selkoe et al. (1988) Proc. Natl. Acad. Sci. USA 85:7341-7345. .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. Methods 9:301-316. Use of aggregating brain cultures to study the replication of herpes simplex virus types 1 and 2 in central nervous system tissue.
Goding, J.W. (1983) Academic Press, pp. 56-75. Monoclonal Antibodies: Principles and Practice.
Sahasrabudhe et al. (1993) J. Biol. Chem. 268:16699-16705. Enzymatic generation of the amino terminus of the .beta.-amyloid peptide.
Knops et al. (1995) J. Biol. Chem. 270:2419-2422. Cell-type and amyloid precursor protein-type specific inhibition of A.beta. release by bafilomycin A1, a selective inhibitor of vacuolar ATPases.
Haass et al. (1995) Nature Medicine 1:1291-1296. The Swedish mutation causes early-onset Alzheimer's disease by .beta.-secretase cleavage within the secretory pathway.
Harlow, E. and Lane, D. (1988) Cold Spring Harbor Laboratory, pp. 74-76. Antibodies: A Laboratory Manual.
Henricksson et al. (1991) J. Neurochem. 56:1037-1042. Analysis and quantitation of the .beta.-amyloid precursor protein in the cerebrospinal fluid of Alzheimer's disease patients with a monoclonal antibody-based immunoassay.
Tamaoka et al. (1992) Proc. Natl. Acad. Sci. USA 89:1345-1349. Identification of a stable fragment of the Alzheimer amyloid precursor containing the .beta.-protein in brain microvessels.
Fritz Lawrence C.
Schenk Dale B.
Seubert Peter A.
Elan Pharmaceuticals
Russel Jeffrey E.
LandOfFree
Methods and compositions for monitoring cellular processing of b 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 and compositions for monitoring cellular processing of b, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Methods and compositions for monitoring cellular processing of b will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-2316628