Multicellular living organisms and unmodified parts thereof and – Nonhuman animal – Transgenic nonhuman animal
Reexamination Certificate
2005-05-31
2005-05-31
Woitach, Joseph (Department: 1632)
Multicellular living organisms and unmodified parts thereof and
Nonhuman animal
Transgenic nonhuman animal
C800S012000, C800S003000
Reexamination Certificate
active
06900367
ABSTRACT:
Transgenic flies displaying altered phenotypes due to expression of the Abeta and C99 portions of the human APP gene are disclosed. Use of these flies in a method to identifyDrosophilagenes and the human homologs of theseDrosophilagenes, that are potentially involved in Alzheimer's Disease, is also disclosed. The use of said human homologs as drug targets for the development of therapeutics to treat Alzheimer's Disease and other conditions associated with defects in the APP pathway, as well as pharmaceutical compositions comprising substances directed to these genes, are also disclosed.
REFERENCES:
patent: 5795963 (1998-08-01), Mullan
patent: 5811633 (1998-09-01), Wadsworth et al.
patent: 5840540 (1998-11-01), St. George-Hyslop et al.
patent: 5891991 (1999-04-01), Wasco et al.
patent: 5986054 (1999-11-01), St. George-Hyslop et al.
patent: WO 94/00569 (1994-01-01), None
patent: WO 98/54300 (1998-12-01), None
patent: WO 01/85912 (2001-11-01), None
Siman, 2000, Journal of Neuroscience, vol. 20, pp. 8717-8726.*
Niemann, 1997, Transg. Res. vol. 7, pp. 73-75.*
Overbeek, 1994, “Factors affecting transgenic animal production,” Transgenic animal technology, pp. 96-98.*
Wall, 1996, Theriogenology, vol. 45, pp. 57-68.*
Houdebine, 1994, J. Biotech. vol. 34, pp. 269-287.*
Kellum, 1991, Cell, vol. 64, pp. 941-950.*
WaIl, 1996, Theriogenology, vol. 45, pp. 57-68.
Abrams et al., “Programmed cell death during Drosophila embryogenesis,” Development, vol. 117, pp. 29-43 (1993).
Abstract, Finelli et al., “Alzheimer's Abeta peptide induces rough eye phenotype in Drosophila,” 42nd Annual Drosophila Research Conference, Mar. 2001.
Abstract, Finelli et al., “Beta-Amyloid Induced Neurodegeneration in the Drosophila Eye,” Neurobiology of Drosophila, CSHL Oct. 2001.
Abstract, Finelli et al., “Genetic analysis of Alzheimer's-related pathways in Drosophila,” Therapeutic Opportunities in Neurodegenerative Diseases, CSHL 2000.
Abstract, Lanoue et al., “Dominant phenotypes caused by overexpression of human amyloid precursor protein (APP) in flies,” 41st Annual Drosophila Research Conference, Mar. 2000.
Abstract, Lanoue, et al., “Dominant phenotypes caused by overexpression of human amyloid precursor protein (APP) in flies,” World Alzheimer Congress 2000.
Anderton et al., Does dysregulation of the Notch and wingless/Wnt pathways underlie the pathogenesis of Alzheimer's disease? Molecular Medicine Today, vol. 6, pp. 54-59 (2000).
Behl et al., “Amyloid beta peptide induces necrosis rather than apoptosis,” Brain Research, vol. 645, pp. 253-264 (1994).
BehI, C., “Apoptosis and Alzheimer's Disease,” J. Neural Transm, vol. 107, pp. 1325-1344 (2000).
Benzer, S., “Behavioral Mutants of Drosophila Isolated by Countercurrent Distribution,” PNAS, vol. 58, pp. 1112-1119 (1967).
Bertram et al., “Evidence for Genetic Linkage of Alzheimer's Disease to Chromosome 10q,” Science, vol. 290, pp. 2302-2303 (2000).
Blochlinger et al., “Primary structure and expression of a product from cut, a locus involved in specifying sensory organ identity in Drosophila,” Nature, vol. 333, pp. 629-635, (1988).
Boulianne et al., “Cloning and characterization of the Drosophila presenilin homologue,” Molecular Neuroscience, vol. 8, pp. 1025-1029 (1997).
Brand et al., “Targeted gene expression as a means of altering cell fates and generating dominant phenotypes,” Development, vol. 118, p. 401-415 (1993).
Brewer et al., “Age-related Toxicity to Lactate, Glutamate, and Beta-Amyloid in Cultured Adult Neurons,” Neurobiology of Aging, vol. 19(6), pp. 561-568 (1998).
Cagan et al., “The Emergence of Order in the Drosophila Pupal Retina,” Developmental Biology, vol. 136, pp. 346-362 (1989).
Cao et al., “A Transcriptively Active Complex of APP with Fe65 and Histone Acetyltransferase Tip60,” Science, vol. 293, pp. 115-120 (2001).
Cescato et al., “Increased Generation of Alternatively Cleaved Beta-Amyloid Peptides in Cells Expressing Mutants of the Amyloid Precursor Protein Defective in Endocytosis,” Journal of Neurochemistry, pp. 1131-1139 (2000).
Chan et al., “Presenilin-1 Mutations Increase Levels of Ryanodine Receptors and Calcium Release in PC12 Cells and Cortical Neurons,” Journal of Biological Chemistry, vol. 275(24), pp.18195-18200 (2000).
Chen et al., “Where do Alzheimer's Plaques and Tangles come from? Aging-induced Protein Degradation Inefficiency,” Frontiers in Bioscience, vol. 6, E1-11 (2001).
Citron et al., “Excessive production of amyloid beta-protein by peripheral cells of symptomatic and presymptomatic patients carrying the Swedish familial Alzheimer disease mutation,” Proc. Natl. Acad. Sci., vol. 91, pp. 11993-11997 (1994).
Citron et al., “Generation of Amyloid Beta Protein from Its Precursor Is Sequence Specific,” Neuron, vol. 14, pp. 661-670 (1995).
Citron et al., “Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice,” Nature Medicine, vol. 3(1), pp. 67-72 (1997).
Cook et al., “Alzheimer's Abeta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells,” Nature Medicine, vol. 3(9), pp. 1021-1023 (1997).
Cotman et al., “A Potential Role for Apoptosis in Neurodegeneration and Alzheimer's Disease,” Molecular Neurobiology, vol. 10, pp. 19-45 (1995).
Coughlan et al., “Factors influencing the processing and function of the amyloid beta precursor protein—a potential therapeutic target in Alzheimer's disease?” Pharmacology & Therapeutics, vol. 86, pp. 111-144 (2000).
Czech et al., “APP/Preseninlin interaction: The amino-terminus of presenilin 2 is able to interact with Abeta42 in vitro,” Society for Neurscience, vol. 25, 641.1999.
Dawson, V.L., “Of Flies and Mice,” Science, vol. 288, pp. 631-632 (2000).
De Strooper et al., “A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain,” Nature, vol. 398, pp. 518-522 (1999).
Deveraux et al., “lAP family proteins—suppressors of apoptosis,” Genes. Dev., vol. 13, pp. 239-252 (1999).
Diaz-Benjumea et al., “Interaction between Dorsal and Ventral Cells in the lmaginal Disc Directs Wing Development in Drosophila,” Cell, vol. 75, pp. 741-752 (1993).
Dyrks et al., “Generation of betaA4 from the amyloid protein precursor and fragments thereof,” FEBS Lett., vol. 335(1), pp. 89-93 (1993).
Ellis et al, “Expression of Drosophila glass protein and evidence for negative regulation of its activity in non-neuronal cells by another DNA-binding protein,” Development, vol. 119, pp. 855-865 (1993).
Engelender et al., “Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions,” Nature Genetics, vol. 22, pp. 110-114 (1999).
Engels, W.R., “A trans-Acting Product Needed for P Factor Transposition in Drosophila,” Science, vol. 226, pp. 1194-1196 (1984).
Ertekin-Taner, et al., “Linkage of Plasma ABeta42 to a Quantitative Locus on Chromosome 10 in Late-Onset Alzheimer's Disease Pedigrees,” Science, vol. 290, pp. 2303-2304 (2000).
Feany et al., “A Drosophila model of Parkinson's disease,” Nature, vol. 404, pp. 394-398 (2000).
Fernandez-Funez et al., “Identification of genes that modify ataxin-1-induced neurodegeneration,” Nature, vol. 408, pp. 101-106 (2000).
Flucher et al., “Distribution of Na+ Channels and Ankyrin in Neuromuscular Junctions is Complementary to That of Acetylcholine Receptors and the 43 kd Protein,” Neuron, vol. 3, pp. 163-175 (1989).
Fortini et al., “Modeling human neurodegenerative diseases in Drosophila on a wing and a prayer,” Trends Genet., vo
Cohen Dalia
Dengler Uwe Jochen
Finelli Alyce Lynn
Freuler Felix
Konsolaki Mary
Bautista Regina
Bertoglio Valarie
Novartis
Woitach Joseph
LandOfFree
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