Yeast screens for treatment of human disease

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving nucleic acid

Reexamination Certificate

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C435S254110, C435S254210

Reexamination Certificate

active

08039209

ABSTRACT:
Screening methods for identifying substances that provide therapeutic value for various diseases associated with protein misfolding are provided. Genetic and chemical screening methods are provided using a yeast system. The methods of the invention provide a rapid and cost-effective method to screen for compounds that prevent protein misfolding and/or protein fibril formation and/or protein aggregation which includes numerous neurodegenerative diseases including Parkinson's disease, Alzheimer's disease, Huntington's disease as well as non-neuronal diseases such as type 2 diabetes.

REFERENCES:
patent: 5492812 (1996-02-01), Vooheis
patent: 5547841 (1996-08-01), Marotta et al.
patent: 5643562 (1997-07-01), Kisilevsky et al.
patent: 5652092 (1997-07-01), Vitek et al.
patent: 5686288 (1997-11-01), MacDonald et al.
patent: 5693757 (1997-12-01), MacDonald et al.
patent: 5952217 (1999-09-01), Gorman et al.
patent: 5958721 (1999-09-01), Marshall et al.
patent: 5994084 (1999-11-01), Anderton et al.
patent: 6071694 (2000-06-01), Takashima et al.
patent: 6093549 (2000-07-01), Ross et al.
patent: 7045290 (2006-05-01), Lindquist et al.
patent: 2001/0006793 (2001-07-01), Bjornsti et al.
patent: 2002/0187157 (2002-12-01), Jensen et al.
patent: 2003/0022243 (2003-01-01), Kondejewski et al.
patent: 2003/0073610 (2003-04-01), Lindquist et al.
patent: 2005/0009019 (2005-01-01), Van Lueven et al.
patent: 2006/0147902 (2006-07-01), Lindquist et al.
patent: 1328814 (2006-10-01), None
patent: 2001/501802 (2008-02-01), None
patent: WO 91/04339 (1991-04-01), None
patent: WO 91/05044 (1991-04-01), None
patent: WO 93/03369 (1993-02-01), None
patent: WO 99/06545 (1999-02-01), None
patent: WO 99/29891 (1999-06-01), None
patent: WO 99/62548 (1999-12-01), None
patent: WO 01/02552 (2001-01-01), None
patent: WO 01/06989 (2001-02-01), None
patent: WO 01/23412 (2001-04-01), None
patent: WO 02/35237 (2002-05-01), None
patent: WO 02/065136 (2002-08-01), None
patent: WO 2005/005640 (2005-01-01), None
Adams et al., “Methods in Yeast Genetics,” A Cold Spring Harbor Laboratory Course Manual, 1997.
Borkovich et al,, “hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures,” Mol Cell Biol. 9:3919-3930, 1989.
Boucherie et al., “Differential synthesis of glyceraldehyde-3-phosphate dehydrogenase polypeptides in stressed yeast cells,” FEMS Microbiol Lett., 125:127-134, 1995.
Burke et al., “Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH,” Nat Med. 2:347-350, 1996.
Chai et al., “Analysis of the role of heat shock protein (Hsp)molecular chaperones in polyglutamine disease,” J Neurosci., 19:10338-10347, 1999.
Chai et al., “Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro,” Hum Mol Genet., 8:673-682, 1999.
Chen and Hochstrasser, “Biogenesis, structure and function of the yeast 20S proteasome,” Embo J., 14:2620-2630, 1995.
Cummings et al., “Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1,” Nat Genet., 19:148-154, 1998.
DeMarini et al., “The yeast SEN3 gene encodes a regulatory subunit of the 26S proteasome complex required for ubiquitin-dependent protein degradation in vivo,” Mol Cell Biol., 15:6311-6321, 1995.
Gething, Guidebook to molecular chaperones and protein folding catalysts. Oxford University Press, 1997.
Jana et al., “Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with trunacted N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity,” Hum Mol Genet., 9(13):2009-2018, 2000.
Kazantsev et al., “Insoluble detergent-resistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammalian cells,” Proc Natl Acad Sci U.S.A., 96: 11404-1 1409, 1999.
Kimura et al., “Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transuction pathways,” Science, 268:1362-1365, 1995.
Koo et al., “Amyloid diseases: Abnormal protein aggregation in neurodegeneration,” PNAS 96:9989-9990, 1999.
Krobitsch and Lindquist, “Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins,” Proc Natl Acad Sci U.S.A., 97(4):1589-1594, 2000.
Masison et al. “Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells,” Trends in Genetics, Elsevier Science Publishers, B.V. Amsterdam, NL, 12:14, 1996.
Moore et al., “Triplet repeats form secondary structures that escape DNA repair in yeast,” Proc. Natl. Acad. Sci. U.S.A., 96:1504-1509, 1999.
Muchowski et al., “Hsp70 and Hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils,” Proc. Natl. Acad. Sci. USA, 97:7841-7846, 2000.
Mumberg et al., “Regulatable promoters ofSaccharmoyce cerevisiae: comparison of transcriptional activity and their use for heterologous expression,” Nucleic Acids Res. 22:5767-5768, 1994.
Mumberg et al., “Yeast vectors for the controlled expression of heterolgous proteins in different genetic backgrounds,” Gene. 156:119-122, 1995.
Nathan and Lindquist, “Mutational analysis of HspPO function: interactions with a steroid receptor and a protein kinase,” Mol Cell Biol. 15:3917-3925, 1995.
Nathan et al., “Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of aSaccharomyces cerevisiaeHsp90 loss-of-function mutation,” Proc. Natl. Acad. Sci. U.S.A. 96:1409-1414, 1999.
Parsell and Lindquist, “The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins,” Annu. Rev. Genet. 27:437-496, 1993.
Parsell et al., “Protein disaggregation mediated by heat-shock protein Hsp104,” Nature. 372:475-478, 1994.
Parsell et al., “Saccharomyces cerevisiaeHsp104 protein,” J. Biol. Chem. 269(6):4480-4487, 1994.
Petko et al., “Hsp26 is not required for growth at high temperatures, nor for thermotolerance, spore development, or germination,” Cell., 45:885-894, 1986.
Saudou et al., “Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions,” Cell., 95:55-66, 1998.
Schweitzer et al., “Destabilization of CAG trinucleotide repeat tracts by mismatch repair mutations in yeast,” Hum Mol Genet. 6:349-355, 1997.
Stenoien et al., “Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone,” Hum Mol Genet., 8:731-741, 1999.
Stone and Craig, “Self-regulation of 70-kilodalton heat shock proteins inSaccharomyces cerevisiae,” Mol Cell Biol., 10:1622-1632, 1990.
Temussi et al., “From Alzheimer's to Huntington: why is a structural understanding so difficult,” EMBO Journal 22(3):355-361, 2003.
Tuite et al., “Maintenance and inheritance of yeast prions,” Trends in Genetics, Elsevier Science Publishers, B.V. Amsterdam, NL, 12:467-471, 1996.
Vogel et al., “Heat-shock proteins Hsp104 and Hsp70 reactivate mRNA splicing after heat inactivation,” Current Biology, 5:306-317, 1995.
Vonsattel et al., “Neuropathological classification of huntington's disease,” J Neuropathol Exp Neurol., 44:559-577, 1985.
Neystat et al., “Identification of alpha-synuclein interacting proteins in rat brain by yeast two-hybrid screen,” Database Biosis (Online), Biosciences Information Services, XP-002431841, Database Accession No. PREV200100070267, Society for Neuroscience Abstracts, 26:1-2, 2000.
Andoh et al., “Yeast Glycogen Synthase Kinase 3 is I

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