Targeting protein aggregation in neurodegeneration – lessons from polyglutamine disorders

Bibliography

• GATCHEL JR, ZOGHBI HY: Diseases of unstable repeat expansion: mechanisms and common principles. Nat. Rev. Genet. (2005) 6(10):743-755.
   PubMed Web of Science ®Google Scholar
• GUTEKUNST CA, NORFLUS F, HERSCH S: The neuropathology of Huntington’s disease. In: Huntington’s Disease. Bates G et al. (Eds), Oxford University Press, Oxford (2002):256-275.
   Google Scholar
• LA SPADA AR, WILSON EM, LUBAHN DB, HARDING AE, FISCHBECK KH: Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy. Nature (1991) 352(6330):77-79.
   PubMed Web of Science ®Google Scholar
• POLETTI A: The polyglutamine tract of androgen receptor: from functions to dysfunctions in motor neurons. Front. Neuroendocrinol. (2004) 25(1):1-26.
   PubMed Web of Science ®Google Scholar
• ATSUTA N, WATANABE H, ITO M et al.: Natural history of spinal and bulbar muscular atrophy (SBMA): a study of 223 Japanese patients. Brain (2006) 129(6):1446-1455.
   PubMed Web of Science ®Google Scholar
• GUSELLA JF, MACDONALD ME: Molecular genetics: unmasking polyglutamine triggers in neurodegenerative disease. Nat. Rev. Neurosci. (2000) 1(2):109-115.
   PubMedGoogle Scholar
• PERUTZ MF, JOHNSON T, SUZUKI M, FINCH JT: Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc. Natl. Acad. Sci. USA (1994) 91(12):5355-5358.
   PubMed Web of Science ®Google Scholar
• TROTTIER Y, LUTZ Y, STEVANIN G et al.: Polyglutamine expansion as a pathological epitope in Huntington’s disease and four dominant cerebellar ataxias. Nature (1995) 378(6555):403-406.
   PubMed Web of Science ®Google Scholar
• PAULSON HL, PEREZ MK, TROTTIER Y et al.: Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia Type 3. Neuron (1997) 19(2):333-344.
   PubMed Web of Science ®Google Scholar
• DAVIES SW, TURMAINE M, COZENS BA et al.: From neuronal inclusions to neurodegeneration: neuropathological investigation of a transgenic mouse model of Huntington’s disease. Philos. Trans. R. Soc. Lond. B. Biol. Sci. (1999) 354(1386):981-989.
   Google Scholar
• DIFIGLIA M, SAPP E, CHASE KO et al.: Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science (1997) 277(5334):1990-1993.
   PubMed Web of Science ®Google Scholar
• DAVIES SW, TURMAINE M, COZENS BA et al.: Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell (1997) 90(3):537-548.
   PubMed Web of Science ®Google Scholar
• SCHERZINGER E, LURZ R, TURMAINE M et al.: Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell (1997) 90(3):549-558.
   PubMed Web of Science ®Google Scholar
• NANCE MA: Clinical aspects of CAG repeat diseases. Brain Pathol. (1997) 7(3):881-900.
   PubMed Web of Science ®Google Scholar
• CUMMINGS CJ, REINSTEIN E, SUN Y et al.: Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice. Neuron (1999) 24(4):879-892.
   PubMed Web of Science ®Google Scholar
• SAUDOU F, FINKBEINER S, DEVYS D, GREENBERG ME: Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell (1998) 95(1):55-66.
   PubMed Web of Science ®Google Scholar
• KUEMMERLE S, GUTEKUNST CA, KLEIN AM et al.: Huntington aggregates may not predict neuronal death in Huntington’s disease. Ann. Neurol. (1999) 46(6):842-849.
   PubMed Web of Science ®Google Scholar
• TAYLOR JP, HARDY J, FISCHBECK KH: Toxic proteins in neurodegenerative disease. Science (2002) 296(5575):1991-1995.
   PubMed Web of Science ®Google Scholar
• ROSS CA, POIRIER MA: Opinion: what is the role of protein aggregation in neurodegeneration? Nat. Rev. Mol. Cell Biol. (2005) 6(11):891-898.
   PubMed Web of Science ®Google Scholar
• KOPITO RR: Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. (2000) 10(12):524-530.
   PubMed Web of Science ®Google Scholar
• SCHUBERT U, ANTON LC, GIBBS J et al.: Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature (2000) 404(6779):770-774.
   PubMed Web of Science ®Google Scholar
• BUKAU B, WEISSMAN J, HORWICH A: Molecular chaperones and protein quality control. Cell (2006) 125(3):443-451.
   PubMed Web of Science ®Google Scholar
• SHERMAN MY, GOLDBERG AL: Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron (2001) 29(1):15-32.
   PubMed Web of Science ®Google Scholar
• DOBSON CM: Protein folding and misfolding. Nature (2003) 426(6968):884-890.
   PubMed Web of Science ®Google Scholar
• MUCHOWSKI PJ, WACKER JL: Modulation of neurodegeneration by molecular chaperones. Nat. Rev. Neurosci. (2005) 6(1):11-22.
   PubMed Web of Science ®Google Scholar
• LEVINE B, YUAN J: Autophagy in cell death: an innocent convict? J. Clin. Invest. (2005) 115(10):2679-2688.
   PubMed Web of Science ®Google Scholar
• RAVIKUMAR B, VACHER C, BERGER Z et al.: Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington’s disease. Nat. Genet. (2004) 36(6):585-595.
   PubMed Web of Science ®Google Scholar
• YAMAMOTO A, CREMONA ML, ROTHMAN JE: Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway. J. Cell Biol. (2006) 172(5):719-731.
   PubMed Web of Science ®Google Scholar
• IWATA A, CHRISTIANSON JC, BUCCI M et al.: Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation. Proc. Natl. Acad. Sci. USA (2005) 102(37):13135-13140.
   PubMed Web of Science ®Google Scholar
• HARA T, NAKAMURA K, MATSUI M et al.: Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature (2006) 441(7095):885-889.
   PubMed Web of Science ®Google Scholar
• KOMATSU M, WAGURI S, CHIBA T et al.: Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature (2006) 441(7095):880-884.
   PubMed Web of Science ®Google Scholar
• RAVIKUMAR B, ACEVEDO-AROZENA A, IMARISIO S et al.: Dynein mutations impair autophagic clearance of aggregate-prone proteins. Nat. Genet. (2005) 37(7):771-776.
   PubMed Web of Science ®Google Scholar
• ROSS CA, POIRIER MA, WANKER EE, AMZEL M: Polyglutamine fibrillogenesis: the pathway unfolds. Proc. Natl. Acad. Sci. USA (2003) 100(1):1-3.
   PubMedGoogle Scholar
• POIRIER MA, LI H, MACOSKO J et al.: Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization. J. Biol. Chem. (2002) 277(43):41032-41037.
   PubMed Web of Science ®Google Scholar
• WACKER JL, ZAREIE MH, FONG H, SARIKAYA M, MUCHOWSKI PJ: Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer. Nat. Struct. Mol. Biol. (2004) 11(12):1215-1222.
   PubMed Web of Science ®Google Scholar
• SANCHEZ I, MAHLKE C, YUAN J: Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature (2003) 421(6921):373-379.
   PubMed Web of Science ®Google Scholar
• ARRASATE M, MITRA S, SCHWEITZER ES, SEGAL MR, FINKBEINER S: Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature (2004) 431(7010):805-810.
   PubMed Web of Science ®Google Scholar
• ADACHI H, KATSUNO M, MINAMIYAMA M et al.: Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein. J. Neurosci. (2003) 23(6):2203-2211.
   PubMed Web of Science ®Google Scholar
• WARRICK JM, CHAN HYL, GRAY-BOARD GL et al.: Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat. Genet. (1999) 23(4):425-428.
   PubMed Web of Science ®Google Scholar
• CUMMINGS CJ, SUN Y, OPAL P et al.: Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice. Hum. Mol. Genet. (2001) 10(14):1511-1518.
   PubMed Web of Science ®Google Scholar
• FUJIMOTO M, TAKAKI E, HAYASHI T et al.: Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models. J. Biol. Chem. (2005) 280(41):34908-34916.
   PubMed Web of Science ®Google Scholar
• SUPKO JG, HICKMAN RL, GREVER MR, MALSPEIS L: Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent. Cancer Chemother. Pharmacol. (1995) 36(4):305-315.
   PubMed Web of Science ®Google Scholar
• STEBBINS CE, RUSSO AA, SCHNEIDER C et al.: Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell (1997) 89(2):239-250.
   PubMed Web of Science ®Google Scholar
• SITTLER A, LURZ R, LUEDER G et al.: Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington’s disease. Hum. Mol. Genet. (2001) 10(12):1307-1315.
   PubMed Web of Science ®Google Scholar
• LA SPADA AR, WEYDT P: Targeting toxic proteins for turnover. Nat. Med. (2005) 11(10):1052-1053.
   PubMed Web of Science ®Google Scholar
• WAZA M, ADACHI H, KATSUNO M et al.: 17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration. Nat. Med. (2005) 11(10):1088-1095.
   PubMed Web of Science ®Google Scholar
• HEISER V, SCHERZINGER E, BOEDDRICH A et al.: Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: implications for Huntington’s disease therapy. Proc. Natl. Acad. Sci. USA (2000) 97(12):6739-6744.
   PubMed Web of Science ®Google Scholar
• TANAKA M, MACHIDA Y, NIU S et al.: Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington’s disease. Nat. Med. (2004) 10(2):148-154.
   PubMed Web of Science ®Google Scholar
• TANAKA M, MACHIDA Y, NUKINA N: A novel therapeutic strategy for polyglutamine diseases by stabilizing aggregation-prone proteins with small molecules. J. Mol. Med. (2005) 83(5):343-352.
   PubMed Web of Science ®Google Scholar
• BODNER RA, OUTEIRO TF, ALTMANN S et al.: Pharmacological promotion of inclusion formation: a therapeutic approach for Huntington’s and Parkinson’s diseases. Proc. Natl. Acad. Sci. USA (2006) 103(11):4246-4251.
   PubMedGoogle Scholar
• ZU T, DUVICK LA, KAYTOR MD et al.: Recovery from polyglutamine-induced neurodegeneration in conditional SCA1 transgenic mice. J. Neurosci. (2004) 24(40):8853-8861.
   PubMed Web of Science ®Google Scholar
• YAMAMOTO A, LUCAS JJ, HEN R: Reversal of neuropathology and motor dysfunction in a conditional model of Huntington’s disease. Cell (2000) 101(1):57-66.
   PubMed Web of Science ®Google Scholar
• BONINI NM, LA SPADA AR: Silencing polyglutamine degeneration with RNAi. Neuron (2005) 48(5):715-718.
   PubMedGoogle Scholar
• HARPER SQ, STABER PD, HE X et al.: RNA interference improves motor and neuropathological abnormalities in a Huntington’s disease mouse model. Proc. Natl. Acad. Sci. USA (2005) 102(16):5820-5825.
   PubMed Web of Science ®Google Scholar
• XIA H, MAO Q, ELIASON SL et al.: RNAi suppresses polyglutamine-induced neurodegeneration in a model of spinocerebellar ataxia. Nat. Med. (2004) 10:816-820.
   PubMed Web of Science ®Google Scholar
• MILLER TM, KASPAR BK, KOPS GJ et al.: Virus-delivered small RNA silencing sustains strength in amyotrophic lateral sclerosis. Ann. Neurol. (2005) 57(5):773-776.
   PubMed Web of Science ®Google Scholar
• RALPH GS, RADCLIFFE PA, DAY DM et al.: Silencing mutant SOD1 using RNAi protects against neurodegeneration and extends survival in an ALS model. Nat. Med. (2005) 11:429-433.
   PubMed Web of Science ®Google Scholar
• RAOUL C, ABBAS-TERKI T, BENSADOUN JC et al.: Lentiviral-mediated silencing of SOD1 through RNA interference retards disease onset and progression in a mouse model of ALS. Nat. Med. (2005) 11(4):423-428.
   PubMed Web of Science ®Google Scholar
• BRUJIN LI, MILLER TM, CLEVELAND DW: Unraveling the mechanisms involved in motor neuron degeneration in ALS. Ann. Rev. Neurosci. (2004) 27:723-749.
   PubMed Web of Science ®Google Scholar
• CLEMENT AM, NGUYEN MD, ROBERTS EA et al.: Wild-type nonneuronal cells extend survival of SOD1 mutant motor neurons in ALS mice. Science (2003) 302(5642):113-117.
   PubMed Web of Science ®Google Scholar
• GARDEN GA, LIBBY RT, FU YH et al.: Polyglutamine-expanded ataxin-7 promotes non-cell-autonomous purkinje cell degeneration and displays proteolytic cleavage in ataxic transgenic mice. J. Neurosci. (2002) 22(12):4897-4905.
   PubMedGoogle Scholar
• GIORGINI F, GUIDETTI P, NGUYEN Q, BENNETT SC, MUCHOWSKI PJ: A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington’s disease. Nat. Genet. (2005) 37(5):526-531.
   PubMed Web of Science ®Google Scholar
• SHIN JY, FANG ZH, YU ZX et al.: Expression of mutant huntingtin in glial cells contributes to neuronal excitotoxicity. J. Cell. Biol. (2005) 171(6):1001-1012.
   PubMed Web of Science ®Google Scholar
• ROTHSTEIN JD, PATEL S, REGAN MR et al.: Beta-lactam antibiotics offer neuroprotection by increasing glutamate transporter expression. Nature (2005) 433(7021):73-77.
   PubMed Web of Science ®Google Scholar
• DEININGER M, BUCHDUNGER E, DRUKER BJ: The development of imatinib as a therapeutic agent for chronic myeloid leukemia. Blood (2005) 105(7):2640-2653.
   PubMed Web of Science ®Google Scholar