Anti-oligomeric single chain variable domain antibody differentially affects huntingtin and α-synuclein aggregates

FEBS Letters

Volumn 582, Issue 4, 2008, Pages 517-522

  Nannenga, Brent L ^a   Zameer, Andleeb ^a,b   Sierks, Michael R ^a  

^a Arizona State University   (United States)

^b MOUNT SINAI SCHOOL OF MEDICINE   (United States)

Author keywords

synuclein; Atomic force microscopy; Huntingtin; Oligomer; Single chain variable domain antibody fragment; Toxicity

Indexed keywords

ALPHA SYNUCLEIN; HUNTINGTIN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY;

ARTICLE; ATOMIC FORCE MICROSCOPY; CONTROLLED STUDY; HUMAN; HUMAN CELL; HUNTINGTON CHOREA; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS;

ALPHA-SYNUCLEIN; BIOPOLYMERS; HUMANS; IMMUNOGLOBULIN FRAGMENTS; MICROSCOPY, ATOMIC FORCE; NERVE TISSUE PROTEINS; NUCLEAR PROTEINS;

EID: 39149092670     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.01.014     Document Type: Article

References (18)

1. Macdonald M.E., Ambrose C.M., Duyao M.P., Myers R.H., Lin C., Srinidhi L., Barnes G., Taylor S.A., James M., Groot N., Macfarlane H., Jenkins B., Anderson M.A., Wexler N.S., Gusella J.F., Bates G.P., Baxendale S., Hummerich H., Kirby S., North M., Youngman S., Mott R., Zehetner G., Sedlacek Z., Poustka A., Frischauf A.M., Lehrach H., Buckler A.J., Church D., Doucettestamm L., Odonovan M.C., Ribaramirez L., Shah M., Stanton V.P., Strobel S.A., Draths K.M., Wales J.L., Dervan P., Housman D.E., Altherr M., Shiang R., Thompson L., Fielder T., Wasmuth J.J., Tagle D., Valdes J., Elmer L., Allard M., Castilla L., Swaroop M., Blanchard K., Collins F.S., Snell R., Holloway T., Gillespie K., Datson N., Shaw D., and Harper P.S. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntingtons-disease chromosomes. Cell 72 (1993) 971-983
2. Rubinsztein D.C., Leggo J., Coles R., Almqvist E., Biancalana V., Cassiman J.J., Chotai K., Connarty M., Craufurd D., Curtis A., Curtis D., Davidson M.J., Differ A.M., Dode C., Dodge A., Frontali M., Ranen N.G., Stine O.C., Sherr M., Abbott M.H., Franz M.L., Graham C.A., Harper P.S., Hedreen J.C., Jackson A., Kaplan J.C., Losekoot M., MacMillan J.C., Morrison P., Trottier Y., Novelletto A., Simpson S.A., Theilmann J., Whittaker J.L., Folstein S.E., Ross C.A., and Hayden M.R. Phenotypic characterization of individuals with 30-40 CAG repeats in the Huntington disease (HD) gene reveals HD cases with 36 repeats and apparently normal elderly individuals with 36-39 repeats. Am. J. Human Genet. 59 (1996) 16-22
3. Kieburtz K., Macdonald M., Shih C., Feigin A., Steinberg K., Bordwell K., Zimmerman C., Srinidhi J., Sotack J., Gusella J., and Shoulson I. Trinucleotide repeat length and progression of illness in Huntingtons-disease. J. Med. Genet. 31 (1994) 872-874
4. Haass C., and Selkoe D.J. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat. Rev. Mol. Cell Biol. 8 (2007) 101-112
5. DiFiglia M., Sapp E., Chase K.O., Davies S.W., Bates G.P., Vonsattel J.P., and Aronin N. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277 (1997) 1990-1993
6. Arrasate M., Mitra S., Schweitzer E.S., Segal M.R., and Finkbeiner S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431 (2004) 805-810
7. Glabe C.G., and Kayed R. Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis. Neurology 66 (2006) S74-S78
8. McLean C.A., Cherny R.A., Fraser F.W., Fuller S.J., Smith M.J., Beyreuther K., Bush A.I., and Masters C.L. Soluble pool of A beta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann. Neurol. 46 (1999) 860-866
9. Sanchez I., Mahlke C., and Yuan J.Y. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature 421 (2003) 373-379
10. Kayed R., Head E., Thompson J.L., McIntire T.M., Milton S.C., Cotman C.W., and Glabe C.G. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300 (2003) 486-489
11. Glabe C.G. Common mechanisms of amyloid oligomer pathogenesis in degenerative disease. Neurobiol. Aging 27 (2006) 570-575
12. Emadi S., Barkhordarian H., Wang M.S., Schulz P., and Sierks M.R. Isolation of a human single chain antibody fragment against oligomeric alpha-synuclein that inhibits aggregation and prevents alpha-synuclein-induced toxicity. J. Mol. Biol. 368 (2007) 1132-1144
13. Scherzinger E., Lurz R., Turmaine M., Mangiarini L., Hollenbach B., Hasenbank R., Bates G.P., Davies S.W., Lehrach H., and Wanker E.E. Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell 90 (1997) 549-558
14. Zameer A., Schulz P., Wang M.S., and Sierks M.R. Single chain Fv antibodies against the 25-35 Abeta fragment inhibit aggregation and toxicity of Abeta42. Biochemistry 45 (2006) 11532-11539
15. Lambert M.P., Velasco P.T., Chang L., Viola K.L., Fernandez S., Lacor P.N., Khuon D., Gong Y.S., Bigio E.H., Shaw P., De Felice F.G., Krafft G.A., and Klein W.L. Monoclonal antibodies that target pathological assemblies of A beta. J. Neurochem. 100 (2007) 23-35
16. Manoutcharian K., Acero G., Munguia M.E., Montero J.A., Govezensky T., Cao C., Ugen K., and Gevorkian G. Amyloid-beta peptide-specific single chain Fv antibodies isolated from an immune phage display library. J. Neuroimmunol. 145 (2003) 12-17
17. Zhou C., Emadi S., Sierks M.R., and Messer A. A human single-chain Fv intrabody blocks aberrant cellular effects of overexpressed alpha-synuclein. Mol. Ther. 10 (2004) 1023-1031
18. Wolfgang W.J., Miller T.W., Webster J.M., Huston J.S., Thompson L.M., Marsh J.L., and Messer A. Suppression of Huntington's disease pathology in Drosophila by human single-chain Fvantibodies. Proc. Nat. Acad. Sci. USA 102 (2005) 11563-11568