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Titolo:
Mutant huntingtin forms in vivo complexes with distinct context-dependent conformations of the polyglutamine segment
Autore:
Persichetti, F; Trettel, F; Huang, CC; Fraefel, C; Timmers, HTM; Gusella, JF; MacDonald, ME;
Indirizzi:
Massachusetts Gen Hosp, Mol Neurogenet Unit, Charlestown, MA 02129 USA Massachusetts Gen Hosp Charlestown MA USA 02129 Charlestown, MA 02129 USA Univ Utrecht, Physiol Chem Lab, NL-3438 GD Utrecht, Netherlands Univ Utrecht Utrecht Netherlands NL-3438 GD 3438 GD Utrecht, Netherlands Univ Utrecht, Ctr Biomed Genet, NL-3438 GD Utrecht, Netherlands Univ Utrecht Utrecht Netherlands NL-3438 GD 3438 GD Utrecht, Netherlands
Titolo Testata:
NEUROBIOLOGY OF DISEASE
fascicolo: 5, volume: 6, anno: 1999,
pagine: 364 - 375
SICI:
0969-9961(199910)6:5<364:MHFIVC>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
INTRANUCLEAR NEURONAL INCLUSIONS; SIMPLEX VIRUS TYPE-1; AGGREGATES IN-VITRO; GLUTAMINE REPEATS; NEURODEGENERATIVE DISEASES; TISSUE TRANSGLUTAMINASE; LOCALIZATION; EXPRESSION; MECHANISM; PROTEIN;
Keywords:
Huntington's disease; huntingtin; aggregation; polyglutamine; 1F8 mAb;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: MacDonald, ME Massachusetts Gen Hosp, Mol Neurogenet Unit, Bldg 149,13th St, Charlestown, MA 02129 USA Massachusetts Gen Hosp Bldg 149,13th St Charlestown MA USA 02129
Citazione:
F. Persichetti et al., "Mutant huntingtin forms in vivo complexes with distinct context-dependent conformations of the polyglutamine segment", NEUROBIOL D, 6(5), 1999, pp. 364-375

Abstract

Huntington's disease (HD) is caused by an expanded glutamine tract, which confers a novel aggregation-promoting property on the 350-kDa huntingtin protein. Using specific antibodies, we have probed the structure of the polyglutamine segment in mutant huntingtin complexes formed in cell culture fromeither truncated or full-length protein, Complexes formed by a mutant amino terminal fragment most frequently entail a change in conformation that eliminates reactivity with the polyglutamine-specific mAb 1F8, coincident with production of insoluble aggregate. By contrast, complexes formed by the full-length mutant protein remain soluble and are invariably 1F8-reactive, indicating a soluble polyglutamine conformation. Therefore, aggregates in HDmay form by different biochemical mechanisms that invoke different possibilities for the pathogenic process. If pathogenesis is triggered by a truncated fragment, it probably involves the formation of an insoluble aggregate. However, the observation of soluble complexes in which an HD-specific pathogenic conformation of the glutamine tract remains accessible suggests thatpathogenesis could also be triggered at the level of full-length huntingtin by abnormal aggregation with normal or abnormal protein partners. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 10:21:24