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Titolo:
Disruption of pathologic amyloid beta-protein fibril assembly on the surface of cultured human cerebrovascular smooth muscle cells
Autore:
Van Nostrand, WE; Melchor, JP;
Indirizzi:
SUNY Stony Brook, Dept Med, Ctr Hlth Sci, Stony Brook, NY 11794 USA SUNY Stony Brook Stony Brook NY USA 11794 Sci, Stony Brook, NY 11794 USA SUNY Stony Brook, Dept Pathol, Ctr Hlth Sci, Stony Brook, NY 11794 USA SUNY Stony Brook Stony Brook NY USA 11794 Sci, Stony Brook, NY 11794 USA
Titolo Testata:
AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS
, volume: 8, anno: 2001, supplemento:, 1
pagine: 20 - 27
SICI:
1350-6129(200107)8:<20:DOPABF>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALZHEIMERS-DISEASE; AGGREGATION; PRECURSOR; NEUROTOXICITY; ANGIOPATHY; DEGENERATION; INHIBITION; INVITRO; ARREST;
Keywords:
amyloid beta-protein; fibrils; cerebrovascular smooth muscle cells;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Van Nostrand, WE SUNY Stony Brook, Dept Med, Ctr Hlth Sci, HSC T-15-081, Stony Brook, NY 11794 USA SUNY Stony Brook HSC T-15-081 Stony Brook NY USA 11794 SA
Citazione:
W.E. Van Nostrand e J.P. Melchor, "Disruption of pathologic amyloid beta-protein fibril assembly on the surface of cultured human cerebrovascular smooth muscle cells", AMYLOID, 8, 2001, pp. 20-27

Abstract

Cerebral amyloid beta -protein (A beta) angiopathy (CAA) is a common pathological feature of Alzheimer disease and several related disorders. In thiscondition, the accumulation of fibrillar A beta deposits is associated with degeneration of smooth muscle cells within the cerebral blood vessel wall. We have been using primary cultures of human cerebrovascular smooth muscle (HCSM) cells to investigate pathogenic mechanisms of A beta in CAA. The specific assembly of A beta fibrils on the surface of these cell types initiates several pathologic responses including increased expression and cell surface accumulation of the A beta precursor protein (A beta PP) and induction of apoptotic cell death. These pathologic responses are not observed with preparations of A beta that are assembled into fibrils in solution, further underscoring the significance of the fibril assembly process on the cellsurface. Since cell surface A beta fibril assembly is the key initiator ofthe cerebrovascular cellular pathology that is observed in vitro, inhibition of this process remains an attractive therapeutic target for CAA. We have tested the efficacy, of a variety of compounds that have been reported toinhibit A beta fibril assembly in solution and block the neurotoxic properties of A beta in vitro. The vast majority of these agents were ineffectivein inhibiting the cell surface fibrillar assembly of A beta and the subsequent pathologic responses in the cultured HCSM cells. This emphasizes the likely requirement of therapeutic, compounds that are effective in disrupting cell surface-driven A beta fibril assembly in the treatment of CAA.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/01/20 alle ore 14:47:01