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Titolo:
Assembly of Alzheimer's amyloid-beta fibrils and approaches for therapeutic intervention
Autore:
Yang, DS; Serpell, LC; Yip, CM; McLaurin, J; Chrishti, MA; Horne, P; Boudreau, L; Kisilevsky, R; Westaway, D; Fraser, PE;
Indirizzi:
Univ Toronto, Ctr Res Neurodegenerat Dis, Toronto, ON M5S 3H2, Canada UnivToronto Toronto ON Canada M5S 3H2 t Dis, Toronto, ON M5S 3H2, Canada Univ Cambridge, Struct Med Unit, Cambridge Inst Med Res, Wellcome Trust Ctr Mol Mech Dis, Cambridge CB2 2XY, England Univ Cambridge Cambridge England CB2 2XY Dis, Cambridge CB2 2XY, England Univ Toronto, Dept Chem Engn, Toronto, ON, Canada Univ Toronto Toronto ONCanada onto, Dept Chem Engn, Toronto, ON, Canada Univ Toronto, Dept Appl Chem, Toronto, ON, Canada Univ Toronto Toronto ONCanada onto, Dept Appl Chem, Toronto, ON, Canada Univ Toronto, Dept Biochem, Toronto, ON, Canada Univ Toronto Toronto ON Canada oronto, Dept Biochem, Toronto, ON, Canada Univ Toronto, Inst Biomed Engn, Toronto, ON, Canada Univ Toronto Toronto ON Canada to, Inst Biomed Engn, Toronto, ON, Canada Univ Toronto, Lab Med & Pathobiol, Toronto, ON, Canada Univ Toronto Toronto ON Canada Lab Med & Pathobiol, Toronto, ON, Canada Queens Univ, Kingston Gen Hosp, Dept Pathol, Syl & Molly Apps Res Ctr, Kingston, ON K7L 3N6, Canada Queens Univ Kingston ON Canada K7L 3N6 Ctr, Kingston, ON K7L 3N6, Canada Queens Univ, Kingston Gen Hosp, Dept Biochem, Syl & Molly Apps Res Ctr, Kingston, ON K7L 3N6, Canada Queens Univ Kingston ON Canada K7L 3N6 Ctr, Kingston, ON K7L 3N6, Canada Univ Toronto, Dept Med Biophys, Toronto, ON, Canada Univ Toronto Toronto ON Canada to, Dept Med Biophys, Toronto, ON, Canada
Titolo Testata:
AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS
, volume: 8, anno: 2001, supplemento:, 1
pagine: 10 - 19
SICI:
1350-6129(200107)8:<10:AOAAFA>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
X-RAY-DIFFRACTION; PROTEASE INHIBITOR ALPHA-1-ANTICHYMOTRYPSIN; HEPARAN-SULFATE PROTEOGLYCAN; A-BETA; PRECURSOR PROTEIN; CONGO RED; IN-VIVO; NEUROFIBRILLARY TANGLES; PEPTIDE POLYMERIZATION; BASEMENT-MEMBRANE;
Keywords:
amyloid-beta; Alzheimer's disease; heparan sulfate proteoglycans; senile plaques; fibril formation; transgenic mice;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
87
Recensione:
Indirizzi per estratti:
Indirizzo: Fraser, PE Univ Toronto, Ctr Res Neurodegenerat Dis, 6 Queens Pk Cresent W,Tanz Neurosci Bldg, Toronto, ON M5S 3H2, Canada Univ Toronto 6 Queens Pk Cresent W,Tanz Neurosci Bldg Toronto ON Canada M5S 3H2
Citazione:
D.S. Yang et al., "Assembly of Alzheimer's amyloid-beta fibrils and approaches for therapeutic intervention", AMYLOID, 8, 2001, pp. 10-19

Abstract

Amyloid plaques are the principal features of Alzheimer disease (AD) pathology and are considered to be a major factor in the disease process. These fibrillar deposits are composed primarily of the 40-42 residue amyloid-beta(A beta) peptide which is a proteolytic product of a larger membrane precursor protein. Electron microscopy and X-ray diffraction have revealed that the mature amyloid fibrils are assembled as a highly P-sheet polymer that has a well-defined protofilament quaternary structure. This organization is observed for amyloid fibrils from a wide variety of disorders and appears to represent a structural super family. Amyloid plaques also contain a number of other components such as proteogylcans that contain highly sii fated glycosaminoglycan (GAG) chains. These amyloid-associated elements may contribute to the aggregation and/or stabilization of A beta as insoluble fibrils. We have recently developed an aggressive model for A beta plaque formation in transgenic mice that exhibits an "early-onset" phenotype. Immunocytochemistry has demonstrated that even with this rapid progression, A beta deposits within the neuropil and cerebrovascular system till co-localize with heparan sulfate proteoglycans (HSPG). These findings indicate a number of structural features that can be targeted as potential sites for the development of amyloid inhibitors. In addition, the use of small compounds that interfere with the proteoglycan-amyloid pathway may be effective therapeutic agents that can be assessed through the use of these transgenic models.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 11:15:45