Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
I-125-labeled ApoE binds competitively to beta(1-40) fibrils with pathological chaperone proteins
Autore:
LeVine, H;
Indirizzi:
Parke Davis Pharmaceut Res Div, Neurosci Therapeut, Ann Arbor, MI 48105 USA Parke Davis Pharmaceut Res Div Ann Arbor MI USA 48105 Arbor, MI 48105 USA
Titolo Testata:
AMYLOID-INTERNATIONAL JOURNAL OF EXPERIMENTAL AND CLINICAL INVESTIGATION
fascicolo: 2, volume: 7, anno: 2000,
pagine: 83 - 89
SICI:
1350-6129(200006)7:2<83:IABCTB>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALZHEIMERS AMYLOID-BETA; HUMAN APOLIPOPROTEIN-E; PEPTIDE A-BETA; P COMPONENT; IN-VITRO; DISEASE; COMPLEMENT; EXPRESSION; INHIBITION; MICE;
Keywords:
filtration; isoforms; Apo J; transthyretin; alpha2-macroglobulin; alpha1-antichymotrypsin; complement; apo B; apo A1;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: LeVine, H Parke Davis Pharmaceut Res Div, Neurosci Therapeut, 2800 Plymouth Rd, Ann Arbor, MI 48105 USA Parke Davis Pharmaceut Res Div 2800 Plymouth Rd Ann Arbor MI USA 48105
Citazione:
H. LeVine, "I-125-labeled ApoE binds competitively to beta(1-40) fibrils with pathological chaperone proteins", AMYLOID, 7(2), 2000, pp. 83-89

Abstract

Radiolabeled Apolipoprotein E (Apo E) was used in a competitive binding filtration assay to amyloid fibrils preformed from beta(I-40)peptide as a probe of the binding sites for proteins either found in senile plaques in Alzheimer's Disease brain or reported to be associated with the soluble peptide. Apo E, Apo J, Apo A-I, Apo B, laminin, complement components C3 and C4, and alpha 1-antichymotrypsin all displayed sub-micromolar apparent affinities for the Apo E binding site on fibrils. Transthyretin, alpha 2-macroglobulin, amyloid P protein, heparan sulfate proteoglycan, complement component C1q, chondroitin sulfate A, and GM1 ganglioside were much less effective. The epsilon 2, epsilon 3, and epsilon 4 isoforms of Apo E showed different affinities for fibrils and lipidation of these lipoproteins made little difference. Other fibrillar beta-peptides also bound Apo E, with A beta 40 (similar to) A beta 42 > A beta(12-28); A beta(25-35) = 0. A series of soluble beta-peptides and fragments failed to effect Apo E binding. Thus, both conformational and quaternary structural features are important in high affinitybinding of Apo E to A beta 40 fibrils. Different amyloid plaque-associatedmolecules apparently associate with alternative primary and secondary structural features on fibrils.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 02:43:29