{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,7]],"date-time":"2026-04-07T20:24:10Z","timestamp":1775593450061,"version":"3.50.1"},"reference-count":40,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2004,7,16]],"date-time":"2004-07-16T00:00:00Z","timestamp":1089936000000},"content-version":"vor","delay-in-days":2722,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[1997,2]]},"abstract":"<jats:p>C\u2010terminal fragments of the Alzheimer amyloid peptide (amino acids 29\u201340 and 29\u201342) have physico\u2010chemical properties related to those of the fusion peptides of viral proteins and they are able to induce the fusion of liposomes <jats:italic>in vitro.<\/jats:italic> We proposed that these properties could mediate a direct interaction of the amyloid peptide with cell membranes and account for part of the cytotoxicity of the amyloid peptide. In view of the epidemiologic and biochemical linkages between the pathology of Alzheimer's disease and apolipoprotein E (apoE) polymorphism, we examined the potential interaction between the three common apoE isoforms and the C\u2010terminal fragments of the amyloid peptide. We show that, at low concentration, only apoE2 and apoE3 are potent inhibitors of the amyloid peptide fusogenic and aggregational properties, whereas the apoE4 isoform has no effect. We further show that the protective effect of apoE is mediated by the formation of stable apoE\/amyloid peptide complexes, as determined by trypto\u2010phan emission fluorescence measurements and by gel electrophoresis. The interaction specificity between apoE2 and apoE3 and the amyloid fragments is demonstrated here, since other apolipoproteins (e.g. apolipoprotein A\u2010I and A\u2010II), with similar amphipathic structures, do not interact with the amyloid C\u2010terminal fragments. Finally, we show that, reciprocally, the amyloid peptide can interact directly with the apoE2 and apoE3 isoforms to decrease or perturb their normal association with lipids. These data suggest that the 29\u201040 and 29\u201342 domains of the amyloid peptide could be critical for the amyloid\u2010apoE interaction, and that apoE2 and apoE3 isoforms, but not apoE4, could play a protective role against the formation of amyloid aggregates and\/or against their interaction with cellular membranes.<\/jats:p>","DOI":"10.1111\/j.1432-1033.1997.00650.x","type":"journal-article","created":{"date-parts":[[2004,7,16]],"date-time":"2004-07-16T14:29:27Z","timestamp":1089988167000},"page":"650-659","source":"Crossref","is-referenced-by-count":28,"title":["Specific Modulation of the Fusogenic Properties of the Alzheimer \u03b2\u2010Amyloid Peptide by Apolipoprotein E Isoforms"],"prefix":"10.1111","volume":"243","author":[{"given":"Thierry","family":"Pillot","sequence":"first","affiliation":[]},{"given":"Marc","family":"Goethals","sequence":"additional","affiliation":[]},{"given":"Berlinda","family":"Vanloo","sequence":"additional","affiliation":[]},{"given":"Laurence","family":"Lins","sequence":"additional","affiliation":[]},{"given":"Robert","family":"Brasseur","sequence":"additional","affiliation":[]},{"given":"Joel","family":"Vandekerckhove","sequence":"additional","affiliation":[]},{"given":"Maryvonne","family":"Rosseneu","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2004,7,16]]},"reference":[{"key":"e_1_2_2_2_1","doi-asserted-by":"crossref","first-page":"6249","DOI":"10.1016\/S0021-9258(18)68779-4","article-title":"Human apolipoprotein E3 in aqueous solution. 11. 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