{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,16]],"date-time":"2026-05-16T05:24:47Z","timestamp":1778909087869,"version":"3.51.4"},"reference-count":38,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2003,5,22]],"date-time":"2003-05-22T00:00:00Z","timestamp":1053561600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Neurochemistry"],"published-print":{"date-parts":[[2003,6]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Vaccination against human beta\u2010amyloid peptide (A\u03b2) has been shown to remove the amyloid burden produced in transgenic mice overexpressing the mutated human amyloid precursor protein (APP) gene. For human beings, the efficiency of this therapeutic strategy has to take into account the specificities of human amyloid, especially at the early stages of \u2018sporadic\u2019 Alzheimer's disease (AD). A\u03b2 40\/42 were previously quantified in tissues from our well\u2010established brain bank, including non\u2010demented individuals with both mild amyloid and tau pathologies, hence corresponding to the earliest stages of Alzheimer pathology. Herein, we have adapted a proteomic method combined with western blotting and mass spectrometry for the characterization of insoluble A\u03b2 extracted in pure\u2010formic acid. We demonstrated that amino\u2010truncated A\u03b2 species represented more than 60% of all A\u03b2 species, not only in full blown AD, but also, and more interestingly, at the earliest stage of Alzheimer pathology. At this stage, A\u03b2 oligomers were exclusively made of A\u03b2\u201042 species, most of them being amino\u2010truncated. Thus, our results strongly suggest that amino\u2010truncated A\u03b2\u201042 species are instrumental in the amyloidosis process. In conclusion, a vaccine specifically targeting these pathological amino\u2010truncated species of A\u03b2\u201042 are likely to be doubly beneficial, by inducing the production of specific antibodies against pathological A\u03b2 products that are, in addition, involved in the early and basic mechanisms of amyloidosis in humans.<\/jats:p>","DOI":"10.1046\/j.1471-4159.2003.01818.x","type":"journal-article","created":{"date-parts":[[2003,6,3]],"date-time":"2003-06-03T10:18:04Z","timestamp":1054635484000},"page":"1581-1591","source":"Crossref","is-referenced-by-count":169,"title":["Truncated beta\u2010amyloid peptide species in pre\u2010clinical Alzheimer's disease as new targets for the vaccination 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