In Alzheimer's disease, the main component of amyloid deposits is a 39–43 amino acid peptide referred to as amyloid peptide or A β. A crucial issue in the study of this disorder is to define the sequence of events that lead to amyloid deposition. In the present study, a new approach was developed that allows to specifically solubilize A β peptide trapped within amyloid deposits and to quantify its amount by dot-blot immunoassay. The present method also permits to isolate components tightly bound to A β and that are likely to catalyze its aggregation. Biochemical A β quantitation was performed in 4 Brodmann areas from 17 elderly individuals exhibiting different degrees of amyloidosis. In parallel, classical neuropathology was done by histochemical and immunohistochemical methods. A β amounts (pmol) were correlated to the number of amyloid deposits determined by neuropathology showing high statistical significance. Moreover, amyloid-binding proteins including apolipoprotein E and heparan sulfate proteoglycans were also found associated to A β in the amyloid preparation. The present biochemical procedure is a new and reliable method to quantify amyloid deposition in brain. Furthermore, it allows to detect amyloid-associated components such as apolipoprotein E, that may be involved in the pathological process of amyloidogenesis.

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{{Explor lien
   |wiki=    Wicri/Sante
   |area=    ParkinsonFranceV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     ISTEX:B8401D072C64B3BB7B811CBB9F6126FB98E98D9F
   |texte=   Quantitation of Alzheimer's amyloid peptide and identification of related amyloid proteins by dot-blot immunoassay
}}