作者: T. Wisniewski , G. Gallo , J. Ghiso , B. Frangione , Nam-Ho Choi-Miura
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摘要: Immunohistochemical and biochemical studies have demonstrated several different proteins in amyloid deposits that are not intrinsic components of the fibril itself but may play a role their deposition formation. We compared distribution amyloid-associated proteins, ie, P component, apolipoprotein-E, apolipoprotein-J, vitronectin, amyloids, particular light chain amyloid, with those nonamyloid monoclonal immunoglobulin, which be considered form preamyloid disease. Although 100% specimens (7 A, 15 immunoglobulin chain, 1 transthyretin) had component apolipoprotein-E (2 10 co-localized primary protein, none cases (14 disease 6 heavy disease) only 11 apolipoprotein-E. On other hand, staining for apolipoprotein-J vitronectin was positive deposits. The association between presence fibrillar absence nonfibrillar suggest these process fibrillogenesis. This lends support previously proposed concept functions as pathological chaperone by altering conformation amyloidogenic proteins.