No abstract

Abstract. Generalized amyloidosis was diagnosed post-mortem in a mountain gazelle (Guzdlu guz~llu). To test whether the amyloid deposits consisted of amyloid-A fibril protein a series of monoclonal and polyclonal antibodies directed against amyloid-A fibril protein of different species was applied to formalin-fixed paraffin sections using the indirect immunoperoxidase technique. The immunohistochemical results showed a moderate cross-reaction of gazelle amyloid with human. murine. hamster, and canine amyloid-A fibril protein. A strong cross-reaction. however, was found with one of two monoclonal anti-human amyloid-A antibodies and with an antiserum against bovine amyloid-A fibril protein, the amyloid fibril protein of another ungulate. These results demonstrate the presence of amyloid-A fibril protein in the gazelle amyloid and illustrate the diagnostic value of cross-reacting anti-amyloid-A antibodies for the identification of amyloid-A-amyloidosis in species and in individuals in which amyloid has not yet been examined.

Amyloid fibrils were isolated from the renal papillae and glomeruli of cows with spontaneous AA amyloidosis. The fibrils were solubilized by treatment with guanidine hydrochloride (Gu HCl) and subjected to gel filtration on Sephacryl S-200. Two other fractions were obtained beside the void volume and the AA fractions. Reaggregation studies were performed by dialysing the fractions, separately or in combinations, against Gu-HCl-free solutions. Protein AA alone (about 10 kd) appeared not to precipitate. The other fractions alone and the combinations of fractions tested formed precipitates. The precipitates containing all fractions (including protein AA) or protein AA plus a fraction containing a 19- and a 23-kd protein revealed congophilic green birefringent fibrillar material. Dialysis against acidic and calcium-containing solutions gave the best results. Amyloid fibril-like material was visible on electron microscopic examination. The amino acid composition of the 19 + 23-kd material appeared to be slightly different from protein AA and evidently unlike SAP. On immunofluorescence-absorbance studies the 19 + 23-kd material appeared evidently unlike protein AA and SAP. From these findings it is concluded that for spontaneous formation of AA amyloid fibrils other non-AA proteins are necessary.

No abstract

No abstract