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Murine Amyloidosis: Immunologic Characterization of Amyloid Fibril Protein

Laboratory of Experimental Pathology, National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland 20014

Abstract

Immunization of rabbits with amyloid-laden murine tissue denatured with 6 M guanidine-HC1 produced antibodies to denatured purified murine amyloid fibril protein. Attempted immunization with native amyloid-laden murine tissues, however, failed to produce antibodies to any component unique to amyloid tissues, indicating that native murine amyloid was not immunogenic. Radioimmunoassay and immunofluorescence studies, nonetheless, demonstrated that native amyloid possessed antigenic determinants in common with denatured amyloid. A high degree of immunologic cross-reactivity was detected between extracts of amyloidotic tissues from different strains of mice regardless of the method of amyloid induction. Sera from amyloidotic mice were shown to contain a component capable of inhibiting the reaction between specific antibodies and purified amyloid protein.

Footnotes

¹ Present address: Johns Hopkins Medical School, 725 North Wolfe St., Baltimore, Maryland 21205.

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