Chemical typing of porcine systemic amyloid as AA-amyloid

T.A. Niewold, C.L. Murphy, M.J.M. Toussaint, A. Solomon, E. Gruys

    Research output: Contribution to journalArticleAcademicpeer-review

    7 Citations (Scopus)


    Systemic AA amyloidosis is frequently reported in a wide variety of domestic and wild animal species. Porcine amyloidosis is rare and the amyloid has not been typed chemically thus far. In the present study, we have extracted porcine amyloid from formalin-fixed tissue sections. By subsequent amino acid sequencing, an N-terminal fragment was obtained identifying porcine systemic amyloid as AA amyloid. The N-terminal sequence had a great homology to bovine and ovine SAA1, suggesting that pig AA amyloid is derived from the systemic isoform of SAA. It is argued that the low incidence of amyloidosis in pigs is not likely to be attributed to unique features of porcine amyloid precursor protein. Elucidation of the basis for the high apparent resistance of pigs against amyloidosis may yield important clues for treatment and prevention of amyloidosis in other species. This is the first report on chemical identification of porcine amyloid.
    Original languageEnglish
    Pages (from-to)164-166
    JournalAmyloid: international journal of experimental and clinical investigation
    Issue number3
    Publication statusPublished - 2005


    • pathogenesis
    • proteins
    • rat


    Dive into the research topics of 'Chemical typing of porcine systemic amyloid as AA-amyloid'. Together they form a unique fingerprint.

    Cite this