Amyloid: journal of protein folding disorders vol:12 issue:3 pages:164-166
date:Anim Sci Grp Wageningen UR, NL-8200 AB Lelystad, Netherlands; Univ Tennessee, Grad Sch Med, Knoxville, TN USA; Univ Utrecht, Fac Vet Med, Dept Pathobiol, NL-3508 TD Utrecht, Netherlands
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.