Chemical typing of porcine systemic amyloid as AA-amyloid.
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.
Niewold
Theo A
TA
Animal Sciences Group of Wageningen UR, AB Lelystad, The Netherlands. theo.niewold@wur.nl
Murphy
Charles L
CL
Toussaint
Mathilda J M
MJ
Solomon
Alan
A
Gruys
Erik
E
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry* / Q000145:classification* / Q000235:genetics / Q000378:metabolism; D000686:Amyloidosis / Q000175:diagnosis / Q000209:etiology / Q000662:veterinary*; D000818:Animals; D000906:Antibodies; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D009395:Nephritis, Interstitial / Q000378:metabolism / Q000662:veterinary; D013552:Swine
D000682:Amyloid; D000906:Antibodies