In mouse senile amyloidosis, apolipoprotein A-II polymerizes into amyloid f
ibrils (AApoAII) and deposits systemically. Peripheral injection of AApoAII
fibrils into young mice induces systemic amyloidosis (Higuchi et at, 1998)
. We isolated AApoAII amyloid fibrils from the livers of old R1.P1-Apoa2(c)
mice and injected them with feeding needles into the stomachs of young R1.
P1-Apoa2(c) mice for 5 consecutive days. After 2 months, all mice had AApoA
II deposits in the lamina propria of the small intestine. Amyloid depositio
n extended to the tongue, stomach, heart, and liver at 3 and 4 months after
feeding. AApoAII suspended in drinking water also induced amyloidosis. Amy
loid deposition was induced in young mice reared in the same cage for 3 mon
ths with old mice who had severe amyloidosis. Detection of AApoAII in feces
of old mice and induction of amyloidosis by the injection of an amyloid fr
action of feces suggested the propagation of amyloidosis by eating feces. H
ere, we substantiate the transmissibility of AApoAII amyloidosis and presen
t a possible pathogenesis of amyloidosis, ie, oral transmission of amyloid
fibril conformation, where we assert that exogenous amyloid fibrils act as
templates and change the conformation of endogenous amyloid protein to poly
merize into amyloid fibrils.