C. Rocken et al., PORTAL AMYLOID - NOVEL AMYLOID DEPOSITS IN GASTROINTESTINAL VEINS, Archives of pathology and laboratory medicine, 120(11), 1996, pp. 1044-1051
Citations number
41
Categorie Soggetti
Pathology,"Medical Laboratory Technology","Medicine, Research & Experimental
Objective.-To specify uncharacterized amyloid deposits in gastrointest
inal vessels of the elderly. Materials and Methods.-The gastrointestin
al tracts from 110 consecutive autopsies of individuals aged 85 years
and older were examined for amyloid using Congo red staining. Immunohi
stochemical classification of the amyloid deposits was conducted using
antisera directed against amyloid A, apolipoprotein A-I, apolipoprote
in A-II, apolipoprotein B, apolipoprotein C-I, lysozyme, lambda and ka
ppa light chain amyloid fibril proteins, transthyretin, beta(2)-microg
lobulin, and amyloid P component. Electron microscopic examination ass
essed the ultrastructural features. Results.-Thirty-eight (35%) of the
110 cases had gastrointestinal amyloid deposits. In 17 cases the amyl
oid fibril proteins were defined immunohistochemically. In five cases
(5%) the amyloid could not be classified because amyloid deposits were
not present in the deeper serial sections used for immunohistochemist
ry. In 13 cases (11%) the vascular amyloid deposits could not be chara
cterized because they did not demonstrate immunoreactivity with any of
a panel of antibodies specific for the fibril proteins of all major e
xtracerebral amyloids. In three individual cases, the vascular amyloid
deposits showed variable immunoreactivity, with deposits being negati
ve in some vessels. The immunohistochemically nonreactive vascular amy
loid in these 16 cases had several consistent features: it affected on
ly vessels of the small and large intestine, it was limited to mesente
ric veins, it consisted of small dot- or comma-like deposits located i
n close proximity to fragmented elastic fibers, and it demonstrated in
consistent immunostaining for amyloid P component. Conclusions.-The si
milar morphologic characteristics of nonreactive gastrointestinal amyl
oid deposits, which we have designated ''portal amyloid,'' suggest a c
ommon origin. Determination of whether portal amyloid represents a new
type of amyloid will require chemical analysis.