Ls. Perlmutter et al., LOCALIZATION OF AMYLOID-P COMPONENT IN HUMAN BRAIN - VASCULAR STAINING PATTERNS AND ASSOCIATION WITH ALZHEIMERS-DISEASE LESIONS, Journal of comparative neurology, 352(1), 1995, pp. 92-105
Amyloid P component is a normal serum protein that is highly conserved
across phylogeny. Although it resembles the classic acute-phase react
ant C-reactive protein, and is considered to be a normal extracellular
matrix component, its physiologic role in humans is unknown. Amyloid
P component is also colocalized with accumulations of all recognized f
orms of amyloid. The present study uses light and electron microscopy
to compare the cerebral localization of amyloid P component in cases w
ith (n=19) and without (n=15) Alzheimer's disease (AD). In non-AD case
s, amyloid P component was predominantly localized to the cerebrovascu
lature. Perivascular staining was observed in most cases, more so in t
he white than in the gray matter. In AD cases, amyloid P component was
localized to all three characteristic histopathologic lesions, namely
, neurofibrillary tangles, senile plaques, and amyloid angiopathy. Fur
thermore, in cases with prominent staining of gray matter parenchymal
lesions, intravascular staining was decreased. Given the fixation and
processing methods used, amyloid P component was never seen to be loca
lized to the cerebrovascular basement membrane. These data argue again
st amyloid P component's postulated role as the anchor for vascular P-
amyloid deposition. Because there is no evidence for intrinsic amyloid
P component production in brain, its perivascular and parenchymal dis
tributions suggest either compromise of the blood-brain barrier or tra
nsport across vascular endothelium. (C) 1995 Wiley-Liss, Inc.