Relationship between non-fibrillary amyloid precursors and cell processes in the cortical neuropil of Alzheimer patients.
We examined the ultrastructural localization of amyloid beta-protein in 8 Alzheimer neocortical biopsies. Intense immunoreactivity was located extracellularly on amyloid fibrils and amorphous material. Amorphous labelled material was also found in cell processes. No ultrastructural cell marker, such as glial fibrils, glycogen, tubules, paired helical filaments (PFHs) or synaptic vesicles could be seen in these processes that could allow their identification as glial processes, neurites or presynaptic terminals, respectively; occasional membrane stacks were observed. These findings suggest that preamyloid deposits are related to cell processes and, by elimination, that postsynaptic terminals may be involved in abnormal metabolism of the amyloid fibril precursors.
Laboratoire de Neurohistologie EPHE, U.106 INSERM, La Salpêtrière, Paris, France.
K H
KH
el Hachimi
L
L
Verga
G
G
Giaccone
F
F
Tagliavini
B
B
Frangione
O
O
Bugiani
J F
JF
Foncin
D000368:Aged; D000544:Alzheimer Disease / Q000378:metabolism* / Q000473:pathology; D016564:Amyloid beta-Protein Precursor / Q000032:analysis* / Q000276:immunology; D002540:Cerebral Cortex / Q000737:chemistry* / Q000648:ultrastructure; D006801:Humans; D016253:Microscopy, Immunoelectron; D008875:Middle Aged; D016874:Neurofibrillary Tangles / Q000737:chemistry*
D016564:Amyloid beta-Protein Precursor