Colocalization of cholinesterases with β amyloid protein in aged and Alzheimer's brains

Document Type

Article

Abstract

The colocalization of β amyloid protein with the enzymes acetyl- and butyrylcholinesterase was assessed using immunocytochemistry for β amyloid protein and a sensitive histochemical technique for cholinesterases. In non-demented aged and Alzheimer's disease brains, double-stained sections for cholinesterases and thioflavin-S showed that all thioflavin-S-positive plaques were also positive for cholinesterases, indicating the presence of these enzymes in all plaques with β-pleated amyloid protein. When amyloid angiopathy was present, cholinesterases were also observed in amyloid-laden vessels walls. Comparison of series of adjacent sections alternatively stained for acetylcholinesterase, β amyloid protein and butyrylcholinesterase, as well as by double histo-immunocytochemical staining, showed either cholinesterase in a proportion of the preamyloid diffuse plaques. These data indicate that cholinesterases are associated with the amyloid protein from very early stages, when the β-pleated structure is being formed. Novel functions attributed to acetyl- and butyrylcholinesterase, such us their proteolytic activity either by themselves or in association with heparan sulfate proteoglycans, may play a role in the aggregation or the consolidation processes taking place at the early stages of diffuse plaque formation. © 1993 Springer-Verlag.

Keywords

β Amyloid, Acetylcholinesterase, Butyrylcholinesterase, Diffuse plaques, Preamyloid deposits

Publication Date

7-1-1993

Publication Title

Acta Neuropathologica

ISSN

00016322

E-ISSN

14320533

Volume

85

Issue

4

First Page

362

Last Page

369

PubMed ID

8480510

Digital Object Identifier (DOI)

10.1007/BF00334445

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