Colocalization of cholinesterases with β amyloid protein in aged and Alzheimer's brains
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.
β Amyloid, Acetylcholinesterase, Butyrylcholinesterase, Diffuse plaques, Preamyloid deposits
Digital Object Identifier (DOI)
Morán, M. A.; Mufson, E. J.; and Gómez-Ramos, P., "Colocalization of cholinesterases with β amyloid protein in aged and Alzheimer's brains" (1993). Translational Neuroscience. 1759.