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

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Summary

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.

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Supported by Fondo de Investigaciones Sanitarias de la Seguridad Social grant no. 90/0259 (Spain), NIA AG09466 and AG10161 (USA)

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Morán, M.A., Mufson, E.J. & Gómez-Ramos, P. Colocalization of cholinesterases with β amyloid protein in aged and Alzheimer's brains. Acta Neuropathol 85, 362–369 (1993). https://doi.org/10.1007/BF00334445

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