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Estrogen protects neuronal cells from the cytotoxicity induced by acetylcholinesterase‐amyloid complexes
Author(s) -
Bonnefont Andrea B,
Muñoz Francisco J,
Inestrosa Nibaldo C
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01552-x
Subject(s) - acetylcholinesterase , cytotoxicity , chemistry , estrogen , cytotoxic t cell , peptide , amyloid beta , fibril , senile plaques , neurotoxicity , amyloid (mycology) , in vitro , biochemistry , microbiology and biotechnology , medicine , endocrinology , toxicity , alzheimer's disease , biology , enzyme , disease , inorganic chemistry , organic chemistry
The senile plaques present in Alzheimer's disease (AD) are composed of a core of amyloid β‐peptide (Aβ) plus several proteins including acetylcholinesterase (AChE). Recently we found that AChE forms complexes with the Aβ peptide in vitro and that these are more cytotoxic than Aβ fibrils alone. Considering that estrogen has been reported to act as a protective agent against Aβ‐induced cytotoxicity, the effect of 17β‐estradiol was studied in rat pheochromocytoma (PC12) and mouse neuroblastoma (Neuro 2a) cells exposed to either Aβ alone or AChE‐Aβ complexes. Estrogen showed a powerful protective effect in response to the challenge of AChE‐Aβ complexes as well as with Aβ fibrils. This was also the case for other cytotoxic agents such as glutamate and H 2 O 2 . Our results suggest a common mechanism for cellular protection by estrogen against the toxicity of both Aβ fibrils and AChE‐Aβ complexes, likely avoiding the free radical apoptotic pathway.