Does purified ACE inhibit the aggregation and deposition of amyloid beta-peptide in vitro?
Purified ACE inhibits the aggregation, fibril formation, and deposition of Alzheimer's amyloid beta-peptide in vitro, suggesting a potential protective mechanism against Alzheimer's disease.
We have demonstrated that the angiotensin-converting enzyme (ACE) genotype is associated with Alzheimer's disease (AD) in the Japanese population (1). To determine why ACE affects susceptibility to AD, we examined the effect of purified ACE on aggregation of the amyloid -peptide (A) in vitro. Surprisingly, ACE was found to significantly inhibit A aggregation in a dose response manner. The inhibition of aggregation was specifically blocked by preincubation of ACE with an ACE inhibitor, lisinopril. ACE was confirmed to retard A fibril formation with electron microscopy. ACE inhibited A deposits on a synthaloid plate, which was used to monitor A deposition on autopsied brain tissue.
Hu et al. (Sat,) studied this question.
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