December 1, 2001Journal of Biological Chemistry357 citationsOpen Access

Angiotensin-converting Enzyme Degrades Alzheimer Amyloid β-Peptide (Aβ); Retards Aβ Aggregation, Deposition, Fibril Formation; and Inhibits Cytotoxicity

JHJianguo HuShanghai International Studies University AIAkira IgarashiYamagata University MKMakiko KamataShin Nippon Biomedical Laboratories (Japan)

Structured PICO

Does purified ACE inhibit the aggregation and deposition of amyloid beta-peptide in vitro?

Population

In vitro model using purified angiotensin-converting enzyme (ACE) and amyloid beta-peptide (Aβ)

Intervention

Purified angiotensin-converting enzyme (ACE)

Comparator

Preincubation of ACE with lisinopril (ACE inhibitor) or no ACE

Outcome

Aggregation of amyloid beta-peptide (Aβ)surrogate

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.

Abstract

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.

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