Acetaldehyde inhibits serum aminopeptidases

被引:13
作者
Brecher, AS
Stauffer, R
Knight, J
机构
[1] Department of Chemistry, Bowling Green State University, Bowling Green
关键词
alcoholism; alcohol; aminopeptidase A; angiotensinases; hypertension; angiotensin II; arylamidases; high blood pressure; naphthylamidases;
D O I
10.1016/0741-8329(95)02023-3
中图分类号
R194 [卫生标准、卫生检查、医药管理];
学科分类号
摘要
Aminopeptidase A (APA)- and aminopeptidase M (APM)-like activity were assayed in Moni-Trol ES with L-ol-aspartyl-beta-naphthylamide and L-alanyl-beta-naphthylamide, respectively. Upon preincubation of the serum with 89.4, 223.5, and 447 mM acetaldehyde at room temperature for 30 min, a reduction in 26.8%, 55.3%, and 75.8% aminopeptidase A activity was observed. Similarly, aminopeptidase M activity was reduced by 26.5% and 53.1% upon preincubation with 223.5 and 447 mM acetaldehyde. Ethanol at 84.9, 212.3, and 427.9 mM did not significantly affect the enzymic activity. Because aminopeptidase A and aminopeptidase M also degrade the presser substance, angiotensin II, it is suggested that inhibition of aminopeptidase A- and aminopeptidase M-like activity by acetaldehyde, the product of ethanol metabolism, may lead to higher levels of circulating angiotensin II and, consequently, hypertension, in alcoholics. The hydrolysis of lysine-p-nitroanilide, an aminopeptidase B substrate, was also inhibited upon addition of acetaldehyde to Moni-Trol ES serum.
引用
收藏
页码:125 / 131
页数:7
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