Binding of amyloid β-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB):: regulation of an SDR enzyme activity with implications for apoptosis in Alzheimer's disease
Binding of amyloid β-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB):: regulation of an SDR enzyme activity with implications for apoptosis in Alzheimer's disease
复制标题
DOI：
10.1016/s0014-5793(99)00586-4
复制
发表时间：
1999-05-28
期刊：
影响因子：
3.5
通讯作者：
Jörnvall, H
中科院分区：
文献类型：
--
作者：
Oppermann, UCT;Salim, S;Jörnvall, H
细胞内淀粉样蛋白β -肽（A β）结合蛋白ERAB是短链脱氢酶/还原酶（SDR）家族的成员，已知在不同细胞系中介导凋亡，是II类羟酰基辅酶A脱氢酶。A - β肽利用3-羟基丁基辅酶A抑制酶促反应，K-i为1.2 μ mol/l， K-iES为0.3 μ mol/l，呈混合型抑制。抑制所需的肽区包括A β 1-40的残基12-24，覆盖16-20片段，这是阻断A β聚合的最小序列，但这个最小片段不足以产生更多的边际抑制。ERAB定位于内质网和线粒体，表明与程序性细胞死亡机制的组成部分存在复杂的相互作用，a β与ERAB的相互作用进一步将氧化还原酶活性与细胞凋亡和淀粉样蛋白毒性联系起来。(C) 1999年欧洲生化学会联合会。
The intracellular amyloid beta-peptide (A beta) binding protein, ERAB, a member of the short-chain dehydrogenase/reductase (SDR) family, is known to mediate apoptosis in different cell lines and to be a class II hydroxyacyl-CoA dehydrogenase. The A beta peptide inhibits the enzymatic reaction in a mixed type fashion with a K-i of 1.2 mu mol/l and a K-iES of 0.3 mu mol/l, using 3-hydroxybutyryl-CoA. The peptide region necessary for inhibition comprises residues 12-24 of A beta 1-40, covering the 16-20 fragment, which is the minimum sequence for the blockade of A beta polymerization, but that minimal fragment is not sufficient for more than marginal inhibition. The localization of ERAB to the endoplasmic reticulum and mitochondria suggests a complex interaction with components of the programmed cell death machinery, The interaction of A beta with ERAB further links oxidoreductase activity with both apoptosis and amyloid toxicity. (C) 1999 Federation of European Biochemical Societies.