Parvathy S, Karran E H, Turner A J, Hooper N M
School of Biochemistry and Molecular Biology, University of Leeds, UK.
FEBS Lett. 1998 Jul 10;431(1):63-5. doi: 10.1016/s0014-5793(98)00726-1.
Angiotensin converting enzyme (ACE) and the Alzheimer's amyloid precursor protein are cleaved from the membrane by zinc metalloproteinases termed ACE secretase and alpha-secretase, respectively. Tumour necrosis factor-alpha (TNF-alpha) convertase (ADAM 17) is a recently identified member of the adamalysin family of mammalian zinc metalloproteinases that is involved in the production of TNF-alpha and possibly in the cleavage of other membrane proteins. Using two different cell-free assays we were unable to detect significant cleavage and secretion of ACE by TNF-alpha convertase. In addition, there was a different effect of three hydroxamic acid-based inhibitors (batimastat, compound 1 and compound 4) towards TNF-alpha convertase as compared to ACE secretase and alpha-secretase. Thus TNF-alpha convertase would appear to be distinct from, but possibly related to, the secretases that cleave ACE and the amyloid precursor protein.
血管紧张素转换酶（ACE）和阿尔茨海默病淀粉样前体蛋白分别被称为ACE分泌酶和α-分泌酶的锌金属蛋白酶从细胞膜上切割下来。肿瘤坏死因子-α（TNF-α）转换酶（ADAM 17）是最近发现的哺乳动物锌金属蛋白酶adamalysin家族的成员，它参与TNF-α的产生，可能还参与其他膜蛋白的切割。使用两种不同的无细胞检测方法，我们未能检测到TNF-α转换酶对ACE的显著切割和分泌。此外，与ACE分泌酶和α-分泌酶相比，三种基于异羟肟酸的抑制剂（batimastat、化合物1和化合物4）对TNF-α转换酶有不同的作用。因此，TNF-α转换酶似乎与切割ACE和淀粉样前体蛋白的分泌酶不同，但可能有关联。
