Boomsma F, Tipton K F
Department of Internal Medicine, Section of Vascular Pharmacology, Erasmus MC, Rotterdam, The Netherlands.
J Neural Transm (Vienna). 2007;114(6):775-6. doi: 10.1007/s00702-007-0672-1. Epub 2007 Mar 26.
Recently, a new FAD-dependent amine oxidase, renalase, was described. It was secreted by the kidney into the blood and shown to have significant cardiovascular actions, which were attributed to its catecholamine-metabolising activity. The authors concluded that renalase might be an important regulatory factor in human (patho)physiology. The catecholamine-metabolising activity of renalase in plasma contrasts with previous investigations where catecholamines were found to be stable in human plasma, provided autoxidation is prevented by an antioxidant. The claim of catecholamine-metabolising activity of renalase was based on the generation of H(2)O(2) during incubation of the enzyme with catecholamines. Careful inspection and calculations of the data lead to the conclusion that the rate of H(2)O(2) generation is far too low to be ascribed to enzymatic conversion of catecholamines by renalase. Renalase may well have important cardiovascular functions, but there is no proof that its actions are mediated through catecholamine-metabolising activity.
最近,一种新的黄素腺嘌呤二核苷酸(FAD)依赖性胺氧化酶——肾酶被发现。它由肾脏分泌进入血液,并被证明具有显著的心血管作用,这归因于其儿茶酚胺代谢活性。作者得出结论,肾酶可能是人类(病理)生理学中的一个重要调节因子。肾酶在血浆中的儿茶酚胺代谢活性与之前的研究形成对比,在之前的研究中,只要通过抗氧化剂防止自氧化,儿茶酚胺在人体血浆中是稳定的。肾酶具有儿茶酚胺代谢活性这一说法是基于该酶与儿茶酚胺孵育过程中过氧化氢(H₂O₂)的生成。对数据的仔细检查和计算得出结论,H₂O₂的生成速率过低,不能归因于肾酶对儿茶酚胺的酶促转化。肾酶很可能具有重要的心血管功能,但没有证据表明其作用是通过儿茶酚胺代谢活性介导的。