PEPITE EA4267, Université de Bourgogne Franche-Comté, F-25030 Besançon, France.
Normandie University, UNICAEN, CERMN, 14000 Caen, France.
Mini Rev Med Chem. 2022;22(15):1963-1976. doi: 10.2174/1389557522666211229105703.
Arginase, which converts arginine into ornithine and urea, is a promising therapeutic target. Arginase is involved in cardiovascular diseases, parasitic infections and through a critical role in immunity, in some cancers. There is a need to develop effective arginase inhibitors and therefore efforts to identify and optimize new inhibitors are increasing. Several methods of evaluating arginase activity are available, but few directly measure the product. Radiometric assays need to separate urea and dying reactions require acidic conditions and sometimes heating. Hence, there are a variety of different approaches available, and each approach has its own limits and benefits. In this review, we provide an update on arginase inhibitors, followed by a discussion on available arginase assays and alternative methods, focusing on the intrinsic biases and parameters that are likely to impact results.
精氨酸酶将精氨酸转化为鸟氨酸和尿素,是一种很有前途的治疗靶点。精氨酸酶参与心血管疾病、寄生虫感染,并通过在某些癌症中的关键作用影响免疫。因此,需要开发有效的精氨酸酶抑制剂,因此,识别和优化新抑制剂的努力正在增加。有几种评估精氨酸酶活性的方法,但很少有方法直接测量产物。放射性分析需要分离尿素,而终止反应需要酸性条件,有时还需要加热。因此,有各种各样不同的方法,每种方法都有其自身的局限性和优势。在这篇综述中,我们首先提供精氨酸酶抑制剂的最新进展,然后讨论现有的精氨酸酶检测方法和替代方法,重点介绍可能影响结果的内在偏差和参数。