Title:An Update on Arginase Inhibitors and Inhibitory Assays
Volume: 22
Issue: 15
Author(s): Jason Muller, Rym Attia, Andy Zedet, Corine Girard and Marc Pudlo*
Affiliation:
- PEPITE EA4267, Université de Bourgogne Franche-Comté, F-25030 Besançon, France
Keywords:
Arginase, inhibitors, evaluation, assays, colorimetric, radiometric, cell culture.
Abstract: 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.