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Updated: Apr 13, 2026

Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase
Published on: November 23, 2016
Arginase: an old enzyme with new tricks
Ruth B Caldwell1, Haroldo A Toque2, S Priya Narayanan3
1Veterans Affairs Medical Center, One Freedom Way, Augusta, GA 30904, USA; Vision Discovery Institute, Medical College of Georgia, Georgia Regents University, 1459 Laney Walker Boulevard, Augusta, GA 30912, USA; Vascular Biology Center, Medical College of Georgia, Georgia Regents University, 1459 Laney Walker Boulevard, Augusta, GA 30912, USA.
Abstract:
Arginase has roots in early life-forms. It converts L-arginine to urea and ornithine. The former provides protection against NH3; the latter serves to stimulate cell growth and other physiological functions. Excessive arginase activity in mammals has been associated with cardiovascular and nervous system dysfunction and disease. Two relevant aspects of this elevated activity may be involved in these disease states. First, excessive arginase activity reduces the supply of L-arginine needed by nitric oxide (NO) synthase to produce NO. Second, excessive production of ornithine leads to vascular structural problems and neural toxicity. Recent research has identified inflammatory agents and reactive oxygen species (ROS) as drivers of this pathologic elevation of arginase activity and expression. We review the involvement of arginase in cardiovascular and nervous system dysfunction, and discuss potential therapeutic interventions targeting excess arginase.
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