Arginase: an old enzyme with new tricks

RB Caldwell, HA Toque, SP Narayanan… - Trends in …, 2015 - cell.com
RB Caldwell, HA Toque, SP Narayanan, RW Caldwell
Trends in pharmacological sciences, 2015cell.com
Arginase has roots in early life-forms. It converts L-arginine to urea and ornithine. The former
provides protection against NH 3; 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 …
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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