Development and characterization of fused human arginase I for cancer therapy.

Recombinant human arginase I (rhArg I) have emerged as a potential candidate for the treatment of varied pathophysiological conditions ranging from arginine-auxotrophic cancer, inflammatory conditions and microbial infection. However, rhArg I have a low circulatory half-life, leading to poor pharmacokinetic and pharmacodynamic properties, which necessitating the rapid development of modifications to circumvent these limitations. To address this, polyethylene glycol (PEG)ylated-rhArg I variants are being developed by pharmaceutical companies.

Human arginase 1, a Jack of all trades?

Arginine, a conditionally essential amino acid, plays a crucial role in several metabolic and signalling pathways. Arginine metabolism in the body can be significantly increased under stress or during certain pathological conditions. Depletion of circulating arginine by administering arginine-hydrolysing enzyme has been shown to mitigate varied pathophysiological conditions ranging from cancer, inflammatory conditions, and microbial infection.