Arginase-1 is abundantly expressed in the liver but is also found in other tissues and cells that lack a complete urea cycle, such as the lungs . The enzyme’s primary function is to detoxify ammonia by converting it into urea, which is then excreted from the body. This process is vital for maintaining the body’s nitrogen balance.
Recombinant human arginase-1 (rhArg1) is a form of the enzyme that has been produced using recombinant DNA technology. This technology allows for the production of large quantities of the enzyme, which can be used for various research and therapeutic purposes.
One of the most promising applications of recombinant human arginase-1 is in cancer therapy. Many cancer cells are auxotrophic for arginine, meaning they cannot synthesize this amino acid and rely on external sources. By depleting arginine, rhArg1 can inhibit the growth of these cancer cells, leading to tumor regression . This approach is being developed as a broad-spectrum anti-cancer therapy, with various rhArg1 variants showing remarkable anti-cancer activity .
Clinical studies have been conducted to evaluate the safety, pharmacokinetics, and potential anti-tumor activity of pegylated recombinant human arginase-1 (peg-rhArg1) in patients with advanced hepatocellular carcinoma (HCC). These studies have shown that peg-rhArg1 has a manageable safety profile and preliminary evidence of activity in advanced HCC patients .