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Published on: September 14, 2018
Arginine deiminase, a potential anti-tumor drug
Ye Ni1, Ulrich Schwaneberg, Zhi-Hao Sun
1Laboratory of Biocatalysis, School of Biotechnology, Jiangnan University, The Key Laboratory of Industrial Biotechnology, Ministry of Education, 1800 Lihu Road, Wuxi 214122, PR China.
Abstract:
Arginine deiminase (ADI; EC 3.5.3.6), an arginine-degrading enzyme, has been studied as a potential anti-tumor drug for the treatment of arginine-auxotrophic tumors, such as hepatocellular carcinomas (HCCs) and melanomas. Studies with human lymphatic leukemia cell lines further suggest that ADI is a potential anti-angiogenic agent and is effective in the treatment of leukemia. For instance ADI-PEG-20, patented by Pheonix Pharmacologic Inc., is currently in clinical trials for the treatment of HCC (Phase II/III) and melanoma (Phase I/II). This review summarizes results on recombinant expression, structural analysis, PEG (polyethylene glycerol) modification, in vivo anti-cancer activities, and clinical studies of ADI. Discussions on heterogeneous expression of ADI, directed evolution for improving enzymatic properties, and HSA-fusion for increased in vivo activity conclude this review.
Insights
Arginine deiminase (ADI) shows promise as an anti-cancer therapy for arginine-auxotrophic tumors like hepatocellular carcinoma and melanoma. This review covers ADI
Area of Science:
- Biochemistry
- Oncology
- Pharmacology
Background:
- Arginine deiminase (ADI) degrades arginine, an amino acid essential for certain tumor cells.
- Arginine auxotrophy is observed in hepatocellular carcinomas (HCCs) and melanomas, making them potential targets for ADI therapy.
- ADI also exhibits anti-angiogenic properties and effectiveness against leukemia.
Purpose of the Study:
- To review the recombinant expression, structural analysis, and PEG modification of ADI.
- To summarize in vivo anti-cancer activities and clinical studies of ADI.
- To discuss strategies for improving ADI's therapeutic potential, including heterogeneous expression, directed evolution, and HSA-fusion.
Main Methods:
- Recombinant expression and structural analysis of ADI.
- Polyethylene glycol (PEG) modification of ADI to create ADI-PEG-20.
- In vivo studies and clinical trials (Phase I/II/III) of ADI and ADI-PEG-20 for various cancers.
Main Results:
- ADI-PEG-20 is in clinical trials for HCC and melanoma.
- ADI demonstrates in vivo anti-cancer activities and potential as an anti-angiogenic agent.
- Ongoing research focuses on enhancing ADI's enzymatic properties and in vivo efficacy.
Conclusions:
- Arginine deiminase (ADI) is a promising therapeutic agent for arginine-dependent cancers.
- ADI-PEG-20 is advancing through clinical trials, indicating its therapeutic potential.
- Further research into ADI modifications and expression systems may improve its anti-cancer efficacy.
