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Published on: December 16, 2021
Recombinant arginine-degrading enzymes in metabolic anticancer therapy and bioanalytics
Oleh V Stasyk1, Yuriy R Boretsky, Mykhailo V Gonchar
1Institute of Cell Biology, National Academy of Sciences of Ukraine, Drahomanov St. 14/16, Lviv, 79005, Ukraine.
Abstract:
Tumor cells often exhibit specific metabolic defects due to the aberrations in oncogene-dependent regulatory and/or signaling pathways that distinguish them from normal cells. Among others, many malignant cells are deficient in biosynthesis of certain amino acids and concomitantly exhibit elevated sensitivity to deprivation of these amino acids. Although the underlying causes of such metabolic changes are still not fully understood, this feature of malignant cells is exploited in metabolic enzymotherapies based on single amino acid, e.g., arginine, deprivation. To achieve efficient arginine depletion in vivo, two recombinant enzymes, bacterial arginine deiminase and human arginase I have been evaluated and are undergoing further development. This review is aimed to summarize the current knowledge on the application of arginine-degrading enzymes as anticancer agents and as bioanalytical tools for arginine assays. The problems that have to be solved to optimize this therapy for clinical application are discussed.
Insights
Cancer cells have unique metabolic needs, making them vulnerable to amino acid deprivation. Arginine-degrading enzymes are being developed as a promising anticancer therapy, with ongoing research to optimize clinical applications.
Area of Science:
- Biochemistry
- Oncology
- Metabolic Engineering
Background:
- Malignant cells display distinct metabolic defects driven by oncogenic pathways.
- Many tumors show deficiencies in amino acid biosynthesis, increasing their sensitivity to nutrient deprivation.
Purpose of the Study:
- To review the use of arginine-degrading enzymes as anticancer agents.
- To explore the application of these enzymes as bioanalytical tools for arginine level assays.
- To discuss challenges and future directions for optimizing arginine deprivation therapy.
Main Methods:
- Evaluation of recombinant bacterial arginine deiminase.
- Assessment of human arginase I for in vivo applications.
- Literature review of current knowledge on arginine-degrading enzymes in cancer therapy.
Main Results:
- Arginine deprivation via enzymatic degradation is a viable strategy against cancer.
- Recombinant arginine deiminase and human arginase I show potential for therapeutic use.
- Enzymes can serve as tools for precise arginine level monitoring.
Conclusions:
- Arginine-degrading enzymes represent a promising therapeutic avenue for cancer treatment.
- Further research is needed to overcome obstacles for successful clinical translation.
- Enzyme-based therapies offer a targeted approach by exploiting cancer-specific metabolic vulnerabilities.
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