Recent developments in L-asparaginase discovery and its potential as anticancer agent
Abhinav Shrivastava1, Abdul Arif Khan2, Mohsin Khurshid3
1College of Life Sciences, Cancer Hospital & Research Institute, Gwalior, MP 474009, India.
L-Asparaginase, an enzyme used to treat acute lymphoblastic leukemia (ALL), has toxic side effects and resistance issues. Researchers are exploring plant and fungal sources for a less toxic alternative cancer therapy.
Area of Science:
- Biochemistry
- Enzymology
- Cancer Therapy
Background:
- L-Asparaginase is a crucial enzyme in treating acute lymphoblastic leukemia (ALL) and other blood cancers.
- It functions by depleting L-asparagine, essential for cancer cell survival, inducing apoptosis.
- Current bacterial L-asparaginase formulations exhibit significant toxicities and lead to treatment resistance.
Purpose of the Study:
- To review the potential of L-asparaginase as an anticancer agent.
- To discuss the mechanism of action and adverse effects of current L-asparaginase treatments.
- To explore alternative sources of L-asparaginase with improved safety profiles.
Main Methods:
- Literature review of L-asparaginase's role in cancer therapy.
- Analysis of current bacterial L-asparaginase formulations and their limitations.
- Investigation into emerging L-asparaginase sources from plants and fungi.
Main Results:
- Bacterial L-asparaginases are effective but associated with toxicities like thrombosis and hyperglycemia.
- Drug resistance is a significant challenge with existing bacterial formulations.
- Plants and fungi represent promising alternative sources for developing less toxic L-asparaginase.
Conclusions:
- L-Asparaginase remains a vital therapeutic enzyme for hematological malignancies.
- Addressing toxicity and resistance necessitates exploring novel L-asparaginase sources.
- Alternative L-asparaginases from non-bacterial origins hold potential for safer and more effective cancer treatment.
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