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Anticancer efficacy of methioninase in vivo

Y Tan1, M Xu, H Guo

  • 1AntiCancer Inc., San Diego, CA 92111, USA.

Anticancer Research
|November 1, 1996
PubMed

Insights

Methioninase, an enzyme targeting methionine-dependent cancers, effectively arrests tumor growth in mice with minimal toxicity. This novel therapeutic approach shows promise for treating solid tumors.

Area of Science:

  • Biochemistry
  • Oncology
  • Pharmacology

Background:

  • Enhanced methionine dependence is a cancer-selective metabolic vulnerability.
  • Methionine restriction halts cancer cell growth via cell-cycle arrest.
  • Previous studies showed dietary methionine restriction partially arrests rodent tumors.

Purpose of the Study:

  • To evaluate the efficacy and toxicity of methioninase from Pseudomonas putida against rodent and human tumors in vivo.
  • To investigate methioninase's mechanism of action, specifically its effect on the cell cycle.

Main Methods:

  • Administration of purified methioninase to nude mice bearing Yoshida sarcoma or H460 human non-small-cell lung carcinoma.
  • Comparison of methioninase efficacy with 5-fluorouracil and vincristine.
  • Assessment of tumor growth, animal weight, and cell-cycle progression.

Main Results:

  • Methioninase arrested Yoshida sarcoma growth and significantly slowed H460 tumor growth.
  • Methioninase demonstrated effectiveness where 5-fluorouracil and vincristine were inactive.
  • Treatment with methioninase showed no weight loss in mice for up to 10 days, indicating low toxicity.
  • Methioninase induced a tumor-specific late cell-cycle block.

Conclusions:

  • Methioninase is a potent antitumor agent with a novel, tumor-selective mechanism.
  • The enzyme exhibits minimal toxicity, suggesting potential for clinical application.
  • Methioninase's ability to induce cell-cycle arrest can be leveraged to enhance other cancer therapies.

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