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Antibody-targeted RNase fusion proteins (immunoRNases) for cancer therapy

Jürgen Krauss1, Michaela A E Arndt, Stefan Dübel

  • 1Natinal center for tumor diseases (NCT), Universit6y of Heidelberg, Im Neuenheimer Fild 350, D-69120 Heidleberg, Germany. juergen.krauss@med.uni-heidelberg.de

Current Pharmaceutical Biotechnology
|August 5, 2008
PubMed

Insights

Ribonucleases (RNases) show anti-cancer effects without significant toxicity. Genetically engineered immunoRNases, like Ranpirnase (Onconase), are being developed as novel cancer therapeutics, enhancing tumor cell killing.

Area of Science:

  • Biochemistry
  • Oncology
  • Immunology

Background:

  • Ribonucleases (RNases) of superfamily A possess significant antineoplastic activity.
  • RNases demonstrate minimal immunogenicity and non-specific toxicity in preclinical and clinical settings.
  • Ranpirnase (Onconase) is the first RNase to reach Phase III clinical trials for unresectable mesothelioma.

Purpose of the Study:

  • To review the development and current status of second-generation immunoRNases.
  • To highlight the potential of immunoRNases as novel anti-cancer therapeutics.

Main Methods:

  • Conjugation of RNases to internalizing, tumor-targeting monoclonal antibodies.
  • Evaluation of enhanced specific cell killing in vitro and in animal models.

Main Results:

  • Antibody-RNase conjugates significantly enhance tumor cell killing.
  • ImmunoRNases represent a promising strategy for targeted cancer therapy.

Conclusions:

  • Genetically engineered immunoRNases are advancing as potent and specific anti-cancer agents.
  • Targeted delivery via monoclonal antibodies amplifies the therapeutic efficacy of RNases.

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