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Recombinant human deoxyribonuclease for hematopoietic stem cell processing

S D Rowley1

  • 1Fred Hutchinson Cancer Research Center, Seattle, WA 98104, USA.

Journal of Hematotherapy
|April 1, 1995
PubMed
Summary
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Pharmaceutical-grade recombinant human deoxyribonuclease (DNase) shows no toxicity to hematopoietic progenitor cells. This enzyme may replace animal-sourced DNase in cell processing for transplantation.

Area of Science:

  • Biotechnology
  • Cell Biology
  • Hematology

Background:

  • Reagents for hematopoietic progenitor cell (HPC) processing require uniform safety and efficacy.
  • Pharmaceutical-grade reagents are often unavailable, necessitating alternatives.
  • Recombinant human deoxyribonuclease (DNase) is a newly approved pharmaceutical.

Purpose of the Study:

  • To evaluate the toxicity of pharmaceutical-grade recombinant human DNase on HPCs.
  • To compare the safety of recombinant human DNase with previously used bovine DNase.
  • To assess the suitability of recombinant human DNase for HPC transplantation procedures.

Main Methods:

  • HPCs were incubated with varying concentrations of recombinant human DNase and bovine DNase.
  • Cell viability and progenitor content were assessed after short-term incubation and direct culture addition.

Related Experiment Videos

  • Toxicity was evaluated in conjunction with an immunologic purge technique using antibodies and complement.
  • Effects on cell recovery after cryopreservation and thawing were analyzed.

    • Main Results:

    • No significant loss of nucleated cells or HPCs was observed with either enzyme source.
    • Incubation concentrations and direct addition to culture medium did not induce incremental toxicity.
    • Recombinant human DNase showed no additional toxicity when used with immunologic purging agents.
    • Variable effects on cell recovery post-thaw were noted for both enzyme types.

    Conclusions:

    • Pharmaceutical-grade recombinant human DNase demonstrates safety for HPCs.
    • Recombinant human DNase is a potential substitute for animal-derived DNase in cell processing.
    • This finding supports the use of high-quality pharmaceutical reagents in transplantation settings.