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Related Experiment Videos

HSP90 function is required for morphogenesis in ascidian and echinoid embryos.

Cory D Bishop1, William R Bates, Bruce P Brandhorst

  • 1Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, BC, V5A 1S6, Canada.

Development Genes and Evolution
|March 27, 2002
PubMed
Summary

Targeting heat shock protein 90 (HSP90) with drugs like geldanamycin and radicicol halts embryonic development in marine invertebrates. This disruption of HSP90 function selectively impairs crucial morphogenetic movements without causing general toxicity.

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Area of Science:

  • Developmental Biology
  • Molecular Biology
  • Marine Biology

Background:

  • Heat shock protein 90 (HSP90) is a crucial molecular chaperone involved in protein folding and stability.
  • HSP90 client proteins regulate numerous cellular processes, including cell division, differentiation, and morphogenesis.
  • Disruption of HSP90 function can lead to the inactivation or degradation of its client proteins, impacting cellular functions.

Purpose of the Study:

  • To investigate the role of HSP90 in embryonic development using anti-HSP90 drugs.
  • To determine the effects of HSP90 inhibition on morphogenetic movements in ascidian and sea urchin embryos.
  • To assess the potential of HSP90 inhibitors as tools for identifying novel proteins involved in morphogenesis.

Main Methods:

  • Treatment of ascidian (Boltenia villosa, Cnemidocarpa finmarkiensis) and sea urchin (Strongylocentrotus purpuratus) embryos with anti-HSP90 drugs (geldanamycin, radicicol).

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  • Observation and analysis of embryonic development, including morphogenetic movements, cell division, and gene expression.
  • Assessment of embryo viability and general toxicity following drug treatment.

    • Main Results:

    • Anti-HSP90 drugs induced morphogenetic arrest across various embryonic stages in both ascidians and sea urchins.
    • Specific morphogenetic movements, such as gastrulation and mesenchyme cell migration, were arrested 8-10 hours after treatment.
    • Cell division and some gene expression continued despite the arrest of morphogenesis, indicating selective effects.
    • Arrested embryos remained viable for extended periods, suggesting low general toxicity of the drugs.

    Conclusions:

    • Inhibition of HSP90 function selectively disrupts essential morphogenetic movements during early development.
    • The observed morphogenetic arrest is likely due to the reduced concentration or activity of HSP90 client proteins required for these processes.
    • Anti-HSP90 drugs serve as valuable tools for dissecting the molecular mechanisms underlying morphogenesis and identifying novel regulatory proteins.