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Nuclear changes in apoptosis

W C Earnshaw1

  • 1Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

Current Opinion in Cell Biology
|June 1, 1995
PubMed
Summary

Specific proteinases initiate a cascade of events leading to programmed cell death (apoptosis). Research using cell-free systems and intact cells reveals key enzymes and DNA fragmentation steps in this process.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Specific proteinases, including the Ced-3/interleukin-1 beta converting enzyme family, are known to trigger apoptotic events.
  • Apoptosis involves a complex cascade of enzymatic reactions.
  • Understanding the substrates and mechanisms of these proteinases is crucial for comprehending cell death pathways.

Purpose of the Study:

  • To identify substrates of proteinases involved in apoptosis using cell-free systems.
  • To elucidate the sequential DNA fragmentation events during apoptosis in intact cells.

Main Methods:

  • Utilized newly developed cell-free systems to study proteinase substrates.
  • Investigated DNA fragmentation patterns in intact cells undergoing apoptosis.

Main Results:

  • Identified substrates of specific proteinases in apoptosis.
  • Observed genome cleavage into domain-sized fragments preceding nucleosome-sized DNA fragmentation.
  • Demonstrated the activation of a second nuclease responsible for DNA fragmentation.

Conclusions:

  • Proteinases of the Ced-3/interleukin-1 beta converting enzyme family play a critical role in initiating apoptosis.
  • Apoptosis involves a multi-step DNA degradation process mediated by distinct nucleases.
  • Cell-free systems provide valuable insights into the molecular mechanisms of apoptosis.

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