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Programmed cell death

R A Gottlieb1

  • 1Division of Hematology, Department of Molecular & Experimental Medicine MEM 220, The Scripps Research Institute, La Jolla, California 92037, USA.

Drug News & Perspectives
|August 26, 2003
PubMed

Insights

Caspases, a family of proteases, are essential for apoptosis (programmed cell death) in animals. Activated caspases trigger cellular dismantling, leading to non-inflammatory cell removal.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Animal development involves programmed cell death, known as apoptosis.
  • Apoptosis is executed by caspases, a family of cysteine proteases.
  • CED-3 in C. elegans is a homolog of mammalian caspase-3, crucial for apoptosis.

Purpose of the Study:

  • To elucidate the role and mechanism of caspase activation in apoptosis.
  • To describe the biochemical and morphological changes during apoptosis.
  • To highlight the conserved nature of apoptosis pathways across species.

Main Methods:

  • Review of existing literature on caspases and apoptosis.
  • Comparative analysis of caspase function in C. elegans and mammals.
  • Description of cellular and molecular events during apoptotic execution.

Main Results:

  • Caspase activation is a hallmark of apoptosis.
  • Activated caspases cleave specific substrates, leading to cell dismantling.
  • Apoptotic cells exhibit characteristic morphological changes like blebbing and DNA fragmentation.
  • Mitochondrial dysfunction and release of cytochrome c are key events.

Conclusions:

  • Caspases are central executioners of apoptosis, conserved across animal species.
  • Apoptosis involves a coordinated series of biochemical and morphological events.
  • These processes ensure the non-inflammatory removal of dying cells.

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