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Properties of the caspases

H R Stennicke1, G S Salvesen

  • 1Program for Apoptosis and Cell Death, Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA. hstennicke@burnham-inst.org

Biochimica Et Biophysica Acta
|September 28, 1998
PubMed
Summary
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Caspases are proteases crucial for programmed cell death (apoptosis) and activating inflammatory cytokines in mammals. This review details their substrate specificity, structure, and activation, linking them to essential biological functions.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Caspases are cysteine proteases found in animal cells.
  • They play key roles in apoptosis and inflammatory responses.
  • Their primary specificity involves cleaving after Asp residues.

Purpose of the Study:

  • To review current knowledge on human caspases.
  • To explore their substrate specificity, structure, and activation.
  • To connect these aspects to their biological roles.

Main Methods:

  • Literature review of existing research on caspases.
  • Analysis of structural and biochemical data.
  • Integration of findings on substrate specificity and activation.

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Main Results:

  • Caspases exhibit specific cleavage patterns, primarily after Asp residues.
  • They are essential executioners of apoptosis across animal species.
  • In mammals, caspases also mediate pro-inflammatory cytokine activation.

Conclusions:

  • Understanding caspase structure, specificity, and activation is vital for elucidating their biological functions.
  • Caspases are central to both cell death and inflammation.
  • Further research can leverage this knowledge for therapeutic interventions.