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Related Experiment Videos

Fas-induced caspase denitrosylation.

J B Mannick1, A Hausladen, L Liu

  • 1Department of Adult Oncology, Dana Farber Cancer Institute, 44 Binney Street, Boston, MA 02115, USA. joan_mannick@dfci.harvard.edu

Science (New York, N.Y.)
|April 24, 1999
PubMed
Summary
This summary is machine-generated.

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Protein S-nitrosylation, a modification on proteins, regulates cell signaling. This study shows Fas pathway activation denitrosylates caspase-3, increasing its activity and demonstrating a role for S-nitrosylation in signal transduction.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • The role of protein S-nitrosylation in cellular signaling remains largely unexplored.
  • Few intracellular S-nitrosylated proteins have been identified to date.

Purpose of the Study:

  • To investigate whether protein S-nitrosylation and denitrosylation are involved in signal transduction pathways.
  • To examine the regulation of caspase-3 activity by S-nitrosylation.

Main Methods:

  • Analysis of S-nitrosylation status of caspase-3 zymogens in human cell lines.
  • Investigating the effect of Fas apoptotic pathway activation on caspase-3 S-nitrosylation.
  • Correlating changes in caspase-3 S-nitrosylation with intracellular caspase activity.

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Main Results:

  • Caspase-3 zymogens were found to be S-nitrosylated on their catalytic-site cysteine in unstimulated cells.
  • Fas pathway activation led to the denitrosylation of caspase-3.
  • Reduced caspase-3 S-nitrosylation correlated with increased intracellular caspase activity.

Conclusions:

  • Protein S-nitrosylation/denitrosylation acts as a regulatory mechanism within signal transduction pathways.
  • Fas-mediated apoptosis involves both caspase-3 cleavage and active-site thiol denitrosylation for caspase-3 activation.