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Hsp27 negatively regulates cell death by interacting with cytochrome c

Nature Cell Biology, ISSN: 1465-7392, Vol: 2, Issue: 9, Page: 645-652
2000
  • 871
    Citations
  • 0
    Usage
  • 252
    Captures
  • 2
    Mentions
  • 0
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    871
  • Captures
    252
  • Mentions
    2
    • Blog Mentions
      1
      • Blog
        1
    • References
      1
      • 1

Article Description

Mammalian cells respond to stress by accumulating or activating a set of highly conserved proteins known as heat-shock proteins (HSPs). Several of these proteins interfere negatively with apoptosis. We show that the small HSP known as Hsp27 inhibits cytochrome-c-mediated activation of caspases in the cytosol. Hsp27 does not interfere with granzyme-B-induced activation of caspases, nor with apoptosis-inducing factor-mediated, caspase-independent, nuclear changes. Hsp27 binds to cytochrome c released from the mitochondria to the cytosol and prevents cytochrome-c-mediated interaction of Apaf-1 with procaspase-9. Thus, Hsp27 interferes specifically with the mitochondrial pathway of caspase-dependent cell death.

Bibliographic Details

Jean Marie Bruey; Philippe Bonniaud; Sandeep Gurbuxani; Eric Solary; Carmen Garrido; Cécile Ducasse; Chantal Diaz-Latoud; André Patrick Arrigo; Luigi Ravagnan; Santos A. Susin; Guido Kroemer

Springer Science and Business Media LLC

Biochemistry, Genetics and Molecular Biology

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