Actin cleavage by CPP-32/apopain during the development of apoptosis

Tetsuo Mashima, Mikihiko Naito, Kohji Noguchi, Douglas K. Miller, Donald W. Nicholson, Takashi Tsuruo

Research output: Contribution to journalArticlepeer-review

218 Citations (Scopus)


Interleukin-1β-converting enzyme (ICE)/ced-3 family proteases play key roles in apoptosis. However, cellular substrates for ICE family proteases involved in apoptosis are not well understood. We previously showed that actin is cleaved ill vitro by an ICE family protease, distinct from ICE itself, which is activated during VP-16-induced apoptosis. In this report, we demonstrate that the actin-cleaving ICE-family protease in the apoptotic cell extract is the activated CPP-32/apopain. CPP-32 effectively cleaves actin protein to 15 kDa and 31 kDa fragments. Studies with an antibody raised against Gly-Gln-Val-IIe-Thr peptide, the N-terminal sequence of the cleaved 15 kDa actin fragment, showed that actin is also cleaved in vivo during the development of apoptosis. Moreover, Benzyloxycarbonyl-Glu-Val-Asp-CH2OC(O)-2,6,-dichlorobenzene (Z-EVD-CH2-DCB), a selective inhibitor of CPP-32(-Like) protease, efficiently inhibited the cleavage of actin and the apoptosis of VP-16-treated U937 cells. Our present results indicate that actin is the substrate of CPP-32/apopain(-like) protease both in vitro and in vivo and suggest the role of actin in the control of cell growth and apoptosis.

Original languageEnglish
Pages (from-to)1007-1012
Number of pages6
Issue number9
Publication statusPublished - 1997
Externally publishedYes


  • Actin
  • Apoptosis
  • CPP-32/apopain
  • ICE

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cancer Research


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