Caspase-1 activity is required for neuronal differentiation of PC12 cells: Cross-talk between the caspase and calpain systems

T. Vaisid, N. S. Kosower, S. Barnoy*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Previously, we have found that caspase-1 activity is increased during myoblast differentiation to myotubes. Here we show that caspase-1 activity is required for PC12 differentiation to neuronal-like cells. Caspase-1 is shown to be activated (by immunoblotting and by assessing activity in cell extracts) in the PC12 cells following the initial stage of differentiation. The inhibition of caspase-1 arrests PC12 cells at an intermediate stage of differentiation and prevents neurite outgrowth in these cells; the inhibition is reversed upon the removal of the inhibitor. Calpastatin (calpain endogenous specific inhibitor, and a known caspase substrate) is diminished at the later stages of PC12 cell differentiation, and diminution is prevented by caspase-1 inhibition. The degradation of fodrin (a known caspase and calpain substrate) is found in the advanced stage of differentiation. Caspase-1 has been implicated in the activation of proinflammatory cytokines, and in cell apoptosis. The involvement of caspase-1 in two distinct differentiation processes (myoblast fusion and neuronal differentiation of PC12 cells) indicates a function for this caspase in differentiation processes, and suggests some common mechanisms underlying caspase roles in such processes.

Original languageEnglish
Pages (from-to)223-230
Number of pages8
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Volume1743
Issue number3
DOIs
StatePublished - 15 Apr 2005

Keywords

  • Calpain
  • Calpastatin
  • Caspase
  • Neuronal cell differentiation
  • PC12

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