Caspase Activation Independent of Cell Death is Required for Proper Cell Dispersal and Correct Morphology in PC12 Cells

Research output: Contribution to journalArticlepeer-review

55 Scopus citations

Abstract

Caspase activation is indispensable for the proper execution of apoptosis. However, to date, little is known about other possible physiologic functions for this class of enzymes in addition to their well-defined role in apoptosis. In this report, we described an action of caspase-3 involving cell dispersion that is independent of cell death. Using an in vitro neuronal model system consisting of PC12 cells, we observed a transient activation of caspase-3 both in situ and by Western blot analysis that was evident at 1 h following plating, was maximal by 3 h, and was attenuated by 24 h. Preincubation of PC12 cells with either the caspase-3 inhibitor, DEVD, or antisense caspase-3 oligonucleotides caused cells to be more rounded in appearance and led to a failure of cells to disperse properly. Additional experiments demonstrated a possible target for caspase cleavage to be the cytoskeletal protein, tau. These data suggest a requirement for caspase activation and subsequent disassembly of the cytoskeleton during cell dispersion and represent a novel role for caspases that may allow for proper migration of neurons to target locations during development.

Original languageAmerican English
Pages (from-to)215-25
Number of pages11
JournalExperimental Cell Research
Volume295
Issue number1
DOIs
StatePublished - 15 Apr 2004

Keywords

  • Caspase-3;Apoptosis;PC12 cells;Tau;Morphology;Dispersal

EGS Disciplines

  • Biology

Fingerprint

Dive into the research topics of 'Caspase Activation Independent of Cell Death is Required for Proper Cell Dispersal and Correct Morphology in PC12 Cells'. Together they form a unique fingerprint.

Cite this