Nuclear translocation of PDCD5 (TFAR19): an early signal for apoptosis?

FEBS Lett. 2001 Dec 7;509(2):191-6. doi: 10.1016/s0014-5793(01)03062-9.

Abstract

The programmed cell death 5 (PDCD5) protein is a novel protein related to regulation of cell apoptosis. In this report, we demonstrate that the level of PDCD5 protein expressed in cells undergoing apoptosis is significantly increased compared with normal cells, then the protein translocates rapidly from the cytoplasm to the nucleus of cells. The appearance of PDCD5 in the nuclei of apoptotic cells precedes the externalization of phosphatidylserine and fragmentation of chromosome DNA. This phenomenon is parallel to the loss of mitochondrial membrane potential, independent of the feature of apoptosis-inducing stimuli and also independent of the cell types and the apoptosis modality. In conclusion, the nuclear translocation of PDCD5 is a universal earlier event of the apoptotic process, and may be a novel early marker for apoptosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus
  • Apoptosis Regulatory Proteins
  • Apoptosis*
  • Camptothecin / pharmacology
  • Cell Nucleus / metabolism*
  • Cisplatin / pharmacology
  • Culture Media, Serum-Free
  • DNA Fragmentation
  • Etoposide
  • HeLa Cells
  • Humans
  • Membrane Potentials
  • Mitochondria / physiology
  • Neoplasm Proteins / metabolism*
  • Phosphatidylserines / metabolism
  • Signal Transduction
  • Staurosporine / pharmacology
  • Time Factors
  • Tumor Cells, Cultured
  • Ultraviolet Rays

Substances

  • Apoptosis Regulatory Proteins
  • Culture Media, Serum-Free
  • Neoplasm Proteins
  • PDCD5 protein, human
  • Phosphatidylserines
  • Etoposide
  • Staurosporine
  • Cisplatin
  • Camptothecin