The role of cleavage of cell structures during apoptosis

Cell Mol Biol (Noisy-le-grand). 2000 Feb;46(1):1-11.

Abstract

In this work we have studied the behavior of some cell structures, such as actin, tubulin and chromatin during apoptosis induced in F9 cells after retinoic acid treatment. In this experimental model, all defined steps of morphological changes described for apoptosis are observed. The correlation between a partial maintenance of F-actin and microtubular structures and the spatial distribution of F-actin suggests a possible relationship between this molecule and the characteristic shape changes observed in apoptosis. Additionally, the disposition of monomeric G-actin suggests a possible relationship between the fragmentation of this molecule and the cleavage of DNA. The analysis of the U2af1-rs1 specific sequence shows that the internucleosomal fragmentation observed in this gene is randomly produced during apoptosis and is not dependent of demethylation status. The results obtained confirm that specific cleavage of these cell structures is inherent to the development of the apoptotic process and do not exclude the possibility that proteolysis of key actin and/or tubulin molecules or the cleavage of specific chromatin sequences other than the ones analyzed here, could control the different phases of the apoptotic process.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Actins / ultrastructure
  • Animals
  • Apoptosis*
  • Cell Differentiation
  • Chromatin / metabolism
  • Cytoskeleton / ultrastructure*
  • Immunohistochemistry
  • Mice
  • Microscopy, Electron
  • Nerve Tissue Proteins*
  • Nuclear Proteins*
  • Proteins / genetics
  • Ribonucleoproteins*
  • Splicing Factor U2AF
  • Tretinoin / pharmacology
  • Tubulin / metabolism
  • Tubulin / ultrastructure
  • Tumor Cells, Cultured

Substances

  • Actins
  • Chromatin
  • Nerve Tissue Proteins
  • Nuclear Proteins
  • Proteins
  • Ribonucleoproteins
  • Splicing Factor U2AF
  • Tubulin
  • Zrsr1 protein, mouse
  • Tretinoin