Chromatin changes induced by lamin A/C deficiency and the histone deacetylase inhibitor trichostatin A

Eur J Cell Biol. 2008 May;87(5):291-303. doi: 10.1016/j.ejcb.2008.01.013. Epub 2008 Apr 8.

Abstract

Recent studies have shown that histone code dictates the type and structure of chromatin. Bearing in mind the importance of A-type lamins for chromatin arrangement, we studied the effect of trichostatin A (TSA)-induced histone hyperacetylation in lamin A/C-deficient (LMNA-/-) fibroblasts. Lamin A/C deficiency caused condensation of chromosome territories and the nuclear reorganization of centromeric heterochromatin, which was accompanied by the appearance of a chain-like morphology of HP1beta foci. Conversely, histone deacetylase (HDAC) inhibition induced de-condensation of chromosome territories, which compensated the effect of lamin A/C deficiency on chromosome regions. The amount of heterochromatin in the area associated with the nuclear membrane was significantly reduced in LMNA-/- cells when compared with lamin A/C-positive (LMNA+/+) fibroblasts. TSA also decreased the amount of peripheral heterochromatin, similarly as lamin A/C deficiency. In both LMNA+/+ and LMNA-/- cells, physically larger chromosomes were positioned more peripherally as compared with the smaller ones, even after TSA treatment. Our observations indicate that lamin A/C deficiency causes not only reorganization of chromatin and some chromatin-associated domains, but also has an impact on the extent of chromosome condensation. As HDAC inhibition can compensate the lamin A/C-dependent chromatin changes, the interaction between lamins and specifically modified histones may play an important role in higher-order chromatin organization, which influences transcriptional activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation / drug effects
  • Animals
  • Cell Nucleus / metabolism
  • Centromere / metabolism
  • Chromatin / drug effects*
  • Chromatin / metabolism*
  • Chromatin Assembly and Disassembly / drug effects*
  • Chromobox Protein Homolog 5
  • Enzyme Inhibitors / pharmacology*
  • Fibroblasts / metabolism
  • Heterochromatin / metabolism
  • Histone Deacetylase Inhibitors*
  • Hydroxamic Acids / pharmacology*
  • Lamin Type A / deficiency*
  • Lamin Type A / genetics
  • Lamin Type A / metabolism
  • Lamin Type B / metabolism
  • Mice
  • Nuclear Proteins / metabolism

Substances

  • CBX1 protein, human
  • Chromatin
  • Enzyme Inhibitors
  • Heterochromatin
  • Histone Deacetylase Inhibitors
  • Hydroxamic Acids
  • LMNA protein, human
  • Lamin Type A
  • Lamin Type B
  • Nuclear Proteins
  • Chromobox Protein Homolog 5
  • trichostatin A