Osmotic modulation of chromatin impacts on efficiency and kinetics of cell fate modulation

Sci Rep. 2018 May 8;8(1):7210. doi: 10.1038/s41598-018-25517-2.

Abstract

Chromatin structure is a major regulator of transcription and gene expression. Herein we explore the use of osmotic modulation to modify the chromatin structure and reprogram gene expression. In this study we use the extracellular osmotic pressure as a chromatin structure and transcriptional modulator. Hyposmotic modulation promotes chromatin loosening and induces changes in RNA polymerase II (Pol II) activity. The chromatin decondensation opens space for higher amounts of DNA engaged RNA Pol II. Hyposmotic modulation constitutes an alternative route to manipulate cell fate decisions. This technology was tested in model protocols of induced pluripotency and transdifferentiation in cells growing in suspension and adherent to substrates, CD34+ umbilical-cord-blood (UCB), fibroblasts and B-cells. The efficiency and kinetics of these cell fate modulation processes were improved by transient hyposmotic modulation of the cell environment.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • B-Lymphocytes / drug effects
  • B-Lymphocytes / metabolism
  • B-Lymphocytes / ultrastructure
  • Cell Differentiation / drug effects*
  • Cell Transdifferentiation / drug effects*
  • Cells, Cultured
  • Chromatin / chemistry*
  • Chromatin / ultrastructure
  • Chromatin Assembly and Disassembly / drug effects
  • Culture Media / chemistry
  • Culture Media / pharmacology*
  • DNA / genetics
  • DNA / metabolism
  • Fetal Blood
  • Fibroblasts / drug effects
  • Fibroblasts / metabolism
  • Fibroblasts / ultrastructure
  • Humans
  • K562 Cells
  • Kinetics
  • Osmosis
  • Osmotic Pressure*
  • RNA Polymerase II / genetics
  • RNA Polymerase II / metabolism
  • Stem Cells / drug effects*
  • Stem Cells / metabolism
  • Stem Cells / ultrastructure
  • Transcription, Genetic / drug effects

Substances

  • Chromatin
  • Culture Media
  • DNA
  • RNA Polymerase II