Heavy metals chromium and neodymium reduced phosphorylation level of heat shock protein 27 in human keratinocytes

Toxicol In Vitro. 2010 Jun;24(4):1098-104. doi: 10.1016/j.tiv.2010.03.011. Epub 2010 Mar 21.

Abstract

Heavy metals may exert their acute and chronic effects on the human skin through stress signals. In the present study, 2DE-based proteomics was used to analyze the protein expression in human keratinocytes exposed to heavy metals, chromium and neodymium, and 10 proteins with altered expression were identified. Among these proteins, small heat shock protein 27 (HSP27) was up-regulated significantly and the up-regulation was validated by Western blot and immunofluorescence. In addition, the mRNA expression level of HSP27 markedly increased as detected by quantitative PCR. More interestingly, the ratio of phosphorylated HSP27 and total HSP27 significantly decreased in keratinocytes treated with the heavy metals. These findings suggested that heavy metals reduced the phosphorylation level of HSP27, and that the ratio of p-HSP27 and HSP27 may represent a potential marker or additional endpoint for the hazard assessment of skin irritation caused by chemical products.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line
  • Chromium / toxicity*
  • Environmental Pollutants / toxicity*
  • HSP27 Heat-Shock Proteins / metabolism*
  • Humans
  • Keratinocytes / drug effects*
  • Keratinocytes / metabolism
  • Neodymium / toxicity*
  • Phosphorylation / drug effects
  • Proteome / drug effects
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Substances

  • Environmental Pollutants
  • HSP27 Heat-Shock Proteins
  • Proteome
  • Chromium
  • Neodymium