Copper accumulation and compartmentalization in mouse fibroblast lacking metallothionein and copper chaperone, Atox1

Toxicol Appl Pharmacol. 2009 Jun 1;237(2):205-13. doi: 10.1016/j.taap.2009.03.024. Epub 2009 Apr 9.

Abstract

Copper (Cu) is the active center of some enzymes because of its redox-active property, although that property could have harmful effects. Because of this, cells have strict regulation/detoxification systems for this metal. In this study, multi-disciplinary approaches, such as speciation and elemental imaging of Cu, were applied to reveal the detoxification mechanisms for Cu in cells bearing a defect in Cu-regulating genes. Although Cu concentration in metallothionein (MT)-knockout cells was increased by the knockdown of the Cu chaperone, Atox1, the concentrations of the Cu influx pump, Ctr1, and another Cu chaperone, Ccs, were paradoxically increased; namely, the cells responded to the Cu deficiency despite the fact that cellular Cu concentration was actually increased. Cu imaging showed that the elevated Cu was compartmentalized in cytoplasmic vesicles. Together, the results point to the novel roles of MT and cytoplasmic vesicles in the detoxification of Cu in mammalian cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cation Transport Proteins / genetics*
  • Cation Transport Proteins / metabolism
  • Cell Line
  • Copper / metabolism
  • Copper / toxicity*
  • Copper Transport Proteins
  • Copper Transporter 1
  • Fibroblasts / metabolism*
  • Gene Expression Regulation
  • Gene Silencing
  • Metallothionein / genetics*
  • Metallothionein / metabolism
  • Mice
  • Mice, Knockout
  • Molecular Chaperones / genetics*
  • Molecular Chaperones / metabolism
  • RNA, Small Interfering

Substances

  • Atox1 protein, mouse
  • Cation Transport Proteins
  • Ccs protein, mouse
  • Copper Transport Proteins
  • Copper Transporter 1
  • Molecular Chaperones
  • RNA, Small Interfering
  • Slc31a1 protein, mouse
  • Copper
  • Metallothionein