The cardiac copper chaperone proteins Sco1 and CCS are up-regulated, but Cox 1 and Cox4 are down-regulated, by copper deficiency

Biol Trace Elem Res. 2011 Oct;143(1):368-77. doi: 10.1007/s12011-010-8858-z. Epub 2010 Sep 28.

Abstract

Copper is ferried in a cell complexed to chaperone proteins, and in the heart much copper is required for cytochrome c oxidase (Cox). It is not completely understood how copper status affects the levels of these proteins. Here we determined if dietary copper deficiency could up- or down-regulate select copper chaperone proteins and Cox subunits 1 and 4 in cardiac tissue of rats. Sixteen weanling male Long-Evans rats were randomized into treatment groups, one group receiving a copper-deficient diet (<1 mg Cu/kg diet) and one group receiving a diet containing adequate copper (6 mg Cu/kg diet) for 5 weeks. Hearts were removed, weighed, and non-myofibrillar proteins separated to analyze for levels of CCS, Sco1, Ctr1, Cox17, Cox1, and Cox4 by SDS-PAGE and Western blotting. No changes were observed in the concentrations of CTR1 and Cox17 between copper-adequate and copper-deficient rats. CCS and Sco1 were up-regulated and Cox1 and Cox4 were both down-regulated as a result of copper deficiency. These data suggest that select chaperone proteins and may be up-regulated, and Cox1 and 4 down-regulated, by a dietary copper deficiency, whereas others appear not to be affected by copper status.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cardiomegaly / metabolism
  • Copper / deficiency*
  • Copper / metabolism*
  • Cyclooxygenase 1 / metabolism*
  • Electron Transport Complex IV / metabolism*
  • Liver / metabolism
  • Male
  • Membrane Proteins / metabolism*
  • Molecular Chaperones / metabolism*
  • Rats
  • Rats, Long-Evans

Substances

  • Ccs protein, rat
  • Membrane Proteins
  • Molecular Chaperones
  • Copper
  • Cyclooxygenase 1
  • Ptgs1 protein, rat
  • Electron Transport Complex IV