Premium
Ancient conserved domain protein‐1 binds copper and modifies its retention in cells
Author(s) -
Alderton Alexandra,
Davies Paul,
Illman Katie,
Brown David R.
Publication year - 2007
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2007.04751.x
Subject(s) - isothermal titration calorimetry , copper , cytoplasm , chemistry , biochemistry , subcellular localization , chaperone (clinical) , metal , affinity chromatography , plasma protein binding , transport protein , biophysics , biology , enzyme , medicine , organic chemistry , pathology
The ancient conserved domain protein (ACDP) family are a recently identified group of homologous mammalian proteins. Some family members have been suggested to have roles in the metabolism of metals. We investigated the capacity of ACDP‐1 to bind metals. Using immobilised metal affinity chromatography and isothermal titration calorimetry we determined that ACDP‐1 is a high affinity copper binding protein able to bind copper at nanomolar concentrations. In addition the promoter of ACDP‐1 contains metal response elements and the cellular expression of ACDP‐1 alters cellular retention of copper. However, cellular expression of ACDP‐1 does not alter cellular resistance to the toxicity of copper or other metals. As our findings place the subcellular localisation of ACDP‐1 in the cytoplasm it is possible that ACDP‐1 represent a novel copper chaperone or storage protein.