Ancient conserved domain protein-1 binds copper and modifies its retention in cells.

Alexandra Alderton; Paul Davies; Katie Illman; David R. Brown

doi:10.1111/j.1471-4159.2007.04751.x

Ancient conserved domain protein-1 binds copper and modifies its retention in cells.

Alexandra Alderton
, Paul Davies
, Katie Illman
, David R. Brown (Lead / Corresponding author)

Research output: Contribution to journal › Article › peer-review

13 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	312-321
Number of pages	10
Journal	Journal of Neurochemistry
Volume	103
Issue number	1
Early online date	9 Jun 2007
DOIs	https://doi.org/10.1111/j.1471-4159.2007.04751.x
Publication status	Published - Oct 2007

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title = "Ancient conserved domain protein-1 binds copper and modifies its retention in cells.",

abstract = "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.",

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AU - Alderton, Alexandra

AU - Davies, Paul

AU - Illman, Katie

AU - Brown, David R.

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AB - 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.

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SP - 312

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JO - Journal of Neurochemistry

JF - Journal of Neurochemistry

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Ancient conserved domain protein-1 binds copper and modifies its retention in cells.

Abstract

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