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

    Alderton, Alexandra / Davies, Paul / Illman, Katie / Brown, David R

    Journal of neurochemistry

    2007  Volume 103, Issue 1, Page(s) 312–321

    Abstract: ... response elements and the cellular expression of ACDP-1 alters cellular retention of copper. However, cellular ... The ancient conserved domain protein (ACDP) family are a recently identified group of homologous ... isothermal titration calorimetry we determined that ACDP-1 is a high affinity copper binding protein able ...

    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.
    MeSH term(s) Amino Acid Sequence ; Animals ; COS Cells ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cation Transport Proteins ; Cell Line ; Cercopithecus aethiops ; Cloning, Molecular ; Copper/metabolism ; Copper/toxicity ; Cyclins/genetics ; Cyclins/metabolism ; Cytoplasm/metabolism ; Metals, Heavy/toxicity ; Mice ; Molecular Sequence Data ; Sequence Homology, Amino Acid
    Chemical Substances ACDP-1 protein, mouse ; Carrier Proteins ; Cation Transport Proteins ; Cyclins ; Metals, Heavy ; Copper (789U1901C5)
    Language English
    Publishing date 2007-10
    Publishing country England
    Document type Journal Article
    ZDB-ID 80158-6
    ISSN 1471-4159 ; 0022-3042 ; 1474-1644
    ISSN (online) 1471-4159
    ISSN 0022-3042 ; 1474-1644
    DOI 10.1111/j.1471-4159.2007.04751.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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

    Alderton, Alexandra / Davies, Paul / Illman, Katie / Brown, David R

    Journal of neurochemistry. 2007 Oct., v. 103, no. 1

    2007  

    Abstract: ... response elements and the cellular expression of ACDP-1 alters cellular retention of copper. However, cellular ... The ancient conserved domain protein (ACDP) family are a recently identified group of homologous ... isothermal titration calorimetry we determined that ACDP-1 is a high affinity copper binding protein able ...

    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.
    Keywords copper
    Language English
    Dates of publication 2007-10
    Size p. 312-321.
    Publisher Blackwell Publishing Ltd
    Publishing place Oxford, UK
    Document type Article
    ZDB-ID 80158-6
    ISSN 1471-4159 ; 0022-3042 ; 1474-1644
    ISSN (online) 1471-4159
    ISSN 0022-3042 ; 1474-1644
    DOI 10.1111/j.1471-4159.2007.04751.x
    Database NAL-Catalogue (AGRICOLA)

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