Alderton Alexandra, Davies Paul, Illman Katie, Brown David R
Department of Biology and Biochemistry, University of Bath, Bath, UK.
J Neurochem. 2007 Oct;103(1):312-21. doi: 10.1111/j.1471-4159.2007.04751.x. Epub 2007 Jul 2.
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.
古老保守结构域蛋白（ACDP）家族是最近发现的一组同源哺乳动物蛋白。一些家族成员被认为在金属代谢中发挥作用。我们研究了ACDP-1结合金属的能力。通过固定化金属亲和色谱法和等温滴定量热法，我们确定ACDP-1是一种高亲和力铜结合蛋白，能够在纳摩尔浓度下结合铜。此外，ACDP-1的启动子含有金属反应元件，ACDP-1的细胞表达会改变细胞对铜的保留。然而，ACDP-1的细胞表达不会改变细胞对铜或其他金属毒性的抗性。由于我们的研究结果表明ACDP-1的亚细胞定位在细胞质中，因此ACDP-1有可能代表一种新型的铜伴侣蛋白或储存蛋白。
