Normal prion protein has an activity like that of superoxide dismutase
Normal prion protein has an activity like that of superoxide dismutase
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DOI：
10.1042/0264-6021:3440001
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发表时间：
1999-11-15
影响因子：
4.1
通讯作者：
Jones, IM
中科院分区：
文献类型：
--
作者：
Brown, DR;Wong, BS;Jones, IM
我们在这里表明，无论是作为重组蛋白还是从脑组织中免疫沉淀的小鼠PrPC蛋白都具有超氧化物歧化酶(SOD)活性。超氧化物歧化酶活性也与重组鸡PrPC相关，证实了序列相似性所提示的进化保守表型。PrPC在蛋白质折叠过程中获得的铜赋予了蛋白质上的SOD活性，但复性后加入铜则不能。PrPC依赖的超氧化物歧化酶活性通过铜结合相关的八肽重复区域的缺失而被取消。这些结果描述了PrPC的酶功能，与其细胞分布一致，并表明它在细胞对氧化应激的抵抗中具有直接作用。
We show here that mouse prion protein (PrPC) either as recombinant protein or immunoprecipitated from brain tissue has superoxide dismutase (SOD) activity. SOD activity was also associated with recombinant chicken PrPC confirming the evolutionary conserved phenotype suggested by sequence similarity. Acquisition of copper by PrPC during protein folding endowed SOD activity on the protein but the addition of copper following refolding did not. PrPC dependent SOD activity was abolished by deletion of the octapeptide-repeat region involved in copper binding. These results describe an enzymic function for PrPC consistent with its cellular distribution and suggest it has a direct role in cellular resistance to oxidative stress.