Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity

被引:384
|
作者
Brown, DR
SchulzSchaeffer, WJ
Schmidt, B
Kretzschmar, HA
机构
[1] UNIV GOTTINGEN,INST NEUROPATHOL,DEPT NEUROPATHOL,D-37075 GOTTINGEN,GERMANY
[2] UNIV GOTTINGEN,ZENTRUM BIOCHEM & MOL ZELLBIOL,D-37075 GOTTINGEN,GERMANY
关键词
D O I
10.1006/exnr.1997.6505
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
The cellular function of the prion protein (PrPC), a cell surface glycoprotein expressed in neurones and astrocytes, has not been elucidated. Cell culture experiments reveal that cerebellar cells lacking PrPC are more sensitive to oxidative stress and undergo cell death more readily than wild-type cells. This effect is reversible by treatment with vitamin E. In vivo studies show that the activity of Cu/Zn superoxide dismutase is reduced in Prnp gene-ablated (Pmp(0/0)) mice. Constitutively high Mn superoxide dismutase activity in these animals may compensate for this loss of responsiveness to oxidative stress. These findings suggest that PrPC may influence the activity of Cu/Zn superoxide dismutase and may be important for cellular resistance to oxidative stress. (C) 1997 Academic Press.
引用
收藏
页码:104 / 112
页数:9
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