Prion protein expression and superoxide dismutase activity

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چکیده

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Prion protein expression and superoxide dismutase activity.

The function of the prion protein (PrPc) remains uncertain. It has been suggested that prion protein expression may aid cellular resistance to oxidative stress by influencing the activity of Cu/Zn superoxide dismutase (Cu,Zn SOD). The activity of Cu,Zn SOD was investigated in mice with different levels of PrPc expression. Increasing levels of PrPc expression were linked to increased levels of C...

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GPI-anchorless human prion protein is secreted and glycosylated but lacks superoxide dismutase activity.

Prion protein (PrP) is a glycosylphosphatidylinositol (GPI)-anchored membrane protein that is thought to play a role in anti-oxidative stress. It remains controversial whether PrP elicits superoxide dismutase (SOD) activity itself or indirectly by activating cellular SOD. Our previous studies showed that soluble PrP produced by a baculovirus expression system did not exhibit any SOD activity in...

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Normal prion protein has an activity like that of superoxide dismutase.

We show here that mouse prion protein (PrP(C)) either as recombinant protein or immunoprecipitated from brain tissue has superoxide dismutase (SOD) activity. SOD activity was also associated with recombinant chicken PrP(C) confirming the evolutionary conserved phenotype suggested by sequence similarity. Acquisition of copper by PrP(C) during protein folding endowed SOD activity on the protein b...

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Prenatal hypoxia decreases lung extracellular superoxide dismutase expression and activity.

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1998

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj3340423