TAILIEUCHUNG - Báo cáo khoa học: Mapping the functional domain of the prion protein

Prion diseases such as Creutzfeldt–Jakob disease are pos-sibly caused by the conversion of a normal cellular glyco-protein, the prion protein (PrP c ) into an abnormal isoform (PrP Sc ). The process that causes this conversion is unknown, but to understand it requires a detailed insight into the normal activity of PrP c . It has become accepted from results of numerous studies that PrP c is a Cu-binding protein and that its normal function requires Cu. | Eur. J. Biochem. 270 3368-3376 2003 FEBS 2003 doi Mapping the functional domain of the prion protein Taian Cui1. Maki Daniels2 Boon Sena Wona3. Ruliana Li3. Man-Sun Sv3. Judvth Sassoon1 and David R. Brown1 2 1 Department of Biology and Biochemistry University of Bath UK 2Department of Biochemistry Cambridge University UK 3Institute of Pathology Case Western Reserve University School of Medicine Cleveland Ohio USA Prion diseases such as Creutzfeldt-Jakob disease are possibly caused by the conversion of a normal cellular glycoprotein the prion protein PrPc into an abnormal isoform PrPSc . The process that causes this conversion is unknown but to understand it requires a detailed insight into the normal activity of PrPc. It has become accepted from results of numerous studies that PrPc is a Cu-binding protein and that its normal function requires Cu. Further work has suggested that PrPc is an antioxidant with an activity like that of a superoxide dismutase. We have shown in this investigation that this activity is optimal for the whole protein and that deletion of parts of the protein reduce or abolish this activity. The protein therefore contains an active domain requiring certain regions such as the Cu-binding octameric repeat region and the hydrophobic core. These regions show high evolutionary conservation fitting with the idea that they are important to the active domain of the protein. Keywords copper Creutzfeldt-Jakob disease oxidative stress scrapie superoxide dismutase. Neurodegenerative diseases are a major threat to human health. One group of disease termed prion diseases 1 2 make up a small percentage of all human neurodegenerative diseases. Prion diseases have become a major concern because of the possibility that one particular from variant Creutzfeldt-Jacob disease vCJD might arise through transmission of an animal disease such as bovine spongiform encephalopathy 3 to humans 4 . Other prion diseases include the sheep .

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