Octapeptide repeat region and N-terminal half of hydrophobic region of prion protein (PrP) mediate PrP-dependent activation of superoxide dismutase
Cellular prion protein PrP C contains two evolutionarily conserved domains among mammals; viz., the octapeptide repeat region (OR; amino acid residue 51–90) and the hydrophobic region (HR; amino acid residue 112–145). Accumulating evidence indicates that PrP C acts as an inhibitor of apoptosis and r...
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Published in | Biochemical and biophysical research communications Vol. 326; no. 3; pp. 600 - 606 |
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Main Authors | , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
21.01.2005
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Subjects | |
Online Access | Get full text |
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Summary: | Cellular prion protein PrP
C contains two evolutionarily conserved domains among mammals; viz., the octapeptide repeat region (OR; amino acid residue 51–90) and the hydrophobic region (HR; amino acid residue 112–145). Accumulating evidence indicates that PrP
C acts as an inhibitor of apoptosis and regulator of superoxide dismutase (SOD) activity. To further understand how PrP
C activates SOD and prevents apoptosis, we provide evidence here that OR and N-terminal half of HR mediate PrP
C-dependent SOD activation and anti-apoptotic function. Removal of the OR (amino acid residue 53–94) enhances apoptosis and decreases SOD activity. Deletion of the N-terminal half of HR (amino acids residue 95–132) abolishes its ability to activate SOD and to prevent apoptosis, whereas that of the C-terminal half of HR (amino acids residue 124–146) has little if any effect on the anti-apoptotic activity and SOD activation. These data are consistent with a model in which the anti-apoptotic and anti-oxidative function of PrP
C is regulated by not only OR but also the N-terminal half of HR. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/j.bbrc.2004.11.092 |