The N-Terminal Tandem Repeat Region of Human Prion Protein Reduces Copper: Role of Tryptophan Residues

Prion protein (PrP) has attracted considerable attention, mainly due to its involvement in transmissible spongiform encephalopathies. Toward its N-terminal region, PrP bears an octapeptide repeat which has been shown to bind copper. We found that a human synthetic peptide (PrP59–91), corresponding t...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 269; no. 2; pp. 491 - 495
Main Authors Ruiz, Francisca H., Silva, Eduardo, Inestrosa, Nibaldo C.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 16.03.2000
Subjects
Copper - metabolism
Humans
Oxidation-Reduction
Oxygen - metabolism
Prions - chemistry
Prions - genetics
Prions - metabolism
Tandem Repeat Sequences
Tryptophan - metabolism
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Summary:Prion protein (PrP) has attracted considerable attention, mainly due to its involvement in transmissible spongiform encephalopathies. Toward its N-terminal region, PrP bears an octapeptide repeat which has been shown to bind copper. We found that a human synthetic peptide (PrP59–91), corresponding to the four repeats of Pro-His-Gly-Gly-Gly-Trp-Gly-Gln has the ability to reduce copper. A mutant peptide lacking tryptophan displayed only 24% of the wild-type copper-reducing activity. Experiments performed in a N2 environment confirmed that O2 is not involved in the reaction. Our results indicated that cell surface PrP, besides its ability to bind copper, bears the capacity to reduce copper in vitro. The potential physiological role of copper reduction by PrP is discussed.
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ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.2000.2270