Calreticulin Inhibits Prion Protein PrP-(23-98) Aggregation in Vitro

Because prion protein PrP-(23-98) was recently found to polymerize into amyloid-like and proteinase K-resistant spherical aggregates in the presence of NADPH plus copper ions, we tested to determine whether calreticulin (CRT) inhibits PrP-(23-98) aggregation in vitro. The results indicated that CRT...

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Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2011, Vol.75 (8), p.1625-1627
Hauptverfasser:	SHIRAISHI, Noriyuki, INAI, Yoko, HIRANO, Yoshiaki, IHARA, Yoshito
Format:	Artikel
Sprache:	eng
Schlagworte:	aggregates Amyloid - metabolism Biological and medical sciences calreticulin Calreticulin - pharmacology Calreticulin - therapeutic use Copper - adverse effects Copper - antagonists & inhibitors Copper - pharmacology Dose-Response Relationship, Drug Endopeptidase K - metabolism Fundamental and applied biological sciences. Psychology Humans NADP - adverse effects NADP - antagonists & inhibitors NADP - pharmacology Peptide Fragments - metabolism Plaque, Amyloid - metabolism Plaque, Amyloid - prevention & control Prion Diseases - drug therapy Prion Diseases - pathology prion protein Prions - metabolism Protein Binding - drug effects Protein Structure, Quaternary PrP-(23-98) Recombinant Proteins - genetics Recombinant Proteins - metabolism Solutions Spectrophotometry
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Zusammenfassung:	Because prion protein PrP-(23-98) was recently found to polymerize into amyloid-like and proteinase K-resistant spherical aggregates in the presence of NADPH plus copper ions, we tested to determine whether calreticulin (CRT) inhibits PrP-(23-98) aggregation in vitro. The results indicated that CRT suppressed PrP-(23-98) aggregation, and that CRT-mediated solubilization occurred in the aggregates.
ISSN:	0916-8451 1347-6947
DOI:	10.1271/bbb.110287