Neurotoxicity of prion peptide 106‐126 not confirmed

FEBS Letters

Christen, Philipp¹  Kunz, Beat¹  Sandmeier, Erika¹ 

[1] Biochemisches Institut der Universität Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland

关键词: Prion peptide PrP106-126;    Prion protein;    Neurotoxicity;    Cell culture;    Cortex;    Hippocampus;    Ara-C;    cytosine-arabinoside;    FCS;    fetal calf serum;    MTT;    3-(4;    5-dimethylthiazol-2-yl)-2;    5-diphenyltetrazolium bromide;    PrPSc;    scrapie isoform of the prion protein;    PrPc;    cellular isoform of the prion protein;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/S0014-5793(99)01123-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Prion-related diseases are accompanied by neurodegeneration, astroglial proliferation and formation of proteinase K-resistant aggregates of the scrapie isoform of the prion protein (PrP^Sc). The synthetic PrP fragment 106-126 was reported to be neurotoxic towards cultured rat hippocampal neurons (Forloni, G., Angeretti, N., Chiesa, R., Monzani, E., Salmona, M., Bugiani, O. and Tagliavini, F. (1993) Nature 362, 543–546) and mouse cortical cells (Brown, D.R., Herms, J. and Kretzschmar, H.A. (1994) Neuroreport 5, 2057–2060). However, we found the viability of these and other neuronal cell types not to be impaired in the presence of PrP106-126 under widely varied sets of conditions. Aged preparations of the peptide as well as synthetic deamidated and isomerized derivatives that correspond to the aging products of the peptide proved also to lack neurotoxicity. Apparently, PrP106-126 cannot serve as a model for the interaction of PrP with neuronal cells.

【 授权许可】

Unknown