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Prion protein fragment interacts with PrP‐deficient cells
Author(s) -
Brown David R.,
Schmidt Bernhard,
Kretzschmar Hans A.
Publication year - 1998
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/(sici)1097-4547(19980501)52:3<260::aid-jnr2>3.0.co;2-b
Subject(s) - biology , phenotype , colchicine , prion protein , tubulin , cell culture , microbiology and biotechnology , wild type , embryonic stem cell , cell type , cell , microtubule , genetics , gene , medicine , disease , pathology , mutant
A fragment of the prion protein (PrP106‐126) induces cell death in cultures of wild‐type embryonic day (E)16 mouse cortical neurons but not cells derived from mice devoid of cellular PrP(PrP o/o) . Two common binding partners for PrP106‐126 expressed in both wild‐type and PrP o/o mouse brain were isolated and their sequences determined. The two proteins were found to be α and β tubulin. Further evidence that tubulin binds PrP106‐126 within cells comes from cell culture experiments. Colchicine toxicity on PrP o/o mouse cortical cells is enhanced by PrP106‐126 and taxol enhances toxicity of PrP106‐126 on wild‐type mouse cortical cells. Our evidence shows that a fragment of PrP can bind a cellular protein and in so doing, alters the metabolism of cells even when they do not express native PrP. This indicates that PrP106‐126 is nontoxic to PrP o/o cells, not because of an inability to interact with these cells but because of the loss of some aspect of a PrP expression‐dependent phenotype. J. Neurosci. Res. 52:260–267, 1998. © 1998 Wiley‐Liss, Inc.