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Prion protein expression aids cellular uptake and veratridine‐induced release of copper
Author(s) -
Brown David R.
Publication year - 1999
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(19991201)58:5<717::aid-jnr13>3.0.co;2-s
Subject(s) - veratridine , copper , synapse , chemistry , microbiology and biotechnology , biophysics , biology , biochemistry , neuroscience , sodium , organic chemistry , sodium channel
The function of the prion protein is unknown despite suggestions it binds copper. Radioactive copper (Cu 67 ) was used to demonstrate that histidine‐dependent uptake of copper by cerebellar cells in culture is related to the level of PrP c expression. Copper is released by neurones at the synapse. Veratridine‐induced release from synapses was proportional to the level of PrP c expression. Veratridine‐induced release can be abolished only from PrP c expressing cells by pretreatment with phosphatidyl‐specific phospholipase C, an enzyme that cleaves PrP c from the cell surface. These results suggest that PrP c aids cellular copper uptake and may have a function at the synapse related to release of copper during transmission. J. Neurosci. Res. 58:717–725, 1999. © 1999 Wiley‐Liss, Inc.