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The Cellular Prion Protein Colocalizes with the Dystroglycan Complex in the Brain
: The function of PrPC, the cellular prion protein (PrP), is still unknown. Like other glycophosphatidylinositol‐anchored proteins, PrP resides on Triton‐insoluble, cholesterol‐rich membranous microdomains, termed rafts. We have recently shown that the activity and subcellular localization of the ne...
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Published in: | Journal of neurochemistry 2000-11, Vol.75 (5), p.1889-1897 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | : The function of PrPC, the cellular prion
protein (PrP), is still unknown. Like other glycophosphatidylinositol‐anchored
proteins, PrP resides on Triton‐insoluble, cholesterol‐rich membranous
microdomains, termed rafts. We have recently shown that the activity and
subcellular localization of the neuronal isoform of nitric oxide synthase
(nNOS) are impaired in adult PrP0/0 mice as well as in scrapie‐infected mice. In this study, we sought to determine whether PrP and nNOS are part of the same functional complex and, if so, to identify additional components of such a complex. To this aim, we looked for proteins that coimmunoprecipitated with PrP in the presence of detergents either that completely dissociate rafts, to identify stronger interactions, or that preserve the raft structure, to identify weaker interactions. Using this detergent‐dependent immunoprecipitation protocol we found that PrP interacts strongly with dystroglycan, a transmembrane protein that is the core of the dystrophin—glycoprotein complex (DGC). Additional results suggest that PrP also interacts with additional members of the DGC, including nNOS. PrP coprecipitated only with established presynaptic proteins, consistent with recent findings suggesting that PrP is a presynaptic protein. |
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ISSN: | 0022-3042 1471-4159 |
DOI: | 10.1046/j.1471-4159.2000.0751889.x |