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Blood, 15 December 2007, Vol. 110, No. 13, pp. 4518-4525. Prepublished online as a Blood First Edition Paper on September 7, 2007; DOI 10.1182/blood-2007-04-085183. This Article Full Text (PDF) All Versions of this Article: blood-2007-04-085183v1 110/13/4518    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Griffiths, R. E Articles by Anstee, D. J. Search for Related Content PubMed PubMed Citation Articles by Griffiths, R. E Articles by Anstee, D. J. Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted April 12, 2007 Accepted September 3, 2007 Normal prion protein trafficking in cultured human erythroblasts Rebecca E Griffiths, Kate J Heesom, and David J. Anstee* Bristol Institute for Transfusion Sciences, National Blood Service, Bristol, United Kingdom Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol, United Kingdom * Corresponding author; email: david.anstee{at}nbs.nhs.uk. Normal prion protein (PrPc), an essential substrate for development of prion disease, is widely distributed in hemopoietic cells. Recent evidence that variant Creutzfeldt-Jakob disease can be transmitted by transfusion of red cell preparations has highlighted the need for a greater understanding of the biology of PrPc in blood and blood forming tissues. Here we show that in contrast to another glycosylphosphoinositol-anchored protein CD59, PrPc at the cell surface of cultured human erythroblasts is rapidly internalised through the endosomal pathway where it colocalises with the tetraspanin CD63. In the plasma membrane PrPc colocalises with the tetraspanin CD81. Cross-linking with anti- PrPc or anti-CD81 causes clustering of PrPc and CD81 suggesting they can share the same microdomain. These data are consistent with a role for tetraspanin-enriched microdomains in trafficking of PrPc. These results, when taken together with recent evidence that exosomes released from cells as a result of endosomal-mediated recycling to the plasma membrane contain prion infectivity, provide a pathway for the propagation of prion diseases. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: G.-J. Wang, Y. Liu, A. Qin, S. V. Shah, Z.-b. Deng, X. Xiang, Z. Cheng, C. Liu, J. Wang, L. Zhang, et al. Thymus Exosomes-Like Particles Induce Regulatory T Cells J. Immunol., October 15, 2008; 181(8): 5242 - 5248. [Abstract] [Full Text] [PDF]

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