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Blood, 15 May 2006, Vol. 107, No. 10, pp. 3907-3911. Prepublished online as a Blood First Edition Paper on January 24, 2006; DOI 10.1182/blood-2005-02-0802. This Article Full Text Full Text (PDF) All Versions of this Article: 2005-02-0802v1 107/10/3907    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map 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 Robertson, C. Articles by McNicol, A. Search for Related Content PubMed PubMed Citation Articles by Robertson, C. Articles by McNicol, A. Related Collections Hemostasis, Thrombosis, and Vascular Biology Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Cellular prion protein is released on exosomes from activated platelets Catherine Robertson, Stephanie A. Booth, Daniel R. Beniac, Michael B. Coulthart, Timothy F. Booth, and Archibald McNicol From the Department of Oral Biology, University of Manitoba, Winnipeg, MB, Canada; the Department of Medical Microbiology, University of Manitoba, Winnipeg, MB, Canada; the Department of Pharmacology and Therapeutics, University of Manitoba, Winnipeg, MB, Canada; the Division of Host Genetics and Prion Diseases, Canadian Science Centre for Human and Animal Health, Winnipeg, MB, Canada; and the Division of Viral Diseases, Canadian Science Centre for Human and Animal Health, Winnipeg, MB, Canada. Cellular prion protein (PrPC) is a glycophosphatidylinositol (GPI)–anchored protein, of unknown function, found in a number of tissues throughout the body, including several blood components of which platelets constitute the largest reservoir in humans. It is widely believed that a misfolded, protease-resistant form of PrPC, PrPSc, is responsible for the transmissible spongiform encephalopathy (TSE) group of fatal neurodegenerative diseases. Although the pathogenesis of TSEs is poorly understood, it is known that PrPC must be present in order for the disease to progress; thus, it is important to determine the physiologic function of PrPC. Resolving the location of PrPC in blood will provide valuable clues as to its function. PrPC was previously shown to be on the alpha granule membrane of resting platelets. In the current study platelet activation led to the transient expression of PrPC on the platelet surface and its subsequent release on both microvesicles and exosomes. The presence of PrPC on platelet-derived exosomes suggests a possible mechanism for PrPC transport in blood and for cell-to-cell transmission. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: R. Linden, V. R. Martins, M. A. M. Prado, M. Cammarota, I. Izquierdo, and R. R. Brentani Physiology of the Prion Protein Physiol Rev, April 1, 2008; 88(2): 673 - 728. [Abstract] [Full Text] [PDF] W. M. Dlakic, E. Grigg, and R. A. Bessen Prion Infection of Muscle Cells In Vitro J. Virol., May 1, 2007; 81(9): 4615 - 4624. [Abstract] [Full Text] [PDF] G. van Niel, I. Porto-Carreiro, S. Simoes, and G. Raposo Exosomes: a common pathway for a specialized function. J. Biochem., July 1, 2006; 140(1): 13 - 21. [Abstract] [Full Text] [PDF]

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