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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.
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Submitted February 28, 2005
Accepted January 13, 2006
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*
Department of Oral Biology, University of Manitoba, Winnipeg, Manitoba, Canada; Division of Host Genetics & Prion Diseases, Canadian Science Centre for Human & Animal Health, Winnipeg, Manitoba, Canada
Division of Host Genetics & Prion Diseases, Canadian Science Centre for Human & Animal Health, Winnipeg, Manitoba, Canada; Department of Medical Microbiology, University of Manitoba, Winnipeg, Manitoba, Canada
Division of Viral Diseases, Canadian Science Centre for Human & Animal Health, Winnipeg, Manitoba, Canada
Department of Medical Microbiology, University of Manitoba, Winnipeg, Manitoba, Canada; Division of Viral Diseases, Canadian Science Centre for Human & Animal Health, Winnipeg, Manitoba, Canada
Department of Oral Biology, University of Manitoba, Winnipeg, Manitoba, Canada; Department of Pharmacology & Therapeutics, University of Manitoba, Winnipeg, Manitoba, Canada
* Corresponding author; email: mcnicol{at}ms.umanitoba.ca.
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 mis-folded, 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, and thus it is important to determine the physiological 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.

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