Cellular prion protein is released on exosomes from activated platelets

DOI PDF 被引用文献2件
  • Catherine Robertson
    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.
  • Stephanie A. Booth
    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.
  • Daniel R. Beniac
    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.
  • Michael B. Coulthart
    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.
  • Timothy F. Booth
    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.
  • 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.

抄録

<jats:p>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.</jats:p>

収録刊行物

  • Blood

    Blood 107 (10), 3907-3911, 2006-05-15

    American Society of Hematology

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