SEARCH:   Advanced

This Article Full Text Full Text (PDF) 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 Dodelet, V. C. Articles by Cashman, N. R. Search for Related Content PubMed PubMed Citation Articles by Dodelet, V. C. Articles by Cashman, N. R. Related Collections Hematopoiesis and Stem Cells Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Prion Protein Expression in Human Leukocyte Differentiation Vincent C. Dodelet and Neil R. Cashman From the Department of Microbiology and Immunology, the Department of Neurology and Neurosurgery, Montreal Neurological Institute and Hospital, McGill University, Montreal, Québec, Canada. The cellular isoform of the prion protein (PrPC) is a small glycoprotein attached to the outer leaflet of the plasma membrane by a glycosylphosphatidylinositol anchor. This molecule is involved in the pathogenesis of prion diseases in both humans and animals. We have characterized the expression patterns of PrPC during human leukocyte maturation by flow cytometry with monoclonal antibodies to PrPC, the glycan moiety CD15, and the stem cell marker CD34. We observe that prion protein is present on CD34+ bone marrow (BM) stem cells. Although lymphocytes and monocytes maintain PrPC expression throughout their differentiation, PrPC is downregulated upon differentiation along the granulocyte lineage. In vitro retinoic acid-induced differentiation of the premyeloid line HL-60 into granulocyte-like cells mimics the suppression of PrPC in granulocyte differentiation, as both PrPC mRNA and protein are downregulated. These data suggest that selected BM cells and peripheral mononuclear cells may support prion agent replication, because this process is dependent on availability of PrPC. Additionally, retinoic acid-induced extinction of PrPC expression in HL-60 cells provides a potential model to study PrP gene regulation and protein function. Finally, these data suggest the existence of cell-specific glycoforms of PrPC that may determine cellular susceptibility to infection by the prion agent. Blood, Vol. 91 No. 5 (March 1), 1998: pp. 1556-1561 © 1998 by The American Society of Hematology. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: S. Tsutsui, J. N. Hahn, T. A. Johnson, Z. Ali, and F. R. Jirik Absence of the Cellular Prion Protein Exacerbates and Prolongs Neuroinflammation in Experimental Autoimmune Encephalomyelitis Am. J. Pathol., October 1, 2008; 173(4): 1029 - 1041. [Abstract] [Full Text] [PDF] 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] G. Martinez del Hoyo, M. Lopez-Bravo, P. Metharom, C. Ardavin, and P. Aucouturier Prion Protein Expression by Mouse Dendritic Cells Is Restricted to the Nonplasmacytoid Subsets and Correlates with the Maturation State J. Immunol., November 1, 2006; 177(9): 6137 - 6142. [Abstract] [Full Text] [PDF] C. C. Zhang, A. D. Steele, S. Lindquist, and H. F. Lodish Prion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewal PNAS, February 14, 2006; 103(7): 2184 - 2189. [Abstract] [Full Text] [PDF] S. Paltrinieri, S. Comazzi, V. Spagnolo, M. Rondena, W. Ponti, and F. Ceciliani Bovine Doppel (Dpl) and Prion Protein (PrP) Expression on Lymphoid Tissue and Circulating Leukocytes J. Histochem. Cytochem., December 1, 2004; 52(12): 1639 - 1645. [Abstract] [Full Text] [PDF] K. Holada, J. G. Vostal, P. W. Theisen, C. MacAuley, L. Gregori, and R. G. Rohwer Scrapie Infectivity in Hamster Blood Is Not Associated with Platelets J. Virol., March 27, 2002; 76(9): 4649 - 4650. [Abstract] [Full Text] [PDF] A. M. Thackray and R. Bujdoso PrPc Expression Influences the Establishment of Herpes Simplex Virus Type 1 Latency J. Virol., March 1, 2002; 76(5): 2498 - 2509. [Abstract] [Full Text] [PDF] A. L. B. Cabral, K. S. Lee, and V. R. Martins Regulation of the Cellular Prion Protein Gene Expression Depends on Chromatin Conformation J. Biol. Chem., February 8, 2002; 277(7): 5675 - 5682. [Abstract] [Full Text] [PDF] J. Burthem, B. Urban, A. Pain, and D. J. Roberts The normal cellular prion protein is strongly expressed by myeloid dendritic cells Blood, December 15, 2001; 98(13): 3733 - 3738. [Abstract] [Full Text] [PDF] M. B. Coulthart and N. R. Cashman Variant Creutzfeldt-Jakob disease: a summary of current scientific knowledge in relation to public health Can. Med. Assoc. J., July 1, 2001; 165(1): 51 - 58. [Abstract] [Full Text] [PDF] D. A. Harris Cellular Biology of Prion Diseases Clin. Microbiol. Rev., July 1, 1999; 12(3): 429 - 444. [Abstract] [Full Text] [PDF] P. C. Pauly and D. A. Harris Copper Stimulates Endocytosis of the Prion Protein J. Biol. Chem., December 11, 1998; 273(50): 33107 - 33110. [Abstract] [Full Text] [PDF]

	Copyright © 1998 by American Society of Hematology         Online ISSN: 1528-0020