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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 Holada, K. Articles by Vostal, J. G. Search for Related Content PubMed PubMed Citation Articles by Holada, K. Articles by Vostal, J. G. Related Collections Brief Reports Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 1 July 2002, Vol. 100, No. 1, pp. 341-343 BRIEF REPORT Activated platelets of patients with paroxysmal nocturnal hemoglobinuria express cellular prion protein Karel Holada, Jan Simak, Antonio M. Risitano, Jaroslaw Maciejewski, Neal S. Young, and Jaroslav G. Vostal From the Laboratory of Cellular Hematology, Division of Hematology, Center for Biologics Evaluation and Research, Food and Drug Administration, and the Hematology Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD. Cellular prion protein (PrPc) is a glycosylphosphatidylinositol (GPI)-anchored membrane glycoprotein that contains a putative membrane-spanning section. Patients with paroxysmal nocturnal hemoglobinuria (PNH) lack GPI proteins on the surface of somatically mutated hematopoietic stem cell and its progeny. Platelet expression of PrPc was studied in 8 PNH patients. Resting PNH (CD55) platelets were devoid of surface PrPc, but activation of platelets resulted in the surface expression of PrPc. Expressed PrPc was detected by 2 monoclonal antibodies (mAbs) against the N-terminal part of the molecule but not by mAb 6H4, which binds at the C-terminus beyond the membrane-spanning section. However, 6H4 detected PrPc on Western blots of PNH platelets, demonstrating that the lack of 6H4 binding was not caused by PrPc truncation. Our results indicate that in the absence of GPI anchor, PrPc can be expressed intracellularly and up-regulated on the platelet membrane, likely in a transmembrane form with the C-terminal part of the molecule inserted into the cytoplasm. © 2002 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: 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] J. Villagra, S. Shiva, L. A. Hunter, R. F. Machado, M. T. Gladwin, and G. J. Kato Platelet activation in patients with sickle disease, hemolysis-associated pulmonary hypertension, and nitric oxide scavenging by cell-free hemoglobin Blood, September 15, 2007; 110(6): 2166 - 2172. [Abstract] [Full Text] [PDF] J Franklin, A Pluetschow, M Paus, L Specht, A-P Anselmo, A Aviles, G Biti, T Bogatyreva, G Bonadonna, C Brillant, et al. Second malignancy risk associated with treatment of Hodgkin's lymphoma: meta-analysis of the randomised trials Ann. Onc., December 1, 2006; 17(12): 1749 - 1760. [Abstract] [Full Text] [PDF] A. Josting, L. Nogova, J. Franklin, J.-P. Glossmann, H. T. Eich, M. Sieber, T. Schober, H.-D. Boettcher, U. Schulz, R.-P. Muller, et al. Salvage Radiotherapy in Patients With Relapsed and Refractory Hodgkin's Lymphoma: A Retrospective Analysis From the German Hodgkin Lymphoma Study Group J. Clin. Oncol., March 1, 2005; 23(7): 1522 - 1529. [Abstract] [Full Text] [PDF] E. Vassella, P. Butikofer, M. Engstler, J. Jelk, and I. Roditi Procyclin Null Mutants of Trypanosoma brucei Express Free Glycosylphosphatidylinositols on Their Surface Mol. Biol. Cell, April 1, 2003; 14(4): 1308 - 1318. [Abstract] [Full Text] [PDF]

	Copyright © 2002 by American Society of Hematology         Online ISSN: 1528-0020