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This Article 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 Bonfanti, R. Articles by Wagner, D. D. Search for Related Content PubMed PubMed Citation Articles by Bonfanti, R. Articles by Wagner, D. D. Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  PADGEM (GMP140) is a component of Weibel-Palade bodies of human endothelial cells R Bonfanti, BC Furie, B Furie and DD Wagner Center for Hemostasis and Thrombosis Research, New England Medical Center, Boston, MA 02111. PADGEM protein (PADGEM), also known as GMP140, is a platelet alpha- granule membrane protein that is translocated to the external membrane after platelet activation. Although the biosynthesis of this protein was originally thought to be confined to megakaryocytes, the synthesis of PADGEM in endothelial cells was recently demonstrated (McEver et al: Blood 70:1974a, 1987). We now describe the subcellular localization of this protein in endothelial cells. Immunofluorescence staining of permeabilized human umbilical vein endothelial cells with KC4, a well characterized monoclonal antibody to PADGEM, showed positively stained elongated structures similar in distribution and shape to Weibel-Palade bodies. Their identity as Weibel-Palade bodies was confirmed by double label immunofluorescence using KC4 and a polyclonal antiserum to von Willebrand factor (vWf), a protein known to be specifically stored in these organelles. All Weibel-Palade bodies were found to contain PADGEM. In contrast to strong perinuclear staining produced with anti- vWf antibodies, no significant perinuclear staining was obtained with KC4, indicating that relatively little PADGEM is present in the endoplasmic reticulum and in the Golgi apparatus. In endothelial cells treated with secretagogues that stimulate vWf release the elongated structures positive for PADGEM disappeared, further identifying these structures as Weibel-Palade bodies. This observation extends the parallels between Weibel-Palade bodies and alpha-granules and suggests a possible functional association between vWf and PADGEM. Volume 73, Issue 5, pp. 1109-1112, 04/01/1989 Copyright © 1989 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: H. Yang, S. Lang, Z. Zhai, L. Li, W. H. A. Kahr, P. Chen, J. Brkic, C. M. Spring, M. J. Flick, J. L. Degen, et al. 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Berliner Induction of P-Selectin by Oxidized Lipoproteins : Separate Effects on Synthesis and Surface Expression Circ. Res., June 19, 1997; 80(6): 810 - 818. [Abstract] [Full Text] K. E. Pedersen, B. S. Bochner, and B. J. Undem Cysteinyl Leukotrienes Induce P-Selectin Expression in Human Endothelial Cells via a Non-CysLT1 Receptor-Mediated Mechanism J. Pharmacol. Exp. Ther., May 1, 1997; 281(2): 655 - 662. [Abstract] [Full Text] K. Fujise, B. M. Revelle, L. Stacy, E. L. Madison, E. T.H. Yeh, J. T. Willerson, and P. J. Beck A Tissue Plasminogen Activator/P-Selectin Fusion Protein Is an Effective Thrombolytic Agent Circulation, February 4, 1997; 95(3): 715 - 722. [Abstract] [Full Text] Y. H. Datta, M. Romano, B. C. Jacobson, D. E. Golan, C. N. Serhan, and B. M. Ewenstein Peptido-Leukotrienes Are Potent Agonists of von Willebrand Factor Secretion and P-Selectin Surface Expression in Human Umbilical Vein Endothelial Cells Circulation, December 1, 1995; 92(11): 3304 - 3311. 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Bevilacqua Quantitative Determination of Selectin-Carbohydrate Interactions Cold Spring Harb Symp Quant Biol, January 1, 1992; 57(0): 271 - 279. [Abstract] [PDF] Gamble JR, M. Skinner, M. Berndt, and M. Vadas Prevention of activated neutrophil adhesion to endothelium by soluble adhesion protein GMP140 Science, July 27, 1990; 249(4967): 414 - 417. [Abstract] [PDF] C. V. Denis, P. Andre, S. Saffaripour, and D. D. Wagner Defect in regulated secretion of P-selectin affects leukocyte recruitment in von Willebrand factor-deficient mice PNAS, March 27, 2001; 98(7): 4072 - 4077. [Abstract] [Full Text] [PDF]

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