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Blood, 1 September 2004, Vol. 104, No. 5, pp. 1396-1403. Prepublished online as a Blood First Edition Paper on May 6, 2004; DOI 10.1182/blood-2004-02-0437. This Article Full Text Full Text (PDF) All Versions of this Article: 2004-02-0437v1 104/5/1396    most recent 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 Majstoravich, S. Articles by Higgs, H. N. Search for Related Content PubMed PubMed Citation Articles by Majstoravich, S. Articles by Higgs, H. N. Related Collections Cytoskeleton Immunobiology Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  IMMUNOBIOLOGY Lymphocyte microvilli are dynamic, actin-dependent structures that do not require Wiskott-Aldrich syndrome protein (WASp) for their morphology Sonja Majstoravich, Jinyi Zhang, Susan Nicholson-Dykstra, Stefan Linder, Wilhelm Friedrich, Katherine A. Siminovitch, and Henry N. Higgs From the Department of Biochemistry, Dartmouth Medical School, Hanover, NH; the Departments of Medicine, Immunology, and Medical Genetics and Microbiology, Univerisity of Toronto, Toronto, ON, Canada; Samuel Lunenfeld and Toronto General Research Institutes, Toronto, ON, Canada; Institut fuer Prophylaxe und Epidemiologie der Kreislaufkrankheiten, Ludwig-Maximilians-Universitaet, Muenchen, Germany; and Universitätskinderklinik, Ulm, Germany. Short microvilli cover the surfaces of circulating mammalian lymphocytes. The surfaces of monocytes and neutrophils are very different, containing ruffles as their predominant structure. In this study, we present the first quantitative characterization of lymphocyte microvilli. From analysis of scanning electron micrographs, we find that median microvillar length and surface density range from 0.3 to 0.4 µm and 2 to 4 microvilli/µm2, respectively, on lymphocytes from a variety of sources. As with similar structures from other cells, lymphocyte microvilli contain parallel bundles of actin filaments. Lymphocyte microvilli rapidly disassemble when exposed to the actin-sequestering molecule, Latrunculin A. This disassembly parallels cellular actin filament depolymerization and is complete within 2 minutes, suggesting that lymphocyte microvilli undergo continuous assembly and disassembly. In contrast to previous reports suggesting lymphocyte microvillar density to be reduced on lymphocytes from Wiskott-Aldrich syndrome (WAS) patient, we find no such deficiency in either mouse or human WAS protein (WASp)–deficient lymphocytes. These results suggest that WASp is either not involved in or is redundant in the rapid dynamics of lymphocyte microvilli. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: The core of the lymphocyte microvilli–WASp issue James R. Bartles Blood 2004 104: 1232-1233. [Full Text] [PDF] This article has been cited by other articles: B. Guezguez, P. Vigneron, N. Lamerant, C. Kieda, T. Jaffredo, and D. Dunon Dual Role of Melanoma Cell Adhesion Molecule (MCAM)/CD146 in Lymphocyte Endothelium Interaction: MCAM/CD146 Promotes Rolling via Microvilli Induction in Lymphocyte and Is an Endothelial Adhesion Receptor J. Immunol., November 15, 2007; 179(10): 6673 - 6685. [Abstract] [Full Text] [PDF] S. Tsuboi A Complex of Wiskott-Aldrich Syndrome Protein with Mammalian Verprolins Plays an Important Role in Monocyte Chemotaxis. J. Immunol., June 1, 2006; 176(11): 6576 - 6585. [Abstract] [Full Text] [PDF] W. Huang, H. D. Ochs, B. Dupont, and Y. M. Vyas The Wiskott-Aldrich Syndrome Protein Regulates Nuclear Translocation of NFAT2 and NF-{kappa}B (RelA) Independently of Its Role in Filamentous Actin Polymerization and Actin Cytoskeletal Rearrangement J. Immunol., March 1, 2005; 174(5): 2602 - 2611. [Abstract] [Full Text] [PDF] L. Westerberg, M. Larsson, S. J. Hardy, C. Fernandez, A. J. Thrasher, and E. Severinson Wiskott-Aldrich syndrome protein deficiency leads to reduced B-cell adhesion, migration, and homing, and a delayed humoral immune response Blood, February 1, 2005; 105(3): 1144 - 1152. [Abstract] [Full Text] [PDF]

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