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Blood, 15 December 2004, Vol. 104, No. 13, pp. 4260-4268. Prepublished online as a Blood First Edition Paper on August 26, 2004; DOI 10.1182/blood-2004-02-0446. This Article Full Text Full Text (PDF) All Versions of this Article: 2004-02-0446v1 104/13/4260    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 Vogl, T. Articles by Roth, J. Search for Related Content PubMed PubMed Citation Articles by Vogl, T. Articles by Roth, J. Related Collections Phagocytes Cell Adhesion and Motility Cytoskeleton Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  PHAGOCYTES MRP8 and MRP14 control microtubule reorganization during transendothelial migration of phagocytes Thomas Vogl, Stephan Ludwig, Matthias Goebeler, Anke Strey, Irmgard S. Thorey, Rudolf Reichelt, Dirk Foell, Volker Gerke, Marie P. Manitz, Wolfgang Nacken, Sabine Werner, Clemens Sorg, and Johannes Roth From the Institute of Experimental Dermatology, Department of Pediatrics, and Institute of Molecular Virology, University of Münster, Germany; Department of Dermatology, University of Würzburg, Germany; Institute of Medical Biochemistry, University of Münster, Germany; Institute of Cell Biology, ETH Zürich, Switzerland; and Institute of Medical Physics and Biophysics, University of Münster, Germany. MRP14 (S100A9) is the major calcium-binding protein of neutrophils and monocytes. Targeted gene disruption reveals an essential role of this S100 protein for transendothelial migration of phagocytes. The underlying molecular mechanism comprises major alterations of cytoskeletal metabolism. MRP14, in complex with its binding partner MRP8 (S100A8), promotes polymerization of microtubules. MRP14 is specifically phosphorylated by p38 mitogen-activated protein kinase (MAPK). This phosphorylation inhibits MRP8/MRP14-induced tubulin polymerization. Phosphorylation of MRP14 is antagonistically regulated by binding of MRP8 and calcium. The biologic relevance of these findings is confirmed by the fact that MAPK p38 fails to stimulate migration of MRP14-/- granulocytes in vitro and MRP14-/- mice show a diminished recruitment of granulocytes into the granulation tissue during wound healing in vivo. MRP14-/- granulocytes contain significantly less polymerized tubulin, which subsequently results in minor activation of Rac1 and Cdc42 after stimulation of p38 MAPK. Thus, the complex of MRP8/MRP14 is the first characterized molecular target integrating MAPK- and calcium-dependent signals during migration of phagocytes. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: H. B. Hammer, S. Odegard, M. K Fagerhol, R. Landewe, D. v. d. Heijde, T. Uhlig, P. Mowinckel, and T. K Kvien Calprotectin (a major leucocyte protein) is strongly and independently correlated with joint inflammation and damage in rheumatoid arthritis Ann Rheum Dis, August 1, 2007; 66(8): 1093 - 1097. [Abstract] [Full Text] [PDF] G. L. Warren, M. Summan, X. Gao, R. Chapman, T. Hulderman, and P. P. Simeonova Mechanisms of skeletal muscle injury and repair revealed by gene expression studies in mouse models J. Physiol., July 15, 2007; 582(2): 825 - 841. [Abstract] [Full Text] [PDF] D. Stygar, B. Masironi, H. Eriksson, and L. 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