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Blood, 1 September 2008, Vol. 112, No. 5, pp. 2035-2045. Prepublished online as a Blood First Edition Paper on June 11, 2008; DOI 10.1182/blood-2008-04-149468. This Article Full Text (PDF) All Versions of this Article: blood-2008-04-149468v1 112/5/2035    most recent Alert me when this article is cited Alert me if a correction is posted 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 Miner, J. J. Articles by McEver, R. P. Search for Related Content PubMed PubMed Citation Articles by Miner, J. J. Articles by McEver, R. P. Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted April 1, 2008 Accepted May 27, 2008 Separable requirements for cytoplasmic domain of PSGL-1 in leukocyte rolling and signaling under flow Jonathan J. Miner, Lijun Xia, Tadayuki Yago, Janos Kappelmayer, Zhenghui Liu, Arkadiusz G. Klopocki, Bojing Shao, J. Michael McDaniel, Hendra Setiadi, David W. Schmidtke, and Rodger P. McEver* Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104, United States Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, United States Department of Clinical Biochemistry and Molecular Pathology, University of Debrecen, Debrecen, Hungary School of Chemical, Biological and Materials Engineering, University of Oklahoma, Norman, OK 73109, United States * Corresponding author; email: rodger-mcever{at}omrf.org. In inflamed venules, leukocytes use P-selectin glycoprotein ligand-1 (PSGL-1) to roll on P-selectin and E-selectin and to activate integrin L2 (lymphocyte function-associated antigen-1, LFA-1) to slow rolling on intercellular adhesion molecule-1 (ICAM-1). Studies in cell lines have suggested that PSGL-1 requires its cytoplasmic domain to localize in membrane domains, to support rolling on P-selectin, and to signal through spleen tyrosine kinase (Syk). We generated "CD" mice that express PSGL-1 without the cytoplasmic domain. Unexpectedly, neutrophils from these mice localized PSGL-1 normally in microvilli, uropods, and lipid rafts. CD neutrophils expressed less PSGL-1 on their surfaces because of inefficient export from the endoplasmic reticulum. Limited digestion of wild-type neutrophils with O-sialoglycoprotein endopeptidase was used to reduce the PSGL-1 density to that on CD neutrophils. At matched PSGL-1 densities, both CD and wild-type neutrophils rolled similarly on P-selectin. However, CD neutrophils rolling on P-selectin did not trigger Syk-dependent activation of LFA-1 to slow rolling on ICAM-1. These data demonstrate that the PSGL-1 cytoplasmic domain is dispensable for leukocyte rolling on P-selectin but is essential to activate 2 integrins to slow rolling on ICAM-1. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: A. Zarbock, H. Muller, Y. Kuwano, and K. Ley PSGL-1-dependent myeloid leukocyte activation J. Leukoc. Biol., November 1, 2009; 86(5): 1119 - 1124. [Abstract] [Full Text] [PDF] H. Oh, E. R. Mohler III, A. Tian, T. Baumgart, and S. L. Diamond Membrane Cholesterol Is a Biomechanical Regulator of Neutrophil Adhesion Arterioscler Thromb Vasc Biol, September 1, 2009; 29(9): 1290 - 1297. [Abstract] [Full Text] [PDF] B. Sarraj, S. Massberg, Y. Li, A. Kasorn, K. Subramanian, F. Loison, L. E. Silberstein, U. von Andrian, and H. R. Luo Myeloid-Specific Deletion of Tumor Suppressor PTEN Augments Neutrophil Transendothelial Migration during Inflammation J. Immunol., June 1, 2009; 182(11): 7190 - 7200. [Abstract] [Full Text] [PDF]

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