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Blood, 28 May 2009, Vol. 113, No. 22, pp. 5588-5598. Prepublished online as a Blood First Edition Paper on January 30, 2009; DOI 10.1182/blood-2008-08-170837. This Article Full Text (PDF) Supplemental Figures All Versions of this Article: blood-2008-08-170837v1 113/22/5588    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 Wygrecka, M. Articles by Preissner, K. T. Search for Related Content PubMed PubMed Citation Articles by Wygrecka, M. Articles by Preissner, K. T. Related Collections Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted August 11, 2008 Accepted January 17, 2009 Enolase-1 promotes plasminogen-mediated recruitment of monocytes to the acutely inflamed lung Malgorzata Wygrecka*, Leigh M. Marsh, Rory E. Morty, Ingrid Henneke, Andreas Guenther, Juergen Lohmeyer, Philipp Markart, and Klaus T. Preissner Department of Biochemistry, University of Giessen Lung Center, Giessen, Germany Department of Internal Medicine, University of Giessen Lung Center, Giessen, Germany * Corresponding author; email: malgorzata.wygrecka{at}innere.med.uni-giessen.de. Cell surface-associated proteolysis plays a crucial role in the migration of mononuclear phagocytes to sites of inflammation. The glycolytic enzyme enolase-1 (ENO-1) binds plasminogen at the cell-surface, enhancing local plasmin production. This study addressed the role played by ENO-1 in lipopolysaccharide (LPS)-driven chemokine-directed monocyte migration and matrix invasion in vitro, as well as recruitment of monocytes to the alveolar compartment in vivo. LPS rapidly upregulated ENO-1 cell-surface expression on human blood monocytes and U937 cells due to protein translocation from cytosolic pools, which increased plasmin generation, enhanced monocyte migration through epithelial monolayers, and promoted matrix degradation. These effects were abrogated by antibodies directed against the plasminogen-binding site of ENO-1. Overexpression of ENO-1 in U937 cells increased their migratory and matrix-penetrating capacity, which was suppressed by overexpression of a truncated ENO-1 variant lacking the plasminogen binding site (ENO-1PLG). In vivo, intratracheal LPS application in mice promoted alveolar recruitment of monocytic cells which overexpressed ENO-1, but not of cells overexpressing ENO-1PLG. Consistent with these data, pneumonia-patients exhibited increased ENO-1 cell-surface expression on blood monocytes and intense ENO-1 staining of mononuclear cells in the alveolar space. These data suggest an important mechanism of inflammatory cell invasion mediated by increased cell-surface expression of ENO-1. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: Enolase-1 as a plasminogen receptor Edward F. Plow and Riku Das Blood 2009 113: 5371-5372. [Full Text] [PDF] This article has been cited by other articles: R. Das, T. Burke, D. R. Van Wagoner, and E. F. Plow L-Type Calcium Channel Blockers Exert an Antiinflammatory Effect by Suppressing Expression of Plasminogen Receptors on Macrophages Circ. Res., July 17, 2009; 105(2): 167 - 175. [Abstract] [Full Text] [PDF] E. F. Plow and R. Das Enolase-1 as a plasminogen receptor Blood, May 28, 2009; 113(22): 5371 - 5372. [Full Text] [PDF]

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