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Blood, 15 November 2007, Vol. 110, No. 10, pp. 3763-3772. Prepublished online as a Blood First Edition Paper on August 9, 2007; DOI 10.1182/blood-2007-03-079392. This Article Full Text (PDF) Supplemental Methods and Figures All Versions of this Article: blood-2007-03-079392v1 110/10/3763    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 Das, R. Articles by Plow, E. F Search for Related Content PubMed PubMed Citation Articles by Das, R. Articles by Plow, E. F Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted March 20, 2007 Accepted August 2, 2007 Histone H2B as a functionally important plasminogen receptor on macrophages Riku Das, Tim Burke, and Edward F Plow* Department of Molecular Cardiology, Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Cleveland Clinic, Cleveland, OH, United States * Corresponding author; email: plowe{at}ccf.org. Plasminogen (Plg) facilitates inflammatory cell recruitment, a function which depends upon its binding to Plg receptors (Plg-Rs). However, the Plg-Rs that are critical for cell migration are not well defined. Three previously characterized Plg-Rs, -enolase, annexin II and p11, and a recently identified Plg-R, histone H2B (H2B), were assessed for their contribution to Plg binding and function on macrophages. Two murine macrophage cell lines (RAW 264.7 and J774A.1) and mouse peritoneal macrophages induced by thioglycollate were analyzed. All four Plg-Rs were present on the surface of these cells and showed enhanced expression on the thioglycollate induced macrophages compared to peripheral blood monocytes. Using blocking Fab fragments to each Plg-R, H2B supported ~50% of the Plg binding capacity, whereas the other Plg-Rs contributed less than 25%. Anti-H2B Fab also demonstrated a major role of this Plg-R in plasmin generation and matrix invasion. Furthermore, when mice were treated intravenously with anti-H2B Fab, peritoneal macrophage recruitment in response to thioglycollate was reduced by ~45% at 24, 48 and 72 hours, with no effect on blood monocyte levels. Taken together, these data suggest that multiple Plg-Rs do contribute to Plg binding to macrophages, and among these, H2B plays a very prominent and functionally important role. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? 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] M. Wygrecka, L. M. Marsh, R. E. Morty, I. Henneke, A. Guenther, J. Lohmeyer, P. Markart, and K. T. Preissner Enolase-1 promotes plasminogen-mediated recruitment of monocytes to the acutely inflamed lung Blood, May 28, 2009; 113(22): 5588 - 5598. [Abstract] [Full Text] [PDF]

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