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Blood, 15 July 2004, Vol. 104, No. 2, pp. 409-414. Prepublished online as a Blood First Edition Paper on March 23, 2004; DOI 10.1182/blood-2004-01-0126. This Article Full Text (PDF) All Versions of this Article: 2004-01-0126v1 104/2/409    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 Sahni, A. Articles by Francis, C. W Search for Related Content PubMed PubMed Citation Articles by Sahni, A. Articles by Francis, C. W Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted January 12, 2004 Accepted March 10, 2004 Interleukin-1 but not IL-1 binds to fibrinogen and fibrin and has enhanced activity in the bound form Abha Sahni*, Min Guo, Sanjeev K Sahni, and Charles W Francis Department of Medicine/Hematology/Oncology Unit, University of Rochester School of Medicine and Dentistry, Rochester, NY, USA * Corresponding author; email: Abha_Sahni{at}urmc.rochester.edu. Fibrin is formed at sites of injury or inflammation and provides the temporary matrix to support vascular cell responses that are also mediated by cytokines including interleukin-1. We have shown previously that FGF-2 binds with high affinity to fibrin(ogen). Because IL-1 has a structure similar to FGF-2, we have investigated the possible binding of IL-1 to fibrin(ogen). Experiments using IL-1 immobilized on Sepharose beads and soluble 125I-labeled fibrinogen demonstrated no specific interaction of IL-1 with fibrinogen, but IL-1showed saturable and specific binding. Scatchard analysis indicated a single binding site with an apparent Kd = 1.5nM and maximum molar binding ratio of IL-1 to fibrinogen of 1.8 to 1. Binding of 125I IL-1 to Sepharose-immobilized fibrinogen also demonstrated a single binding site with an apparent Kd of 3.5nM. IL-1 also bound specifically to fibrin monomer and polymerized fibrin with apparent Kds of 3.4 nM and 2.3 nM, respectively. IL-1 displaced FGF-2 for binding to fibrin, indicating an interaction with the same or a closely related site. Compared with free form, fibrinogen-bound IL-1 stimulated increased activation of endothelial cell NF-B, MCP-1 secretion and NO synthesis. We conclude that IL-1 binds with high affinity to fibrin(ogen) and demonstrates increased activity in bound form. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: C. Karlsson, M. Morgelin, M. Collin, R. Lood, M.-L. Andersson, A. Schmidtchen, L. Bjorck, and I.-M. Frick SufA - a bacterial enzyme that cleaves fibrinogen and blocks fibrin network formation Microbiology, January 1, 2009; 155(1): 238 - 248. [Abstract] [Full Text] [PDF] T. Hou, S. Ray, and A. R. Brasier The Functional Role of an Interleukin 6-inducible CDK9{middle dot}STAT3 Complex in Human {gamma}-Fibrinogen Gene Expression J. Biol. Chem., December 21, 2007; 282(51): 37091 - 37102. [Abstract] [Full Text] [PDF] A. Sahni, A. A. Khorana, R. B. Baggs, H. Peng, and C. W. Francis FGF-2 binding to fibrin(ogen) is required for augmented angiogenesis Blood, January 1, 2006; 107(1): 126 - 131. [Abstract] [Full Text] [PDF] A. Sahni, S. K. Sahni, and C. W. Francis Endothelial Cell Activation by IL-1{beta} in the Presence of Fibrinogen Requires {alpha}V{beta}3 Arterioscler Thromb Vasc Biol, October 1, 2005; 25(10): 2222 - 2227. [Abstract] [Full Text] [PDF]

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