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Prepublished online as a Blood First Edition Paper on November 27, 2002; DOI 10.1182/blood-2002-05-1300. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-05-1300v1 101/7/2652    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 Fiuza, C. Articles by Suffredini, A. F. Search for Related Content PubMed PubMed Citation Articles by Fiuza, C. Articles by Suffredini, A. F. Related Collections Hemostasis, Thrombosis, and Vascular Biology Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 1 April 2003, Vol. 101, No. 7, pp. 2652-2660 HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Inflammation-promoting activity of HMGB1 on human microvascular endothelial cells Carmen Fiuza, Michael Bustin, Shefali Talwar, Margaret Tropea, Eric Gerstenberger, James H. Shelhamer, and Anthony F. Suffredini From the Critical Care Medicine Department, Warren G. Magnuson Clinical Center, National Institutes of Health, Bethesda; and Laboratory of Molecular Carcinogenesis, Division of Basic Sciences, National Cancer Institute, Bethesda, MD. Systemic inflammation because of sepsis results in endothelial cell activation and microvascular injury. High-mobility group protein-1 (HMGB1), a novel inflammatory molecule, is a late mediator of endotoxin shock and is present in the blood of septic patients. The receptor for advanced glycation end products (RAGE) is expressed on endothelium and is a receptor for HMGB1. Here we examine the effects of HMGB1 on human endothelial cell function. Recombinant human HMGB1 (rhHMGB1) was cloned and expressed in Escherichia coli and incubated with human microvascular endothelium. rhHMGB1 caused a dose- and time-dependent increase in the expression of intercellular adhesion molecule 1 (ICAM-1), vascular cell adhesion molecule 1 (VCAM-1), and RAGE. rhHMGB1 induced the secretion of tumor necrosis factor- (TNF), interleukin 8 (IL-8), monocyte chemotactic protein-1 (MCP-1), plasminogen activator inhibitor 1 (PAI-1), and tissue plasminogen activator (tPA) (P < .01). rhHMGB1 stimulation resulted in transient phosphorylation of mitogen-activated protein (MAP) kinases, extracellular signal-related kinase (ERK), Jun N-terminal kinase (JNK), and p38, and in nuclear translocation of transcription factors NF-B and Sp1. These effects are partially mediated by TNF autocrine stimulation, as anti-TNF antibodies significantly decrease chemokine and adhesion molecule responses (P  .002). Thus, rhHMGB1 elicits proinflammatory responses on endothelial cells and may contribute to alterations in endothelial cell function in human inflammation. © 2003 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: D. Tang, R. Kang, W. Xiao, H. Zhang, M. T. Lotze, H. Wang, and X. Xiao Quercetin Prevents LPS-Induced High-Mobility Group Box 1 Release and Proinflammatory Function Am. J. Respir. Cell Mol. Biol., December 1, 2009; 41(6): 651 - 660. [Abstract] [Full Text] [PDF] H. S. Hreggvidsdottir, T. Ostberg, H. Wahamaa, H. Schierbeck, A.-C. Aveberger, L. Klevenvall, K. Palmblad, L. Ottosson, U. Andersson, and H. E. 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