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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 (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 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 Social Bookmarking                   What's this? Submitted May 2, 2002 Accepted November 15, 2002 Inflammatory 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* Critical Care Medicine Department, Warren G Magnuson Clinical Center, National Institutes of Health, Bethesda, MD, USA Laboratory of Molecular Carcinogenesis, Division of Basic Sciences, National Cancer Institute, Bethesda, MD, USA * Corresponding author; email: asuffredini{at}nih.gov. Systemic inflammation due to 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 E.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 (IL) 8, monocyte chemotactic protein-1 (MCP-1), plasminogen activator inhibitor 1 (PAI-1) and tissue plasminogen activator (tPA) (p < 0.01). rhHMGB1 stimulation resulted in transient phosphorylation of MAP kinases ERK, JNK and p38, and nuclear translocation of transcription factors NF-B and SP-1. These effects are partially mediated by TNF autocrine stimulation, as anti-TNF antibodies significantly decrease chemokine and adhesion molecule responses (p 0.002). Thus, rhHMGB1 elicits pro-inflammatory responses on endothelial cells and may contribute to alterations in endothelial cell function in human inflammation. 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