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Blood, 15 August 2004, Vol. 104, No. 4, pp. 1174-1182.
Prepublished online as a Blood First Edition Paper on May 6, 2004; DOI 10.1182/blood-2003-10-3536.
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PHAGOCYTES
Regulation of monocyte migration by amphoterin (HMGB1)
Ari Rouhiainen,
Juha Kuja-Panula,
Erika Wilkman,
Jukka Pakkanen,
Jan Stenfors,
Raimo K. Tuominen,
Mauri Lepäntalo,
Olli Carpén,
Jaakko Parkkinen, and
Heikki Rauvala
From the Finnish Red Cross Blood Transfusion Service, Helsinki, Finland; the Neuroscience Center, Laboratory of Molecular Neurobiology, Institute of Biotechnology and Department of Biosciences, University of Helsinki, Helsinki, Finland; the Department of Medical Chemistry, University of Helsinki, Helsinki, Finland; the Division of Pharmacology and Toxicology, Department of Pharmacy, University of Helsinki, Helsinki, Finland; the Department of Vascular Surgery, Helsinki University Central Hospital, University of Helsinki, Helsinki, Finland; and the Department of Pathology, Haartman Institute, University of Helsinki, Helsinki, Finland.
Amphoterin (HMGB1) is a 30-kD heparin-binding protein involved in process extension and migration of cells by a mechanism involving the receptor for advanced glycation end products (RAGE). High levels of amphoterin are released to serum during septic shock. We have studied the expression of amphoterin in monocytes and the role of amphoterin and RAGE in monocyte transendothelial migration. Un-activated monocytes in suspension did not reveal amphoterin on their surface, but adherent monocytes exported amphoterin to the cell surface. Immunohistochemical staining of arterial thrombi in vivo revealed amphoterin in mononuclear cells and in surrounding extracellular matrix. Amphoterin was secreted from phorbol ester and interferon- (IFN-)-activated macrophages, and the secretion was inhibited by blocking the adenosine 5'-triphosphate (ATP)-binding cassette transporter-1, a member of the multidrug resistance protein family. Amphoterin was specifically adhesive for monocytes in peripheral blood leukocyte adhesion assay. Adhesion caused an extensive spreading of cells, which was inhibited by the dominant-negative RAGE receptor (soluble ectodomain of RAGE), and adhesion up-regulated chromogranin expression in monocytes, also suggesting a RAGE-dependent interaction. Monocyte transendothelial migration was efficiently inhibited by anti-amphoterin and anti-RAGE antibodies and by the soluble RAGE. We suggest that amphoterin is an autocrine/paracrine regulator of monocyte invasion through the endothelium. (Blood. 2004;104:1174-1182)
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