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The Journal of Immunology, Vol 156, Issue 4 1609-1615, Copyright © 1996 by American Association of Immunologists
ARTICLES |
HG Wisniewski, JC Hua, DM Poppers, D Naime, J Vilcek and BN Cronstein
Department of Microbiology, Kaplan Cancer Center, New York University Medical Center, NY 10016, USA.
TNF-stimulated gene 6 (tsg6), encoding a 35-kDa secretory glycoprotein (TSG-6), is induced in fibroblasts, chondrocytes, synovial cells, and mononuclear cells by the proinflammatory cytokines TNF-alpha and IL-1, or by LPS. Large amounts of TSG-6 protein were found in synovial fluids of patients with rheumatoid arthritis. TSG-6 protein forms a stable complex with components of the serine protease inhibitor, inter-alpha- inhibitor (I alpha I). In this work, we show that TSG-6 potentiates the inhibitory effect of l alpha l on the protease activity of plasmin. The plasmin/plasminogen activator system is important in the protease network associated with inflammation. To test the hypothesis that through their cooperative inhibitory effect on plasmin TSG-6 and l alpha l can modulate the protease network and thus inhibit inflammation, we examined the effect of TSG-6 on experimentally induced inflammation. Human recombinant TSG-6 protein showed a potent anti- inflammatory activity in the murine air pouch model of carrageenan- or IL-1-induced acute inflammation. The inhibitory effect of locally administered TSG-6 on the IL-1-induced cellular infiltration was comparable with that of systemic dexamethasone treatment. Two mutant TSG-6 proteins with single amino acid substitutions close to the N terminus showed a complete or partial loss of anti-inflammatory activity. The anti-inflammatory effect of the TNF/IL-1-inducible TSG-6 protein, along with its ability to inhibit protease action through interaction with l alpha l, suggests that TSG-6 production during inflammation is part of a negative feedback loop operating through the protease network.
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S. Yoshioka, S. Ochsner, D. L. Russell, T. Ujioka, S. Fujii, J. S. Richards, and L. L. Espey Expression of Tumor Necrosis Factor-Stimulated Gene-6 in the Rat Ovary in Response to an Ovulatory Dose of Gonadotropin Endocrinology, November 1, 2000; 141(11): 4114 - 4119. [Abstract] [Full Text] [PDF]
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E. Tsifrina, N. M. Ananyeva, G. Hastings, and G. Liau Identification and Characterization of Three cDNAs That Encode Putative Novel Hyaluronan-Binding Proteins, Including an Endothelial Cell-Specific Hyaluronan Receptor Am. J. Pathol., November 1, 1999; 155(5): 1625 - 1633. [Abstract] [Full Text] [PDF]
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M. Thuveson and E. Fries Intracellular Proteolytic Processing of the Heavy Chain of Rat Pre-alpha -inhibitor. THE COOH-TERMINAL PROPEPTIDE IS REQUIRED FOR COUPLING TO BIKUNIN J. Biol. Chem., March 5, 1999; 274(10): 6741 - 6746. [Abstract] [Full Text] [PDF]
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A. M. Blom, M. Morgelin, M. Oyen, J. Jarvet, and E. Fries Structural Characterization of Inter-alpha -inhibitor. EVIDENCE FOR AN EXTENDED SHAPE J. Biol. Chem., January 1, 1999; 274(1): 298 - 304. [Abstract] [Full Text] [PDF]
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 M Jourdain, O Carrette, A Tournoys, F Fourrier, C Mizon, J Mangalaboyi, J Goudemand, J Mizon, and C Chopin Effects of inter-alpha-inhibitor in experimental endotoxic shock and disseminated intravascular coagulation Am. J. Respir. Crit. Care Med., December 1, 1997; 156(6): 1825 - 1833. [Abstract] [Full Text]
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 L. Ye, R. Mora, N. Akhayani, C. C. Haudenschild, and G. Liau Growth Factor and Cytokine-Regulated Hyaluronan-Binding Protein TSG-6 Is Localized to the Injury-Induced Rat Neointima and Confers Enhanced Growth in Vascular Smooth Muscle Cells Circ. Res., September 19, 1997; 81(3): 289 - 296. [Abstract] [Full Text]
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D. J. Mahoney, C. D. Blundell, and A. J. Day Mapping the Hyaluronan-binding Site on the Link Module from Human Tumor Necrosis Factor-stimulated Gene-6 by Site-directed Mutagenesis J. Biol. Chem., June 15, 2001; 276(25): 22764 - 22771. [Abstract] [Full Text] [PDF]
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