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J. Biol. Chem., Vol. 280, Issue 41, 34661-34666, October 14, 2005

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Chemerin Activation by Serine Proteases of the Coagulation, Fibrinolytic, and Inflammatory Cascades^*

Brian A. Zabel, Supported by National Institutes of Health Training Grant 5 T32 AI07290-151, Samantha J. Allen¶2, Paulina Kulig||, Jessica A. Allen, Joanna Cichy||3, Tracy M. Handel¶4, and Eugene C. Butcher

From the Laboratory of Immunology and Vascular Biology, Department of Pathology, Stanford University School of Medicine, Stanford, California 94305, Center for Molecular Biology and Medicine, Veterans Affairs Palo Alto Health Care System, Palo Alto, California 94304, ^¶Molecular and Cell Biology, University of California, Berkeley, California 94720, and ^||Faculty of Biotechnology, Jagiellonian University, Krakow 30-387, Poland

Proteases function at every level in host defense, from regulating vascular hemostasis and inflammation to mobilizing the "rapid responder" leukocytes of the immune system by regulating the activities of various chemoattractants. Recent studies implicate proteolysis in the activation of a ubiquitous plasma chemoattractant, chemerin, a ligand for the G-protein-coupled receptor CMKLR1 present on plasmacytoid dendritic cells and macrophages. To define the pathophysiologic triggers of chemerin activity, we evaluated the ability of serum- and inflammation-associated proteases to cleave chemerin and stimulate CMKLR1-mediated chemotaxis. We showed that serine proteases factor XIIa and plasmin of the coagulation and fibrinolytic cascades, elastase and cathepsin G released from activated neutrophil granules and mast cell tryptase are all potent activators of chemerin. Activation results from cleavage of the labile carboxyl terminus of the chemoattractant at any of several different sites. Activation of chemerin by the serine protease cascades that trigger rapid defenses in the body may direct CMKLR1-positive plasmacytoid dendritic cell and tissue macrophage recruitment to sterile sites of tissue damage, as well as trafficking to sites of infectious and allergic inflammation.

Received for publication, May 3, 2005 , and in revised form, June 22, 2005.

^* This work was supported by National Institutes of Health Grants AI-59635, AI-37832, AI-47822, and GM-37734, Specialized Center of Research Grant HL-67674, Digestive Disease Center Grant DK56339, and a Merit Award from the Veterans Administration (to E. C. B.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

² Supported by a postdoctoral fellowship from the Cancer Research Institute, New York. Present address: Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, La Jolla, CA 92093

³ Supported by Jagiellonian University grants and a Fulbright fellowship.

⁴ Supported by grants from the National Institutes of Health (AI37113-09), the University of California Discovery Program (Bio03-10367), and the University of California AIDS Program (1D03-B-005). Present address: Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, La Jolla, CA 92093.

¹ To whom correspondence should be addressed: Dept. of Pathology (5234), Stanford University Medical Ctr., Stanford, CA 94305. Tel.: 650-493-5000 (ext. 63132); Fax: 650-858-3986; E-mail: bazabel{at}alum.mit.edu.

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