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Cysteine Cathepsins and Antibacterial Activity by Human Regulation Of Regulation of Chemerin Chemoattractant and Antibacterial Activity by Human Cysteine Cathepsins This information is current as Paulina Kulig, Tomasz Kantyka, Brian A. Zabel, Magdalena of September 28, 2021. Banas, Agnieszka Chyra, Anna Stefanska, Hua Tu, Samantha J. Allen, Tracy M. Handel, Andrzej Kozik, Jan Potempa, Eugene C. Butcher and Joanna Cichy J Immunol 2011; 187:1403-1410; Prepublished online 29 June 2011; Downloaded from doi: 10.4049/jimmunol.1002352 http://www.jimmunol.org/content/187/3/1403 References This article cites 31 articles, 16 of which you can access for free at: http://www.jimmunol.org/ http://www.jimmunol.org/content/187/3/1403.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists by guest on September 28, 2021 • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2011 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Regulation of Chemerin Chemoattractant and Antibacterial Activity by Human Cysteine Cathepsins Paulina Kulig,*,1 Tomasz Kantyka,†,1 Brian A. Zabel,‡,1 Magdalena Banas´,* Agnieszka Chyra,* Anna Stefan´ska,* Hua Tu,x Samantha J. Allen,{ Tracy M. Handel,{ Andrzej Kozik,‖ Jan Potempa,†,# Eugene C. Butcher,‡,** and Joanna Cichy* Chemerin, a ligand for the G-protein coupled receptor chemokine-like receptor 1, requires C-terminal proteolytic processing to unleash its chemoattractant activity. Proteolytically processed chemerin selectively attracts specific subsets of immunoregulatory APCs, including chemokine-like receptor 1-positive immature plasmacytoid dendritic cells (pDC). Chemerin is predicted to belong to the structural cathelicidin/cystatin family of proteins composed of antibacterial polypeptide cathelicidins and inhibitors of cys- teine proteinases (cystatins). We therefore hypothesized that chemerin may interact directly with cysteine proteases, and that it might also function as an antibacterial agent. In this article, we show that chemerin does not inhibit human cysteine proteases, but Downloaded from rather is a new substrate for cathepsin (cat) K and L. cat K- and L-cleaved chemerin triggered robust migration of human blood- derived pDC ex vivo. Furthermore, cat K- and L-truncated chemerin also displayed antibacterial activity against Enterobacter- iaceae. Cathepsins may therefore contribute to host defense by activating chemerin to directly inhibit bacterial growth and to recruit pDC to sites of infection. The Journal of Immunology, 2011, 187: 1403–1410. http://www.jimmunol.org/ hemerin is a recently characterized chemoattractant pro- tease-mediated, C-terminal truncation to acquire chemotactic tein that serves as a ligand for the seven-pass G-protein activity. Truncated, bioactive chemerin lacking 6 (chemS157), 8 C coupled receptor chemokine-like receptor 1 (CMKLR1) (chemA155), or 9 (chemF154) amino acids in the C terminus have (1, 2). Two additional heptahelical receptors, GPR1 and CCRL2, been isolated from several biofluids, including ascites, serum, and have been reported to bind chemerin, although they do not appear hemofiltrate, respectively (reviewed in Ref. 5). Serine proteases of to directly support chemotaxis (3, 4). Chemerin circulates as an the coagulation, fibrinolytic, and inflammatory cascades, includ- inactive precursor (prochemerin) in blood and undergoes pro- ing neutrophil elastase and cathepsin (cat) G, generate bioactive chemerin (6, 7). In addition, chemerin can be activated in a se- quential manner by plasma carboxypeptidases after initial cleav- by guest on September 28, 2021 *Department of Immunology, Faculty of Biochemistry, Biophysics and Biotechnol- age by plasmin (8). ogy, Jagiellonian University, 30-387 Krakow, Poland; †Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, 30- Cells that are critical in linking the innate and adaptive immune 387 Krakow, Poland; ‡Veterans Affairs Palo Alto Health Care System, Palo Alto, CA responses, such as plasmacytoid dendritic cells (pDC), NK cells, and 94304; xLakePharma, Inc., Belmont, CA 94002; {Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, La Jolla, CA 92093; macrophages, express CMKLR1 and respond to chemerin through ‖Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and chemotaxis (1, 2, 9–12). Although the structure of chemerin has # Biotechnology, Jagiellonian University, 30-387 Krakow, Poland; Center for Oral not yet been solved, the predicted structural homology between Health and Systemic Diseases, University of Louisville School of Dentistry, Louis- ville, KY 40202; and **Stanford University Medical School, Stanford, CA 94305 chemerin and inhibitors of cysteine proteinases (cystatins) and 1P.K., T.K., and B.A.Z. contributed equally to this work. antimicrobial cathelicidins (1, 5) suggests that chemerin may in- hibit endogenous human cysteine proteases and possibly exhibit Received for publication July 13, 2010. Accepted for publication May 29, 2011. antibacterial activity. Alternatively, host cysteine proteases may This work was supported by the Ministry of Scientific Research, Poland (Grants SPUB3088 and 0724/B/P01/2011/40 to J.C.), a Fogarty International Research Col- bind and proteolytically process chemerin. In support of the latter, laborative award (R03TW007174-01 to E.C.B. and J.C.), a grant from the European we recently reported that the cysteine protease staphopain B Union 6th FP project (SP6MTKD-CT-2006-042586 to J.C.), a Team award from the (SspB) secreted by the human pathogen Staphylococcus aureus Foundation for Polish Science (TEAM/2010-5/1 to J.C.), and the National Institutes of Health (Grant AI079320 to B.A.Z. and National Institutes of Health grants to E.C.B.). selectively cleaves and activates chemerin (13). T.H. is supported by National Institutes of Health Grant R01-AI37113. J.P. is sup- The papain-like cysteine proteases, including cat B, cat L, and ported by the European Community Gums & Joints project (7FP-HEALTH-2010- 261460), the Ministry of Scientific Research, Poland (Warsaw, Poland; Grant 1642/B/ cat K are well-known degradative enzymes of mammalian cells, P01/2008/35), and the Foundation for Polish Science (TEAM Project DPS/424-329/ participating primarily in intracellular proteolytic pathways (such 10). The Faculty of Biochemistry, Biophysics and Biotechnology of Jagiellonian as Ag processing and presentation), but also extracellular protein University is a beneficiary of structural funds from the European Union (Grant POIG.02.01.00-12-064/08). turnover. Recent studies show that lysosomal cathepsins can exert Address correspondence and reprint requests to Dr. Joanna Cichy, Faculty of Bio- their proteolytic activity at extracellular sites (14, 15), where they chemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7 contribute to a variety of pathophysiological processes, including Street, 30-387 Krakow, Poland. E-mail address: [email protected] chronic inflammation associated with obesity (16–18). Abbreviations used in this article: cat, cathepsin; chem, chemerin truncated at in- Cathelicidins consist of two distinct domains: a highly con- dicated residue position; chemS, chemerin serum form; chem/SspB, staphopain B- truncated chemerin; CID, collision-induced dissociation; CMKLR1, chemokine-like served N-terminal cathelin-like domain with homology to the cyst- receptor 1; hCAP18, human cationic antimicrobial peptide of 18 kDa; MHB, Muel- atins and a divergent C-terminal antimicrobial region that varies ler–Hinton broth; MS, matrix-assisted laser desorption ionization time-of-flight mass among species. Only one cathelicidin has been described in hu- spectrometry; pDC, plasmacytoid dendritic cell; SspB, staphopain B. mans: human cationic antimicrobial peptide of 18 kDa (hCAP18). Copyright Ó 2011 by The American Association of Immunologists, Inc. 0022-1767/11/$16.00 hCAP18 is cleaved by neutrophil serine proteases such as pro- www.jimmunol.org/cgi/doi/10.4049/jimmunol.1002352 1404 CHEMERIN ACTIVATION BY HOST CYSTEINE CATHEPSINS teinase 3 to generate a 37-aa antimicrobial peptide LL-37 and a harvested after LSM1077 (PAA Laboratories) gradient separation, as de- 103-aa cathelin-like domain (19, 20). scribed by the manufacturer. pDC were enriched from PBMC using negative In this study, we found that although chemerin does not inhibit selection with biotinylated mAbs directed against CD3, CD14, CD16, CD19, CD20, CD56, and anti-biotin MACS Microbeads (Miltenyi Biotec), the proteolytic activities of cat L or K, these cysteine proteases are according to the manufacturer’s recommendations. Cells were blocked potent activators of chemerin. cat L and K initially and efficiently with 50–80% autologous plasma and then stained for flow cytometry cleave prochemerin to release a 6-aa peptide from the carboxyl analysis using
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