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3 and MBL/Ficolin/CL-11 Associated Serine Heterocomplex Formation between MBL/Ficolin/CL-11−Associated Serine Protease-1 and -3 and MBL/Ficolin/CL-11− Associated Protein-1 This information is current as of October 1, 2021. Anne Rosbjerg, Lea Munthe-Fog, Peter Garred and Mikkel-Ole Skjoedt J Immunol 2014; 192:4352-4360; Prepublished online 28 March 2014; doi: 10.4049/jimmunol.1303263 Downloaded from http://www.jimmunol.org/content/192/9/4352 References This article cites 39 articles, 22 of which you can access for free at: http://www.jimmunol.org/content/192/9/4352.full#ref-list-1 http://www.jimmunol.org/ 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 October 1, 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 © 2014 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Heterocomplex Formation between MBL/Ficolin/ CL-11–Associated Serine Protease-1 and -3 and MBL/Ficolin/CL-11–Associated Protein-1 Anne Rosbjerg, Lea Munthe-Fog, Peter Garred, and Mikkel-Ole Skjoedt The activity of the complement system is tightly controlled by many fluid-phase and tissue-bound regulators. Mannose-binding lectin (MBL)/ficolin/collectin-11–associated protein-1 (MAP-1) is a recently discovered plasma protein that acts as an upstream inhibitor of the lectin complement pathway (LCP). It has previously been shown that MAP-1 can compete with the MBL/ficolin/ collectin-11–associated serine proteases (MASPs) in binding to MBL and the ficolins. However, this mechanism may only partly explain the inhibitory complement effect of MAP-1. We hypothesized that MAP-1 is also involved in heterocomplex formation with the MASPs thereby breaking the stoichiometry of the activation complexes of the LCP, which could represent an alternative mechanism of MAP-1–mediated complement inhibition. We assessed the heterocomplex formation with ELISA, size-exclusion Downloaded from chromatography, and immunoblotting using both recombinant proteins and serum/plasma. We found that rMAP-1 can engage in heterocomplexes with rMASP-1 and rMASP-3 in a calcium-dependent manner. Moreover, we discovered that rMASP-1 and rMASP-3 also form heterocomplexes under these conditions. Complexes containing both MAP-1 and MASP-1 or -3 were detected innormalhumanserumandplasma,anddepletionoftheLCPrecognition molecules from ficolin-3–deficient human serum showed that free circulating heterocomplexes also exist in the blood, although the major part appears to be associated with the LCP recognition molecules. Altogether, these findings suggest that MASPs can associate in various combinations and bring new http://www.jimmunol.org/ perspectives to the complexity of lectin pathway–driven complement activation. The Journal of Immunology, 2014, 192: 4352–4360. he lectin complement pathway (LCP) is one of three ini- tissue damage following myocardial (3, 4), gastrointestinal (5), tiating pathways in the complement cascade and is a part renal (6, 7), and cerebral (8) I/R. MASP-2 knockout mice also T of the innate immune response. The pattern-recognition demonstrate the influence of LCP in myocardial and gastrointes- molecules (PRMs) from the LCP, mannose-binding lectin (MBL), tinal I/R tissue injuries (9). The protective function of LCP in the the ficolins (ficolin-1, -2, and -3), and collectin (CL)-11 bind to early immune response can thus quickly shift and become a direct by guest on October 1, 2021 microbial surfaces and initiate the cascade through MBL/ficolin/ source of tissue damage during situations of oxidative stress. CL-11–associated serine proteases (MASPs) (1, 2). LCP is there- Hence, novel complement regulators are becoming important in fore important in the defense against intruding microorganisms. the prospect of future medical treatment in situations of excessive Inappropriate activity, in contrast, can create detrimental damages complement activation. through recognition and destruction of self-tissue. It is believed that MBL/ficolin/CL-11–associated protein-1 (MAP-1; also known LCP potentiates tissue damage in various ischemia/reperfusion as MAp44) is a newly discovered transcriptional variant of the (I/R) conditions because oxidative stress allows MBL to bind to MASP1 gene and has shown the ability to inhibit LCP activation vascular endothelium (3). In vivo experiments in rats and mice in vitro (10) and also in vivo, where MAP-1 protects against I/R have shown that MBL is a contributing factor in the generation of injuries and inhibits thrombogenesis in mice (11). MAP-1 does not contain a serine protease domain, as it is terminated in a Laboratory of Molecular Medicine, Department of Clinical Immunology, Faculty of unique amino acid sequence located after the first CCP domain. Health and Medical Sciences, Rigshospitalet, University of Copenhagen, DK 2100 However, MAP-1 comprises the H chain domains that mediate Copenhagen, Denmark both homodimerization and MBL/ficolin binding similar to the Received for publication December 6, 2013. Accepted for publication February 19, other MASPs (12–16). In line with this, we have previously shown 2014. that MAP-1 can outcompete the MASPs for MBL and ficolin-3 This work was supported by The Danish Council for Independent Research in Med- ical Sciences, the Novo Nordisk Foundation, the Svend Andersen Research Founda- binding (11, 14), and in the current study, we questioned the ca- tion, the Capital Region of Denmark, and Rigshospitalet. pability of MAP-1 to heterodimerize with the other MASPs. This Address correspondence and reprint requests to Anne Rosbjerg, Laboratory would shed new light on the mechanism of MAP-1 inhibition, but of Molecular Medicine, Department of Clinical Immunology, Section 7631, also on the configuration of the LCP activation complex, where Rigshospitalet, Blegdamsvej 9, DK 2100 Copenhagen, Denmark. E-mail address: [email protected] the possible existence of MASP heterodimers has not been firmly established. Abbreviations used in this article: CHO, Chinese hamster ovary; CL, collectin; I/R, ischemia/reperfusion; LCP, lectin complement pathway; MAP-1, mannose-binding In general, it is debated how the initial activation mechanism in lectin/ficolin/collectin-11–associated protein-1; MASP, mannose-binding lectin/fico- the LCP works. Whether the protease domains of MASPs are cis- lin/collectin-11–associated serine protease; MBL, mannose-binding lectin; NHS, nor- mal human serum; pAb, polyclonal Ab; PRM, pattern-recognition molecule; RPMI+ activatedwithinthe same dimer (17), trans-activated between suppl, RPMI 1640 medium supplemented with 10% FCS, 100 U/ml penicillin, 0.1 separate dimers (18), or whether there is an alternative means of mg/ml streptomycin, 2 mM L-glutamine, and 200 nM methotrexate; SEC, size- activation is still not clear. The existence of MAP-1 hetero- exclusion chromatography; TBS/Ca/Tw, TBS/2 mM CaCl /0.05% Tween 20. 2 complexes could, in any case, very well influence complement Copyright Ó 2014 by The American Association of Immunologists, Inc. 0022-1767/14/$16.00 activation, because a protease-to-protease coactivation step would www.jimmunol.org/cgi/doi/10.4049/jimmunol.1303263 The Journal of Immunology 4353 be disrupted. The observation that heterocomplex formation be- The same procedure was done with the addition of 10 mM EDTA in the tween MAP-1 and the MASPs occurs would therefore indicate the immunoprecipitation step. existence of an alternative inhibitory mechanism of MAP-1 and Size-exclusion chromatography of in vitro heterocomplexes indicate that the LCP actually comprises MASP heterocomplexes m m as well. MAP-1 (75 g) and MASP-1 or -3 (150 g) heterocomplexes were gen- erated as described above. 300 ml complex solution were run on a Super- dex 200 HR 10/30 column (GE Healthcare) including complexes that had Materials and Methods been preincubated with 10 mM EDTA for 2 h. In addition, rMAP-1, Primary Abs rMASP-1,andrMASP-3dilutedinTBS/5mMCaCl2 or TBS/10 mM EDTA were analyzed separately. Running buffers corresponded to the In-house produced mAbs used in the following assays were: anti–MASP-1/- applied dilution buffers. Fractions of 0.5 ml were collected and used in 3 mAb F3-46 (14), anti–MAP-1 mAb 20C4 (10), anti–MASP-3 mAb 7D8, western blotting probing with a combination of biotinylated mAbs 8B3 and and anti–MASP-1/-3/MAP-1 mAb 8B3 (19), anti–ficolin-1 mAb FCN166 20C4. (20) anti–ficolin-2 mAbs FCN216 and FCN219 (21), and anti–ficolin-3 mAb FCN334 (22). Moreover, we used the following commercial Abs: Cotransfection of CHO cells anti–MASP-1 polyclonal Ab (pAb) (C-20, sc-50839; Santa Cruz Bio- CHO cells expressing rMAP-1 and rMASP-3 as previously described were technology, Heidelberg, Germany), anti–ficolin-1 pAb (HP9039; Hycult transiently transfected with a MASP-3 or MAP-1 vector, respectively. Cells Biotech, Uden, The Netherlands), anti-MBL mAbs (HYB 131-10 and 131- were seeded in a culture plate with RPMI+suppl in triplicates of 0.5 3 104 11; Bioporto Diagnotics, Gentofte, Denmark), and finally, anti–CL-11 pAb cells/well. The next day, the culture supernatant were replaced with a mix (antiCOLEC-11, 15269-1-AP; Proteintech, Manchester, U.K.). of DMEM (Life Technologies), Lipofectamine 2000 (Life Technologies), Biotin labeling and vector. Detection of heterocomplexes in the culture supernatant was performed in ELISA assays as previously described using capturing Abs Biotin labeling was done using biotin-N-hydroxysuccinimide ester (H1759; that targeted the transiently expressed heterocomplex proteins (mAbs 7D8/ Downloaded from Sigma-Aldrich, Broendby, Denmark).
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