[{"quality_controlled":"1","oa":1,"day":"22","publication":"Journal of Biological Chemistry","dc":{"date":["2011"],"type":["info:eu-repo/semantics/article","doc-type:article","text","http://purl.org/coar/resource_type/c_6501"],"publisher":["American Society for Biochemistry & Molecular Biology"],"relation":["info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.m111.247395","info:eu-repo/semantics/altIdentifier/issn/0021-9258","info:eu-repo/semantics/altIdentifier/issn/1083-351X"],"source":["Baranova NS, Nilebäck E, Haller FM, et al. The inflammation-associated protein TSG-6 cross-links hyaluronan via hyaluronan-induced TSG-6 oligomers. Journal of Biological Chemistry. 2011;286(29):25675-25686. doi:10.1074/jbc.m111.247395"],"identifier":["https://research-explorer.ista.ac.at/record/6298"],"description":["Tumor necrosis factor-stimulated gene-6 (TSG-6) is a hyalu-ronan (HA)-binding protein that plays important roles ininflammation and ovulation. TSG-6-mediated cross-linking ofHA has been proposed as a functional mechanism (e.g.for regu-lating leukocyte adhesion), but direct evidence for cross-linkingis lacking, and we know very little about its impact on HA ultra-structure. Here we used films of polymeric and oligomeric HAchains, end-grafted to a solid support, and a combination ofsurface-sensitive biophysical techniques to quantify the bindingof TSG-6 into HA films and to correlate binding to morpholog-ical changes. We find that full-length TSG-6 binds with pro-nounced positive cooperativity and demonstrate that it cancross-link HA at physiologically relevant concentrations. Ourdata indicate that cooperative binding of full-length TSG-6arises from HA-induced protein oligomerization and that theTSG-6 oligomers act as cross-linkers. In contrast, the HA-bind-ing domain of TSG-6 (the Link module) alone binds withoutpositive cooperativity and weaker than the full-length protein.Both the Link module and full-length TSG-6 condensed andrigidified HA films, and the degree of condensation scaled withthe affinity between the TSG-6 constructs and HA. We proposethat condensation is the result of protein-mediated HA cross-linking. Our findings firmly establish that TSG-6 is a potent HAcross-linking agent and might hence have important implica-tions for the mechanistic understanding of the biological func-tion of TSG-6 (e.g.in inflammation)."],"title":["The inflammation-associated protein TSG-6 cross-links hyaluronan via hyaluronan-induced TSG-6 oligomers"],"creator":["Baranova, Natalia","Nilebäck, Erik","Haller, F. Michael","Briggs, David C.","Svedhem, Sofia","Day, Anthony J.","Richter, Ralf P."],"language":["eng"],"rights":["info:eu-repo/semantics/openAccess"]},"date_published":"2011-07-22T00:00:00Z","date_created":"2019-04-11T20:57:43Z","uri_base":"https://research-explorer.ista.ac.at","page":"25675-25686","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","citation":{"ieee":"N. S. Baranova et al., “The inflammation-associated protein TSG-6 cross-links hyaluronan via hyaluronan-induced TSG-6 oligomers,” Journal of Biological Chemistry, vol. 286, no. 29. American Society for Biochemistry & Molecular Biology, pp. 25675–25686, 2011.","short":"N.S. Baranova, E. Nilebäck, F.M. Haller, D.C. Briggs, S. Svedhem, A.J. Day, R.P. Richter, Journal of Biological Chemistry 286 (2011) 25675–25686.","apa":"Baranova, N. S., Nilebäck, E., Haller, F. M., Briggs, D. C., Svedhem, S., Day, A. J., & Richter, R. P. (2011). The inflammation-associated protein TSG-6 cross-links hyaluronan via hyaluronan-induced TSG-6 oligomers. Journal of Biological Chemistry. American Society for Biochemistry & Molecular Biology. https://doi.org/10.1074/jbc.m111.247395","mla":"Baranova, Natalia S., et al. “The Inflammation-Associated Protein TSG-6 Cross-Links Hyaluronan via Hyaluronan-Induced TSG-6 Oligomers.” Journal of Biological Chemistry, vol. 286, no. 29, American Society for Biochemistry & Molecular Biology, 2011, pp. 25675–86, doi:10.1074/jbc.m111.247395.","ista":"Baranova NS, Nilebäck E, Haller FM, Briggs DC, Svedhem S, Day AJ, Richter RP. 2011. The inflammation-associated protein TSG-6 cross-links hyaluronan via hyaluronan-induced TSG-6 oligomers. Journal of Biological Chemistry. 286(29), 25675–25686.","chicago":"Baranova, Natalia S., Erik Nilebäck, F. Michael Haller, David C. Briggs, Sofia Svedhem, Anthony J. Day, and Ralf P. Richter. “The Inflammation-Associated Protein TSG-6 Cross-Links Hyaluronan via Hyaluronan-Induced TSG-6 Oligomers.” Journal of Biological Chemistry. American Society for Biochemistry & Molecular Biology, 2011. https://doi.org/10.1074/jbc.m111.247395."},"dini_type":"doc-type:article","author":[{"last_name":"Baranova","orcid":"0000-0002-3086-9124","first_name":"Natalia","id":"38661662-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Erik","last_name":"Nilebäck"},{"last_name":"Haller","first_name":"F. Michael"},{"first_name":"David C.","last_name":"Briggs"},{"first_name":"Sofia","last_name":"Svedhem"},{"last_name":"Day","first_name":"Anthony J."},{"last_name":"Richter","first_name":"Ralf P."}],"oa_version":"Published Version","abstract":[{"lang":"eng"}],"month":"07","intvolume":" 286","main_file_link":[{"url":"http://www.jbc.org/content/286/29/25675.full.pdf","open_access":"1"}],"language":[{}],"publication_identifier":{"issn":[]},"publication_status":"published","volume":286,"issue":"29","_id":"6298","status":"public","type":"journal_article","extern":"1","creator":{"login":"nbaranov","id":"38661662-F248-11E8-B48F-1D18A9856A87"},"date_updated":"2021-01-12T08:06:58Z"}]