| http://purl.uniprot.org/citations/18165226 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18165226 | http://www.w3.org/2000/01/rdf-schema#comment | "Extracellular superoxide dismutase (EC-SOD) is expressed at high levels in lungs. EC-SOD has a polycationic matrix-binding domain that binds to polyanionic constituents in the matrix. Previous studies indicate that EC-SOD protects the lung in both bleomycin- and asbestos-induced models of pulmonary fibrosis. Although the mechanism of EC-SOD protection is not fully understood, these studies indicate that EC-SOD plays an important role in regulating inflammatory responses to pulmonary injury. Hyaluronan is a polyanionic high molecular mass polysaccharide found in the extracellular matrix that is sensitive to oxidant-mediated fragmentation. Recent studies found that elevated levels of low molecular mass hyaluronan are associated with inflammatory conditions. We hypothesize that EC-SOD may inhibit pulmonary inflammation in part by preventing superoxide-mediated fragmentation of hyaluronan to low molecular mass fragments. We found that EC-SOD directly binds to hyaluronan and significantly inhibits oxidant-induced degradation of this glycosaminoglycan. In vitro human polymorphic neutrophil chemotaxis studies indicate that oxidative fragmentation of hyaluronan results in polymorphic neutrophil chemotaxis and that EC-SOD can completely prevent this response. Intratracheal injection of crocidolite asbestos in mice leads to pulmonary inflammation and injury that is enhanced in EC-SOD knock-out mice. Notably, hyaluronan levels are increased in the bronchoalveolar lavage fluid after asbestos-induced pulmonary injury, and this response is markedly enhanced in EC-SOD knock-out mice. These data indicate that inhibition of oxidative hyaluronan fragmentation probably represents one mechanism by which EC-SOD inhibits inflammation in response to lung injury."xsd:string |
| http://purl.uniprot.org/citations/18165226 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m709273200"xsd:string |
| http://purl.uniprot.org/citations/18165226 | http://purl.uniprot.org/core/author | "Gao F."xsd:string |
| http://purl.uniprot.org/citations/18165226 | http://purl.uniprot.org/core/author | "Jiang D."xsd:string |
| http://purl.uniprot.org/citations/18165226 | http://purl.uniprot.org/core/author | "Liang J."xsd:string |
| http://purl.uniprot.org/citations/18165226 | http://purl.uniprot.org/core/author | "Noble P.W."xsd:string |
| http://purl.uniprot.org/citations/18165226 | http://purl.uniprot.org/core/author | "Oury T.D."xsd:string |
| http://purl.uniprot.org/citations/18165226 | http://purl.uniprot.org/core/author | "Tobolewski J.M."xsd:string |
| http://purl.uniprot.org/citations/18165226 | http://purl.uniprot.org/core/author | "Koenitzer J.R."xsd:string |
| http://purl.uniprot.org/citations/18165226 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18165226 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/18165226 | http://purl.uniprot.org/core/pages | "6058-6066"xsd:string |
| http://purl.uniprot.org/citations/18165226 | http://purl.uniprot.org/core/title | "Extracellular superoxide dismutase inhibits inflammation by preventing oxidative fragmentation of hyaluronan."xsd:string |
| http://purl.uniprot.org/citations/18165226 | http://purl.uniprot.org/core/volume | "283"xsd:string |
| http://purl.uniprot.org/citations/18165226 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18165226 |
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