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http://purl.uniprot.org/citations/12842807http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12842807http://www.w3.org/2000/01/rdf-schema#comment"Matrix metalloproteinase (MMP)-9 from alveolar macrophages is a major source of elastolytic activity in the lung. It is increased in the bronchoalveolar lavage fluid of patients with emphysema. Although the importance of macrophage-derived elastolytic activity in the pathogenesis of emphysema is well established, questions remain about MMP-9 regulation and activity. Because surfactant protein A (SP-A) is capable of modulating other functions of human monocytic cells, we hypothesized that SP-A may regulate MMP-9 expression. Vitamin D3-differentiated THP-1 cells and peripheral blood mononuclear cells were stimulated in vitro with several concentrations of SP-A for different incubation times. MMP-9 mRNA expression was measured by dot-blot analysis, gelatinolytic activity in the medium was determined by gel zymography, protein expression was determined by ELISA, and a specific MMP-9 activity assay was used to measure the state of activation of this enzyme in the cell supernatants. SP-A induced the expression of MMP-9 in both cell types, the effect was time and dose dependent, and MMP-9 was released in its zymogen form. On the basis of results of neutralizing antibody studies, we believe that SP-A action is mediated through Toll-like receptor-2. Even though the biological meaning of these findings remains to be elucidated, these observations suggest the presence of a novel, locally controlled mechanism by which MMP-9 levels may be regulated in alveolar macrophages. We speculate that SP-A may influence the protease/antiprotease balance in the lungs of patients with quantitative and/or qualitative changes in surfactant constituents favoring an abnormal breakdown of extracellular matrix components."xsd:string
http://purl.uniprot.org/citations/12842807http://purl.org/dc/terms/identifier"doi:10.1152/ajplung.00082.2003"xsd:string
http://purl.uniprot.org/citations/12842807http://purl.uniprot.org/core/author"Umstead T.M."xsd:string
http://purl.uniprot.org/citations/12842807http://purl.uniprot.org/core/author"Phelps D.S."xsd:string
http://purl.uniprot.org/citations/12842807http://purl.uniprot.org/core/author"Davis S.E."xsd:string
http://purl.uniprot.org/citations/12842807http://purl.uniprot.org/core/author"Vazquez de Lara L.G."xsd:string
http://purl.uniprot.org/citations/12842807http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12842807http://purl.uniprot.org/core/name"Am J Physiol Lung Cell Mol Physiol"xsd:string
http://purl.uniprot.org/citations/12842807http://purl.uniprot.org/core/pages"L899-906"xsd:string
http://purl.uniprot.org/citations/12842807http://purl.uniprot.org/core/title"Surfactant protein A increases matrix metalloproteinase-9 production by THP-1 cells."xsd:string
http://purl.uniprot.org/citations/12842807http://purl.uniprot.org/core/volume"285"xsd:string
http://purl.uniprot.org/citations/12842807http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12842807
http://purl.uniprot.org/citations/12842807http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12842807
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