| pubmed-article:11667972 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11667972 | lifeskim:mentions | umls-concept:C2709248 | lld:lifeskim |
| pubmed-article:11667972 | lifeskim:mentions | umls-concept:C0520990 | lld:lifeskim |
| pubmed-article:11667972 | lifeskim:mentions | umls-concept:C0038891 | lld:lifeskim |
| pubmed-article:11667972 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:11667972 | pubmed:dateCreated | 2001-10-22 | lld:pubmed |
| pubmed-article:11667972 | pubmed:abstractText | Surfactant protein-D (SP-D) participates in the innate response to inhaled microorganisms and organic antigens, and contributes to immune and inflammatory regulation within the lung. SP-D is synthesized and secreted by alveolar and bronchiolar epithelial cells, but is also expressed by epithelial cells lining various exocrine ducts and the mucosa of the gastrointestinal and genitourinary tracts. SP-D, a collagenous calcium-dependent lectin (or collectin), binds to surface glycoconjugates expressed by a wide variety of microorganisms, and to oligosaccharides associated with the surface of various complex organic antigens. SP-D also specifically interacts with glycoconjugates and other molecules expressed on the surface of macrophages, neutrophils, and lymphocytes. In addition, SP-D binds to specific surfactant-associated lipids and can influence the organization of lipid mixtures containing phosphatidylinositol in vitro. Consistent with these diverse in vitro activities is the observation that SP-D-deficient transgenic mice show abnormal accumulations of surfactant lipids, and respond abnormally to challenge with respiratory viruses and bacterial lipopolysaccharides. The phenotype of macrophages isolated from the lungs of SP-D-deficient mice is altered, and there is circumstantial evidence that abnormal oxidant metabolism and/or increased metalloproteinase expression contributes to the development of emphysema. The expression of SP-D is increased in response to many forms of lung injury, and deficient accumulation of appropriately oligomerized SP-D might contribute to the pathogenesis of a variety of human lung diseases. | lld:pubmed |
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| pubmed-article:11667972 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11667972 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
