Source:http://linkedlifedata.com/resource/pubmed/id/15814723
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
8
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| pubmed:dateCreated |
2005-4-7
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| pubmed:abstractText |
Surfactant protein D (SP-D) and CD14 are important innate immune defense molecules that mediate clearance of pathogens and apoptotic cells from the lung. To test whether CD14 expression and function were influenced by SP-D, the surface expression of CD14 was assessed on alveolar macrophages from SP-D-/- mice. CD14 was reduced on alveolar macrophages from SP-D-/- mice and was associated with reduced uptake of LPS and decreased production of TNF-alpha after LPS stimulation. CD14 is proteolytically cleaved from the cell surface to form a soluble peptide. Soluble CD14 (sCD14) was increased in the bronchoalveolar lavage fluid from SP-D-/- mice. Because matrix metalloproteinase (MMP)-9 and -12 activities were increased in the lungs of SP-D-/- mice, the role of these metalloproteases in the production of sCD14 was assessed. sCD14 was decreased in both MMP(9-/-)/SP-D-/- and MMP12(-/-)/SP-D-/- mice demonstrating MMP-9 and MMP-12 contribute to proteolytic shedding of CD14. The increased sCD14 seen in SP-D-/- mice was dependent upon the activation of MMP-12 via an MMP-9-dependent mechanism. Supporting this observation, MMP-12 caused the release of sCD14 from RAW 264.7 cells in vitro. In conclusion, SP-D influences innate host defense, in part, by regulating sCD14 in a process mediated by MMP-9 and MMP-12.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD14,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 12,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 9,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Pulmonary Surfactant-Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
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| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0022-1767
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
174
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
4953-9
|
| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:15814723-Animals,
pubmed-meshheading:15814723-Antigens, CD14,
pubmed-meshheading:15814723-Base Sequence,
pubmed-meshheading:15814723-Bronchoalveolar Lavage Fluid,
pubmed-meshheading:15814723-DNA,
pubmed-meshheading:15814723-Endocytosis,
pubmed-meshheading:15814723-Female,
pubmed-meshheading:15814723-Immunity, Innate,
pubmed-meshheading:15814723-Lipopolysaccharides,
pubmed-meshheading:15814723-Macrophages, Alveolar,
pubmed-meshheading:15814723-Male,
pubmed-meshheading:15814723-Matrix Metalloproteinase 12,
pubmed-meshheading:15814723-Matrix Metalloproteinase 9,
pubmed-meshheading:15814723-Metalloendopeptidases,
pubmed-meshheading:15814723-Mice,
pubmed-meshheading:15814723-Mice, Knockout,
pubmed-meshheading:15814723-Mice, Transgenic,
pubmed-meshheading:15814723-Pulmonary Surfactant-Associated Protein D,
pubmed-meshheading:15814723-RNA, Messenger,
pubmed-meshheading:15814723-Solubility
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| pubmed:year |
2005
|
| pubmed:articleTitle |
Surfactant protein-D regulates soluble CD14 through matrix metalloproteinase-12.
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| pubmed:affiliation |
Division of Neonatology and Pulmonary Biology, Cincinnati Children's Hospital Medical Center, Cincinnati, OH 45229, USA.
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| pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|