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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
29
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pubmed:dateCreated |
1992-11-18
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pubmed:abstractText |
Alveolar type II cells produce and secrete a complex mixture of lipids and proteins called pulmonary surfactant of which phospholipids are the major components. Surfactant proteins (SP) A, B, and C interact with phospholipids and are believed to play important roles in alveolar spaces. However, whether surfactant protein D (SP-D) interacts with phospholipids is unknown. In the present study, we examined whether SP-D binds to phospholipids and investigated phospholipid specificities of SP-D binding and the structural requirements of phospholipids for that binding using 125I-SP-D as a probe. 125I-SP-D bound exclusively to phosphatidylinositol (PI) in various phospholipids or a fraction containing phospholipids extracted from surfactant, which were developed on thin layer chromatography. 125I-SP-D also bound to PI coated on microtiter wells in a manner dependent upon the SP-D concentration. Unlabeled SP-D competed well with 125I-SP-D for PI binding and the antibody against SP-D abolished 125I-SP-D binding to PI. PI liposome also attenuated 125I-SP-D binding to the solid phase PI. Ca2+ is absolutely required for the binding of SP-D to PI. SP-D failed to bind to lyso-PI, fatty acids derived from PI digested with phospholipase A2, or diacylglycerol obtained after phospholipase C treatment of PI. SP-D bound to neither phosphatidylinositol 4-monophosphate nor phosphatidylinositol 4,5-diphosphate. We conclude that SP-D specifically binds to PI. This is the first report that demonstrates that SP-D interacts with surfactant phospholipids.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Liposomes,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Pulmonary Surfactant-Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/Pulmonary Surfactants
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21244-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1400434-Animals,
pubmed-meshheading:1400434-Bronchoalveolar Lavage Fluid,
pubmed-meshheading:1400434-Chromatography, Affinity,
pubmed-meshheading:1400434-Chromatography, Thin Layer,
pubmed-meshheading:1400434-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1400434-Glycoproteins,
pubmed-meshheading:1400434-Kinetics,
pubmed-meshheading:1400434-Liposomes,
pubmed-meshheading:1400434-Phosphatidylinositols,
pubmed-meshheading:1400434-Phospholipids,
pubmed-meshheading:1400434-Pulmonary Surfactant-Associated Protein D,
pubmed-meshheading:1400434-Pulmonary Surfactants,
pubmed-meshheading:1400434-Rats
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pubmed:year |
1992
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pubmed:articleTitle |
Pulmonary surfactant protein D specifically binds to phosphatidylinositol.
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pubmed:affiliation |
Department of Biochemistry, Sapporo Medical College, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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