| pubmed-article:7642568 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7642568 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:7642568 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:7642568 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:7642568 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:7642568 | lifeskim:mentions | umls-concept:C0084692 | lld:lifeskim |
| pubmed-article:7642568 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:7642568 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:7642568 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:7642568 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:7642568 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:7642568 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:7642568 | pubmed:issue | 32 | lld:pubmed |
| pubmed-article:7642568 | pubmed:dateCreated | 1995-9-18 | lld:pubmed |
| pubmed-article:7642568 | pubmed:abstractText | Surfactant protein D (SP-D) is a member of the C-type lectin superfamily with four distinct structural domains: an amino terminus involved in forming intermolecular disulfides, a collagen-like domain, a neck region, and a carbohydrate recognition domain. A collagen domain deletion mutant (CDM) of SP-D was created by site-directed mutagenesis. A second variant lacking both the amino-terminal region and the collagen-like domain was generated by collagenase treatment and purification of the collagenase-resistant fragment (CRF). The CDM expressed in CHO-K1 cells formed the covalent trimers, but not the noncovalent dodecamers, typical of native SP-D. The CRF derived from recombinant SP-D formed only monomers. The CDM bound mannose-Sepharose and phosphatidylinositol (PI) as well as SP-D, but the binding to mannosyl bovine serum albumin and glucosylceramide was diminished by approximately 60%. The CRF displayed weak binding to mannose-Sepharose and PI and essentially no binding to mannosyl bovine serum albumin and glucosylceramide. Both SP-D and CDM altered the self-aggregation of PI-containing liposomes. SP-D reduced the density and the light scattering properties of PI aggregates. These results demonstrate that the collagen-like domain is required for dodecamer but not covalent trimer formation of SP-D and plays an important, but not essential, role in the interaction of SP-D with PI and GlcCer. Removal of the amino-terminal domain of SP-D along with the collagen-like domain diminishes PI binding and effectively eliminates GlcCer binding. | lld:pubmed |
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| pubmed-article:7642568 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7642568 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7642568 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7642568 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:7642568 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7642568 | pubmed:author | pubmed-author:VoelkerD RDR | lld:pubmed |
| pubmed-article:7642568 | pubmed:author | pubmed-author:OgasawaraYY | lld:pubmed |
| pubmed-article:7642568 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7642568 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:7642568 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:7642568 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7642568 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7642568 | pubmed:pagination | 19052-8 | lld:pubmed |
| pubmed-article:7642568 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:7642568 | pubmed:meshHeading | pubmed-meshheading:7642568-... | lld:pubmed |
| pubmed-article:7642568 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7642568 | pubmed:articleTitle | The role of the amino-terminal domain and the collagenous region in the structure and the function of rat surfactant protein D. | lld:pubmed |
| pubmed-article:7642568 | pubmed:affiliation | Lord and Taylor Laboratory for Lung Biochemistry, National Jewish Center for Immunology and Respiratory Medicine, Denver, Colorado 80206, USA. | lld:pubmed |
| pubmed-article:7642568 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7642568 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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