| pubmed-article:1634623 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1634623 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:1634623 | lifeskim:mentions | umls-concept:C0014833 | lld:lifeskim |
| pubmed-article:1634623 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1634623 | lifeskim:mentions | umls-concept:C0023810 | lld:lifeskim |
| pubmed-article:1634623 | lifeskim:mentions | umls-concept:C0084692 | lld:lifeskim |
| pubmed-article:1634623 | lifeskim:mentions | umls-concept:C1535502 | lld:lifeskim |
| pubmed-article:1634623 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:1634623 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1634623 | pubmed:dateCreated | 1992-8-24 | lld:pubmed |
| pubmed-article:1634623 | pubmed:abstractText | Surfactant protein D (SP-D) is a collagenous glycoprotein that is secreted into the pulmonary airspaces by alveolar type II and nonciliated bronchiolar cells. SP-D exhibits Ca(++)-dependent carbohydrate binding in vitro and is structurally related to the collagenous C-type lectins, including serum conglutinin, serum mannose-binding proteins, and surfactant protein A. Preliminary studies showed calcium- and saccharide-dependent binding of fluorescein-conjugated or radioiodinated SP-D to a variety of microorganisms, including Gram-negative bacteria and fungi. A laboratory strain of Escherichia coli (Y1088) was chosen to further examine the mechanism(s) of binding. Binding of SP-D to Y1088 was time dependent, saturable, and inhibited by cold SP-D or competing saccharides; Scatchard analysis gave a Kd of 2 x 10(-11) M. At higher concentrations, SP-D also caused Ca(++)-dependent agglutination of Y1088 that was inhibited by alpha-glucosyl-containing saccharides, antisera to the carbohydrate-binding domain of SP-D, or Y1088 LPS. Lectin blots showed specific binding of 125I-SP-D to Y1088 LPS, as well as LPS from other several strains of enteric Gram-negative bacteria. Immunogold studies demonstrated strong and uniform surface labeling of the bacteria. Rat and human bronchoalveolar lavage (BAL) caused Ca(++)-dependent agglutination of E. coli that was dose dependent and inhibited by competing saccharides or anti-SP-D. SP-D was selectively and efficiently adsorbed from rat BAL by incubation with E. coli, and incubation of E. coli with radiolabeled rat type II cell medium revealed that SP-D is the major E. coli-binding protein secreted by freshly isolated cells in culture. We suggest that SP-D plays important roles in the lung's defense against Gram-negative bacteria. | lld:pubmed |
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| pubmed-article:1634623 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1634623 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1634623 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:1634623 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1634623 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:1634623 | pubmed:issn | 0021-9738 | lld:pubmed |
| pubmed-article:1634623 | pubmed:author | pubmed-author:RusuJJ | lld:pubmed |
| pubmed-article:1634623 | pubmed:author | pubmed-author:CrouchEE | lld:pubmed |
| pubmed-article:1634623 | pubmed:author | pubmed-author:KuanS FSF | lld:pubmed |
| pubmed-article:1634623 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1634623 | pubmed:volume | 90 | lld:pubmed |
| pubmed-article:1634623 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1634623 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1634623 | pubmed:pagination | 97-106 | lld:pubmed |
| pubmed-article:1634623 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1634623 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1634623 | pubmed:articleTitle | Interactions of surfactant protein D with bacterial lipopolysaccharides. Surfactant protein D is an Escherichia coli-binding protein in bronchoalveolar lavage. | lld:pubmed |
| pubmed-article:1634623 | pubmed:affiliation | Department of Pathology, Jewish Hospital, Washington University Medical Center, St. Louis, Missouri 63110. | lld:pubmed |
| pubmed-article:1634623 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1634623 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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