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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4 Pt 1
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pubmed:dateCreated |
1991-5-17
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pubmed:abstractText |
Surfactant protein D (SP-D) is a collagenous, surfactant-associated, carbohydrate-binding protein that is synthesized by alveolar type II epithelial cells. To further characterize SP-D, we isolated RNA from adult rat lungs and rat type II cells and translated mRNAs in vitro. [35S]methionine-labeled translation products were precipitated with antibodies to rat SP-D, resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and visualized by fluorography. Immune precipitates of translation reactions for rat lung or rat type II cells demonstrated a single collagenous polypeptide (39.3 kDa) that was smaller than surfactant-associated SP-D (43 kDa, reduced) but larger than the mature secreted form of rat SP-A. This component was not identified in translation reactions of rat liver, gut, brain, mammary gland, or rat L2 cell RNA. There was a fivefold enrichment of SP-D mRNA in freshly isolated type II cells relative to lung; however, the levels of translatable SP-D mRNA decreased rapidly during the first 24 h of cell culture. The SP-D translation product migrated faster than the major cellular form of SP-D but approximately 1 kDa slower than cellular SP-D synthesized in the presence of 2,2'-dipyridyl plus tunicamycin. Translation in the presence of canine pancreatic microsomes gave a single glycosylated, endoglycosidase F-sensitive form (40.6 kDa) and demonstrated cleavage of a small signal peptide. These results indicate that SP-D is a secretory product of differentiated type II epithelial cells and that SP-D is secreted in a mature form that does not undergo further proteolytic processing in vivo.
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pubmed:grant | |
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/Methionine,
http://linkedlifedata.com/resource/pubmed/chemical/Poly A,
http://linkedlifedata.com/resource/pubmed/chemical/Pulmonary Surfactant-Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/Pulmonary Surfactants,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0002-9513
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
260
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
L247-53
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1708210-Animals,
pubmed-meshheading:1708210-Cell-Free System,
pubmed-meshheading:1708210-Dogs,
pubmed-meshheading:1708210-Epithelium,
pubmed-meshheading:1708210-Glycoproteins,
pubmed-meshheading:1708210-Male,
pubmed-meshheading:1708210-Methionine,
pubmed-meshheading:1708210-Microsomes,
pubmed-meshheading:1708210-Pancreas,
pubmed-meshheading:1708210-Poly A,
pubmed-meshheading:1708210-Protein Biosynthesis,
pubmed-meshheading:1708210-Protein Processing, Post-Translational,
pubmed-meshheading:1708210-Pulmonary Alveoli,
pubmed-meshheading:1708210-Pulmonary Surfactant-Associated Protein D,
pubmed-meshheading:1708210-Pulmonary Surfactants,
pubmed-meshheading:1708210-RNA,
pubmed-meshheading:1708210-RNA, Messenger,
pubmed-meshheading:1708210-Rats,
pubmed-meshheading:1708210-Rats, Inbred Strains,
pubmed-meshheading:1708210-Reticulocytes
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pubmed:year |
1991
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pubmed:articleTitle |
Primary translation products of pulmonary surfactant protein D.
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pubmed:affiliation |
Department of Pathology, Jewish Hospital, Washington University Medical Center, St. Louis, Missouri.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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