Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4 Pt 1
pubmed:dateCreated
1991-5-17
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0002-9513
pubmed:author
pubmed:issnType
Print
pubmed:volume
260
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
L247-53
pubmed:dateRevised
2007-11-14
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
pubmed:year
1991
pubmed:articleTitle
Primary translation products of pulmonary surfactant protein D.
pubmed:affiliation
Department of Pathology, Jewish Hospital, Washington University Medical Center, St. Louis, Missouri.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.