Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5 Pt 1
pubmed:dateCreated
1993-6-22
pubmed:abstractText
Synthesis and secretion of surfactant protein A (SP-A) were studied in the isolated perfused rat lung using Trans35S-label (approximately 85% methionine, 15% cysteine) in the perfusate with or without 1 mM ATP or 0.1 mM 8-bromoadenosine 3',5',-cyclic monophosphate (8-BrcAMP) for up to 6 h of perfusion. By enzyme-linked immunosorbent assay, the SP-A content was 36 +/- 0.3% of total protein in extracellular surfactant and 10.8 +/- 1.9% of total protein in lamellar bodies of control lungs; these relativr proportions were maintained in the presence of ATP or 8-BrcAMP. Incorporation of [35S]methionine (cysteine) into the surfactant and lamellar body protein fraction could be detected at 4 h of perfusion. At 6 h, specific activity of total protein [disintegrations per minute (dpm)/micrograms)] was significantly increased in both the surfactant (54%) and lamellar body fractions (30%) under the influence of either secretagogue compared with control conditions. In the presence of ATP, there was a significant increase in the SP-A immunoprecipitable counts of 61 and 72% in extra- and intracellular compartments, respectively. However, no significant change was observed in the relative abundance of SP-A mRNA between control and secretagogue-treated lungs. This dissociation of SP-A mRNA abundance and label incorporation into protein indicates that alteration in translational efficiency or posttranslational factors may be involved in the secretagogue-induced stimulation of SP-A synthesis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0002-9513
pubmed:author
pubmed:issnType
Print
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
L431-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8388646-8-Bromo Cyclic Adenosine Monophosphate, pubmed-meshheading:8388646-Adenosine Triphosphate, pubmed-meshheading:8388646-Animals, pubmed-meshheading:8388646-Autoradiography, pubmed-meshheading:8388646-Blotting, Northern, pubmed-meshheading:8388646-Blotting, Western, pubmed-meshheading:8388646-Cyclic AMP, pubmed-meshheading:8388646-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:8388646-Lung, pubmed-meshheading:8388646-Male, pubmed-meshheading:8388646-Methionine, pubmed-meshheading:8388646-Perfusion, pubmed-meshheading:8388646-Proteolipids, pubmed-meshheading:8388646-Pulmonary Surfactant-Associated Protein A, pubmed-meshheading:8388646-Pulmonary Surfactant-Associated Proteins, pubmed-meshheading:8388646-Pulmonary Surfactants, pubmed-meshheading:8388646-RNA, Messenger, pubmed-meshheading:8388646-Rats, pubmed-meshheading:8388646-Rats, Sprague-Dawley, pubmed-meshheading:8388646-Sulfur Radioisotopes, pubmed-meshheading:8388646-Tubulin
pubmed:year
1993
pubmed:articleTitle
ATP and adenosine 3',5'-cyclic monophosphate stimulate the synthesis of surfactant protein A in rat lung.
pubmed:affiliation
Institute for Environmental Medicine, University of Pennsylvania School of Medicine, Philadelphia.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.