title: Secretion of surfactant protein A from rat type II pneumocytes.
abstract: Secretion of surfactant phosphatidylcholine has been extensively studied and there is evidence that it is a regulated process that can be influenced by a variety of physiological factors and pharmacological agents. In contrast, secretion of the major surfactant protein, surfactant protein A (SP-A), has been investigated to much lesser extent. It is not known whether SP-A secretion is constitutive or regulated and, if regulated, whether its regulation is similar to that of phosphatidylcholine. To address those questions we measured SP-A secretion in primary cultures of type II pneumocytes under conditions identical to those used to study phosphatidylcholine secretion. Freshly isolated cells from adult rats were cultured overnight, washed, and then incubated in fresh medium in the presence and absence of surfactant phospholipid secretagogues. As previously reported for phosphatidylcholine, SP-A secretion was linear with time for up to 4 h. However, the rate of SP-A secretion, approximately 6% of total SP-A (cells+medium) released into the medium per hour, was more than sixfold greater than that of the lipid. Although freshly isolated cells contained 70% more SP-A than cells that were cultured overnight, the rate of SP-A secretion was not significantly different. Secretion of SP-A by freshly isolated or cultured type II cells was not increased by a combination of ATP, terbutaline, the adenosine A2 receptor agonist 5'(N-ethylcarboxyamido)adenosine, 12-O-tetradecanoylphorbol-13-acetate, and ionomycin at concentrations that optimally stimulated phosphatidylcholine secretion. We conclude that secretion of the major lipid and protein components of surfactant are independently regulated.
authors.affiliation: Department of Pediatrics, Yale University, School of Medicine, New Haven, Connecticut 06510.
authors.forename: S A
authors.initials: SA
authors.lastname: Rooney
authors.forename: L I
authors.initials: LI
authors.lastname: Gobran
authors.forename: T M
authors.initials: TM
authors.lastname: Umstead
authors.forename: D S
authors.initials: DS
authors.lastname: Phelps
mesh_terms: D000241:Adenosine / Q000031:analogs & derivatives / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000494:pharmacology; D019830:Adenosine-5'-(N-ethylcarboxamide); D000818:Animals; D015153:Blotting, Western; D002478:Cells, Cultured; D003208:Concanavalin A / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D007106:Immune Sera; D015759:Ionomycin / Q000494:pharmacology; D037102:Lectins / Q000494:pharmacology; D008168:Lung / Q000187:drug effects / Q000502:physiology*; D008970:Molecular Weight; D010713:Phosphatidylcholines / Q000378:metabolism; D037121:Plant Lectins; D011510:Proteolipids / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism; D037662:Pulmonary Surfactant-Associated Protein A; D037661:Pulmonary Surfactant-Associated Proteins; D011663:Pulmonary Surfactants / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism; D051381:Rats; D018048:Receptors, Purinergic P2 / Q000187:drug effects / Q000502:physiology; D013053:Spectrophotometry; D013726:Terbutaline / Q000494:pharmacology; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
chemical_list: D007106:Immune Sera; D037102:Lectins; D010713:Phosphatidylcholines; D037121:Plant Lectins; D011510:Proteolipids; D037662:Pulmonary Surfactant-Associated Protein A; D037661:Pulmonary Surfactant-Associated Proteins; D011663:Pulmonary Surfactants; D018048:Receptors, Purinergic P2; D003208:Concanavalin A; C034551:maclurin; D019830:Adenosine-5'-(N-ethylcarboxamide); D015759:Ionomycin; D000255:Adenosine Triphosphate; D000241:Adenosine; D013726:Terbutaline; D013755:Tetradecanoylphorbol Acetate