title: The role of palmitic acid in pulmonary surfactant: enhancement of surface activity and prevention of inhibition by blood proteins.
abstract: The surface activity of two surfactant preparations, Lipid Extract Surfactant (LES) and Survanta, was examined during adsorption and dynamic compression using a pulsating bubble surfactometer. At low surfactant phospholipid concentrations (1-2.5 mg/ml), Survanta reduces surface tension at minimum bubble radius faster than LES: however, with continued pulsation LES obtains a lower surface tension. Addition of surfactant-associated protein A (SP-A) to LES significantly reduces the time required to reduce surface tension. Survanta is completely unresponsive to the addition of SP-A in that no further reduction of surface tension is observed. Addition of various blood components has been previously shown to inactivate surfactants in vitro. Addition of fibrinogen to Survanta causes an increase in surface tension when measured in the absence of calcium. When assayed in the presence of calcium, inhibition by fibrinogen is not observed possibly due to aggregation of this protein. Albumin and alpha-globulin strongly inhibit Survanta at physiological serum concentrations both in the presence and absence of calcium. The surface activity of Survanta is also inhibited by lysophosphatidylcholine (lyso-PC). The role of palmitic acid in the surface activity of pulmonary surfactant was examined by adding palmitic acid to LES. At low phospholipid concentrations addition of palmitic acid (10% w/w of the surfactant phospholipid) greatly enhances the surface activity of LES. Maximal enhancement of surface activity and adsorption was observed at or above 7.5% added palmitic acid (w/w of surfactant lipid). LES supplemented with palmitic acid is more resistant to inhibition by fibrinogen, albumin, alpha-globulin and lyso-PC than LES alone, however, the counteraction of blood protein inhibition is not as pronounced as that observed with SP-A.
authors.affiliation: MRC Group in Fetal and Neonatal Health and Development, Department of Biochemistry, University of Western Ontario, London, Canada.
authors.forename: A M
authors.initials: AM
authors.lastname: Cockshutt
authors.forename: D R
authors.initials: DR
authors.lastname: Absolom
authors.forename: F
authors.initials: F
authors.lastname: Possmayer
mesh_terms: D000418:Albumins / Q000502:physiology; D000818:Animals; D001798:Blood Proteins / Q000494:pharmacology; D002118:Calcium / Q000502:physiology; D002417:Cattle; D008055:Lipids / Q000737:chemistry; D010169:Palmitic Acids / Q000737:chemistry / Q000494:pharmacology*; D011510:Proteolipids / Q000494:pharmacology; D037662:Pulmonary Surfactant-Associated Protein A; D037661:Pulmonary Surfactant-Associated Proteins; D011663:Pulmonary Surfactants / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000494:pharmacology*; D013500:Surface Tension
chemical_list: D000418:Albumins; D001798:Blood Proteins; D008055:Lipids; D010169:Palmitic Acids; D011510:Proteolipids; D037662:Pulmonary Surfactant-Associated Protein A; D037661:Pulmonary Surfactant-Associated Proteins; D011663:Pulmonary Surfactants; D002118:Calcium