R. Qanbar et al., ROLE OF THE PALMITOYLATION OF SURFACTANT-ASSOCIATED PROTEIN-C IN SURFACTANT FILM FORMATION AND STABILITY, American journal of physiology. Lung cellular and molecular physiology, 15(4), 1996, pp. 572-580
The effect of palmitoylation of pulmonary surfactant-associated protei
n C (SP-C) on the surface activity of phospholipid mixtures of dipalmi
toylphosphatidylcholine and phosphatidylglycerol was studied. Phosphol
ipids reconstituted with palmitoylated or depalmitoylated bovine SP-C
were examined at neutral and acidic pH using a captive bubble surfacto
meter. At low pH, effective lipid adsorption and near zero surface ten
sions upon compression were obtained even with protein-free samples, A
t physiological pH, only SP-C-containing samples achieved such propert
ies. Lipid adsorption was decreased by prior SP-C depalmitoylation. Bu
bbles with palmitoylated SP-C were more mechanically stable and requir
ed less compression to reach low surface tensions. Subphase depletion
experiments showed that dynamically cycled surface layers containing p
almitoylated SP-C maintained their surface activity after subphase lip
id depletion. In contrast, surface activity was rapidly lost where dep
almitoylated SP-C or SP-B tvas included. Our results indicate that alt
hough SP-C palmitoylation has little effect on its ability to enhance
lipid adsorption and surface tension reduction, it greatly enhances li
pid respreading and film stability and is therefore important for surf
actant function.