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Palmitoylation of pulmonary surfactant protein SP-C is critical for its functional cooperation with SP-B to sustain compression/expansion dynamics in cholesterol-containing surfactant films

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Palmitoylation of pulmonary surfactant protein SP-C is critical for its functional cooperation with SP-B to sustain compression/expansion dynamics in cholesterol-containing surfactant films

dc.contributor.author	Baumgart, Florian
dc.contributor.author	Ospina, Olga L.
dc.contributor.author	Mingarro Muñoz, Ismael
dc.contributor.author	Rodríguez Crespo, Ignacio
dc.contributor.author	Pérez Gil, Jesús
dc.date.accessioned	2016-11-30T15:30:32Z
dc.date.available	2016-11-30T15:30:32Z
dc.date.issued	2010
dc.identifier.citation	Baumgart, Florian Ospina, Olga L. Mingarro Muñoz, Ismael Rodríguez Crespo, Ignacio Pérez Gil, Jesús 2010 Palmitoylation of pulmonary surfactant protein SP-C is critical for its functional cooperation with SP-B to sustain compression/expansion dynamics in cholesterol-containing surfactant films Biophysical Journal 99 10 3234 3243
dc.identifier.uri	http://hdl.handle.net/10550/56212
dc.description.abstract	Recent data suggest that a functional cooperation between surfactant proteins SP-B and SP-C may be required to sustain a proper compression-expansion dynamics in the presence of physiological proportions of cholesterol. SP-C is a dually palmitoylated polypeptide of 4.2 kDa, but the role of acylation in SP-C activity is not completely understood. In this work we have compared the behavior of native palmitoylated SP-C and recombinant nonpalmitoylated versions of SP-C produced in bacteria to get a detailed insight into the importance of the palmitic chains to optimize interfacial performance of cholesterol-containing surfactant films. We found that palmitoylation of SP-C is not essential for the protein to promote rapid interfacial adsorption of phospholipids to equilibrium surface tensions (∼22 mN/m), in the presence or absence of cholesterol. However, palmitoylation of SP-C is critical for cholesterol-containing films to reach surface tensions ≤1 mN/m at the highest compression rates assessed in a captive bubble surfactometer, in the presence of SP-B. Interestingly, the ability of SP-C to facilitate reinsertion of phospholipids during expansion was not impaired to the same extent in the absence of palmitoylation, suggesting the existence of palmitoylation-dependent and -independent functions of the protein. We conclude that palmitoylation is key for the functional cooperation of SP-C with SP-B that enables cholesterol-containing surfactant films to reach very low tensions under compression, which could be particularly important in the design of clinical surfactants destined to replacement therapies in pathologies such as acute respiratory distress syndrome.
dc.language.iso	eng
dc.relation.ispartof	Biophysical Journal, 2010, vol. 99, num. 10, p. 3234-3243
dc.subject	Proteïnes
dc.subject	Biofísica
dc.title	Palmitoylation of pulmonary surfactant protein SP-C is critical for its functional cooperation with SP-B to sustain compression/expansion dynamics in cholesterol-containing surfactant films
dc.type	journal article	es_ES
dc.date.updated	2016-11-30T15:30:32Z
dc.identifier.doi	10.1016/j.bpj.2010.08.070
dc.identifier.idgrec	060733
dc.rights.accessRights	open access	es_ES