期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 285, 期 36, 页码 28174-28182出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.106518
关键词
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资金
- Austrian FWF [P17501, P 20472]
- Spanish Ministry of Science [BIO2009-09694, CSD2007-00010]
- Community of Madrid [S2009MAT-1507]
- European Commission [RTN-512229]
- Austrian Science Fund (FWF) [P17501] Funding Source: Austrian Science Fund (FWF)
- Austrian Science Fund (FWF) [P 20472] Funding Source: researchfish
Pulmonary surfactant is essential for lung function. It is assembled, stored and secreted as particulate entities (lamellar body-like particles; LBPs). LBPs disintegrate when they contact an air-liquid interface, leading to an instantaneous spreading of material and a decline in surface tension. Here, we demonstrate that the film formed by the adsorbed material spontaneously segregate into distinct ordered and disordered lipid phase regions under unprecedented near-physiological conditions and, unlike natural surfactant purified from bronchoalveolar lavages, dynamically reorganized into highly viscous multilayer domains with complex three-dimensional topographies. Multilayer domains, in coexistence with liquid phases, showed a progressive stiffening and finally solidification, probably driven by a self-driven disassembly of LBPs from a sub-surface compartment. We conclude that surface film formation from LBPs is a highly dynamic and complex process, leading to a more elaborated scenario than that observed and predicted by models using reconstituted, lavaged, or fractionated preparations.
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