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The highly packed and dehydrated structure of preformed unexposed human pulmonary surfactant isolated from amniotic fluid



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Castillo Sánchez, José Carlos and Roldán, Nuria and García Álvarez, Begoña and Batllori, Emma and Galindo Izquierdo, Alberto and Cruz Rodríguez, Antonio and Pérez Gil, Jesús (2022) The highly packed and dehydrated structure of preformed unexposed human pulmonary surfactant isolated from amniotic fluid. American Journal of Physiology - Lung Cellular and Molecular Physiology (AJP - Lung Cellular and Molecular Physiology), 332 . L191-L203. ISSN 1040-0605

[thumbnail of Castillo-Sánchez,  J. C. et al. 2021. The highly packed and dehydrated structure of preformed unexposed.pdf] PDF
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Official URL: https://doi.org/10.1152/ajplung.00230.2021


By coating the alveolar air-liquid interface, lung surfactant overwhelms surface tension forces that, otherwise, would hinder the lifetime effort of breathing. Years of research have provided a picture of how highly hydrophobic and specialized proteins in surfactant promote rapid and efficient formation of phospholipid-based complex three-dimensional films at the respiratory surface, highly stable under the demanding breathing mechanics. However, recent evidence suggests that the structure and performance of surfactant typically isolated from bronchoalveolar lung lavages may be far from that of nascent, still unused, surfactant as freshly secreted by type II pneumocytes into the alveolar airspaces. In the present work, we report the isolation of lung surfactant from human amniotic fluid (amniotic fluid surfactant, AFS) and a detailed description of its composition, structure, and surface activity in comparison to a natural surfactant (NS) purified from porcine bronchoalveolar lavages. We observe that the lipid/ protein complexes in AFS exhibit a substantially higher lipid packing and dehydration than in NS. AFS shows melting transitions at higher temperatures than NS and a conspicuous presence of nonlamellar phases. The surface activity of AFS is not only comparable with that of NS under physiologically meaningful conditions but displays significantly higher resistance to inhibition by serum or meconium, agents that inactivate surfactant in the context of severe respiratory pathologies. We propose that AFS may be the optimal model to study the molecular mechanisms sustaining pulmonary surfactant performance in health and disease, and the reference material to develop improved therapeutic surfactant preparations to treat yet unresolved respiratory pathologies.

Item Type:Article
Uncontrolled Keywords:Human amniotic fluid; Lamellar bodies; Lung surfactant; Membrane structure; Surface activity
Subjects:Medical sciences > Biology > Molecular biology
Medical sciences > Biology > Biochemistry
ID Code:72375
Deposited On:20 May 2022 11:11
Last Modified:23 May 2022 07:19

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