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A small key unlocks a heavy door: the essential function of the small hydrophobic proteins SP-B and SP-C to trigger adsorption of pulmonary surfactant lamellar bodies

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Hobi, Nina and Giolabi, Michael and Olmeda Lozano, Bárbara and Miklavc, Pika and Felder, Edward and Walter, Paul and Dietl, Paul and Frick, Manfred and Pérez Gil, Jesús and Haller, Thomas (2016) A small key unlocks a heavy door: the essential function of the small hydrophobic proteins SP-B and SP-C to trigger adsorption of pulmonary surfactant lamellar bodies. Biochimica et Biophysica Acta, 1863 (8). pp. 2124-2134. ISSN 0006-3002

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Official URL: http://www.sciencedirect.com/science/article/pii/S0167488916301288



Abstract

The molecular basis involving adsorption of pulmonary surfactant at the respiratory air–liquid interface and the specific roles of the surfactant proteins SP-B and SP-C in this process have not been completely resolved. The reasons might be found in the largely unknown structural assembly in which surfactant lipids and proteins are released from alveolar type II cells, and the difficulties to sample, manipulate and visualize the adsorption of these micron-sized particles at an air–liquid interface under appropriate physiological conditions. Here, we introduce several approaches to overcome these problems. First, by immunofluorescence we could demonstrate the presence of SP-B and SP-C on the surface of exocytosed surfactant particles. Second, by sampling the released particles and probing their adsorptive capacity we could demonstrate a remarkably high rate of interfacial adsorption, whose rate and extent was dramatically affected by treatment with antibodies against SP-B and SP-C. The effect of both antibodies was additive and specific. Third, direct microscopy of an inverted air–liquid interface revealed that the blocking effect is due to a stabilization of the released particles when contacting the air–liquid interface, precluding their transformation and the formation of surface films. We conclude that SP-B and SP-C are acting as essential, preformed molecular keys in the initial stages of surfactant unpacking and surface film formation. We further propose that surfactant activation might be transduced by a conformational change of the surfactant proteins upon contact with surface forces acting on the air–liquid interface.


Item Type:Article
Uncontrolled Keywords:ARDS; Compliance, Lamellar body; Lung injury; Surface tension
Subjects:Medical sciences > Biology > Biochemistry
ID Code:43450
Deposited On:20 Jun 2017 10:30
Last Modified:20 Jun 2017 11:57

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