Interaction of pulmonary surfactant protein A with dipalmitoylphosphatidylcholine and cholesterol at the air/water interface

Yu, Shi; Possmayer, Fred

doi:10.1016/s0022-2275(20)33294-6

Cited by 37 publications

(12 citation statements)

References 34 publications

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“…However, the amount of cholesterol in surfactant transferred from dispersions of BLES(chol) plus SP-A appears to be lower than in surfactant derived from BLES(chol), suggesting that SP-A could restrain the adsorption of cholesterol. Previously we have shown that SP-A interacts with the hydrophilic head groups of DPPC in DPPC spread monolayers (18). Electron microscopic studies indicate that SP-A also interacts with the head groups of DPPC in bilayers (28,29).…”

Section: Transfer Of Surfactants From Dispersions Of Bles(chol) In the Presence Of Sp-a To Clean Surfacesmentioning

confidence: 90%

“…Cholesterol exists as cholesterol-rich (DPPC-poor) and cholesterol-poor (DPPC-rich) domains in DPPC/cholesterol mixed monolayers formed by successive spreading of DPPC and cholesterol (18). Cholesterol also exists as cholesterolrich and cholesterol-poor domains in biological membranes (31).…”

Section: Transfer Of Surfactants From Dispersions Of Bles(chol) In the Presence Of Sp-a To Clean Surfacesmentioning

confidence: 99%

“…This intriguing protein has a high affinity for DPPC (15) and possesses diverse functions in the surfactant system (16,17). With respect to the biophysical functions of surfactant, SP-A interacts with the head groups of DPPC and aggregates these molecules in spread monolayers of DPPC (18). SP-A facilitates surface tension lowering of DPPC spread monolayers (18) and increases the adsorption rate of pulmonary surfactants (6).…”

mentioning

confidence: 99%

“…With respect to the biophysical functions of surfactant, SP-A interacts with the head groups of DPPC and aggregates these molecules in spread monolayers of DPPC (18). SP-A facilitates surface tension lowering of DPPC spread monolayers (18) and increases the adsorption rate of pulmonary surfactants (6). SP-A also interacts with gellike regions of spread monolayers of porcine surfactant lipid extract, resulting in reorganization of rigid-phase lipid (19).…”

mentioning

confidence: 99%

“…It is known that cholesterol preferentially interacts with DPPC over fluid PC (21). Cholesterol packs in the intermolecular cavities of DPPC (22) and cannot be squeezed out readily from DPPC/cholesterol spread monolayers during compression (18). SP-A is able to impede the interaction of cholesterol with DPPC in DPPC/SP-A/cholesterol spread monolayers and decrease the surface area reduction required to reach near zero surface tension (18).…”

mentioning

confidence: 99%

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Dipalmitoylphosphatidylcholine and cholesterol in monolayers spread from adsorbed films of pulmonary surfactant

Possmayer

2001

Journal of Lipid Research

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Pulmonary surfactant forms a surface film that consists of a monolayer and a monolayer-associated reservoir. The extent to which surfactant components including the main component, dipalmitoylphosphatidylcholine (DPPC), are adsorbed into the monolayer, and how surfactant protein SP-A affects their adsorptions, is not clear. Transport of cholesterol to the surface region from dispersions of bovine lipid extract surfactant [BLES(chol)] with or without SP-A at 37 ؇ C was studied by measuring surface radioactivities of [4-14 C]cholesterollabeled BLES(chol), and the Wilhelmy plate technique was used to monitor adsorption of monolayers. Results showed that transport of cholesterol was lipid concentration dependent. SP-A accelerated lipid adsorption but suppressed the final level of cholesterol in the surface. Surfactant adsorbed from a dispersion with or without SP-A was transferred via a wet filter paper to a clean surface, where the surface radioactivity and surface tension were recorded simultaneously. It was observed that 1) surface radioactivity was constant over a range of dispersion concentrations; 2) cholesterol and DPPC were transferred simultaneously; and 3) SP-A limited transfer of cholesterol. These results indicate that non-DPPC components of pulmonary surfactant can be adsorbed into the monolayer. Studies in the transfer of [1-14 C]DPPC-labeled BLES(chol) to an equal or larger clean surface area revealed that SP-A did not increase selective adsorption of DPPC into the monolayer. Evaluation of transferred surfactant with a surface balance indicated that it equilibrated as a monolayer. Furthermore, examination of transferred surfactants from dispersions with and without prespread BLES(chol) monolayers revealed a functional contiguous association between adsorbed monolayers and reservoirs. -Yu, S-H., and F. Possmayer. Dipalmitoylphosphatidylcholine and cholesterol in monolayers spread from adsorbed films of pulmonary surfactant.

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Section: Transfer Of Surfactants From Dispersions Of Bles(chol) In the Presence Of Sp-a To Clean Surfacesmentioning

confidence: 90%

Section: Transfer Of Surfactants From Dispersions Of Bles(chol) In the Presence Of Sp-a To Clean Surfacesmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Dipalmitoylphosphatidylcholine and cholesterol in monolayers spread from adsorbed films of pulmonary surfactant

Possmayer

2001

Journal of Lipid Research

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The pH dependent interaction between nicotine and simulated pulmonary surfactant monolayers with associated molecular modelling

Davies

Leach

Fullwood

et al. 2017

Surface & Interface Analysis

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Pulmonary surfactant is an endogenous material that lines and stabilises the alveolar air-liquid interface. Respiratory mechanics can be compromised by exposure to environmental toxins such as cigarette smoke, which contains nicotine. This study aims to determine the influence of nicotine on the activity of simulated lung surfactant at pH 7 and pH 9. In all cases, the addition of nicotine to the test zone caused deviation in surfactant film performance. Importantly, the maximum surface pressure was reduced for each system. Computational modelling was applied to assess key interactions between each species, with the GAUSSIAN 09 software platform used to calculate electrostatic potential surfaces. Modelling data confirmed either nicotine penetration into the two-dimensional structure or interfacial/electrostatic interactions across the underside. The results obtained from this study suggest that nicotine can impair the ability of pulmonary surfactant to reduce the surface tension term, which can increase the work of breathing. When extrapolated to gross lung function, alveolar collapse and respiratory disease (e.g. chronic airway obstruction) may result. The delivery of nicotine to the (deep) lung can cause a deterioration in lung function and lead to reduced quality of life.

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Structural Changes of Surfactant Protein A Induced by Cations Reorient the Protein on Lipid Bilayers

Palaniyar

Ridsdale

Holterman

et al. 1998

Journal of Structural Biology

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Interaction of pulmonary surfactant protein A with dipalmitoylphosphatidylcholine and cholesterol at the air/water interface

Cited by 37 publications

References 34 publications

Dipalmitoylphosphatidylcholine and cholesterol in monolayers spread from adsorbed films of pulmonary surfactant

Dipalmitoylphosphatidylcholine and cholesterol in monolayers spread from adsorbed films of pulmonary surfactant

The pH dependent interaction between nicotine and simulated pulmonary surfactant monolayers with associated molecular modelling

Structural Changes of Surfactant Protein A Induced by Cations Reorient the Protein on Lipid Bilayers

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