Formation and structure of surface films: captive bubble surfactometry

Schürch, Samuel; Green, Francis H. Y.; Bachofen, H

doi:10.1016/s0925-4439(98)00067-2

Cited by 242 publications

(267 citation statements)

References 40 publications

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“…Compressibility at ␥ 20 (C 20 ) was 0.078 Ϯ 0.020. As reported previously, control BLES adsorbed at 50 g/ml required ϳ60% surface area reduction to lower ␥ from equilibrium (23 mN/m) to near zero during the first compression (16,35,42).…”

Section: Fig 4 Typical Negative Electrospray Ion Mass Spectra For Asupporting

confidence: 79%

“…After (␥ eq , mN/m) was attained, the chamber was sealed, and quasi-static or dynamic compression-expansion cycles were performed. Changes in bubble area were recorded during each individual experiment and the bubble shapes analyzed using custom designed software to calculate the surface tension of the film (34,35).…”

Section: Methodsmentioning

confidence: 99%

“…Effect of Free Radical Exposure on Surfactant Function-The effects of free radical exposure on surfactant function were studied with the CBT (16,35). With this apparatus, the ability of a surfactant to adsorb to the interface is assessed, after which surface area compression-expansion isotherms are performed, either quasi-statically or dynamically, to evaluate the surface properties of the sample under conditions that mimic…”

Section: Effect Of Free Radical Exposure On Surfactantmentioning

confidence: 99%

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Pulmonary Surfactant Protein-A (SP-A) Restores the Surface Properties of Surfactant after Oxidation by a Mechanism That Requires the Cys6 Interchain Disulfide Bond and the Phospholipid Binding Domain

Rodríguez-Capote

McCormack

Possmayer

2003

Journal of Biological Chemistry

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Reactive oxygen species produced by activated leukocytes in the alveolar epithelial lining fluid have been implicated in the inactivation of pulmonary surfactant and the impairment of lung function. Oxidation of bovine lipid extract surfactant (BLES), a therapeutic surfactant, with hypochlorous acid (H-BLES) or the Fenton reaction (F-BLES) led to temporary increases in conjugated dienes and formation of malondialdehyde and 4-hydroxy-2-nonenal. Electrospray ionization mass spectrometry revealed the appearance of lipid hydroperoxides, peroxides, lysophospholipids, and free fatty acids. Captive bubble tensiometer studies of H-BLES demonstrated prolonged adsorption times, film instability at low surface tensions during film compression, and reduced respreadability during film expansion. F-BLES exhibited prolonged adsorption times, a marked effect on increasing compressibility during compression, and a lesser effect on reducing respreadability on expansion. Addition of native bovine or rat surfactant-associated protein A (SP-A) reversed the effects of oxidation on surfactant biophysical properties. Studies using mutant recombinant rat SP-As indicated that an intact carbohydrate recognition domain and disulfide-dependent oligomeric assembly are critical for these effects, but the collagen-like region is not required. We conclude that SP-A can reverse the detrimental effects of surfactant oxidation on the biophysical properties of surfactant, by a mechanism that is dependent on interchain disulfide bond formation and the Cterminal domains of the protein.

show abstract

Section: Fig 4 Typical Negative Electrospray Ion Mass Spectra For Asupporting

confidence: 79%

Section: Methodsmentioning

confidence: 99%

Section: Effect Of Free Radical Exposure On Surfactantmentioning

confidence: 99%

See 1 more Smart Citation

Pulmonary Surfactant Protein-A (SP-A) Restores the Surface Properties of Surfactant after Oxidation by a Mechanism That Requires the Cys6 Interchain Disulfide Bond and the Phospholipid Binding Domain

Rodríguez-Capote

McCormack

Possmayer

2003

Journal of Biological Chemistry

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“…Ultrastructural analysis of surfactant films in vitro demonstrates the presence of both monolayers and multilayers of phospholipids, the latter being evident when surfactant films are highly compressed (23). Analysis of the alveolar surfactant film structure by electron microscopy demonstrates that the surface film contains regions of multilamellar stacks in vivo that are similar to those found in vitro (24). We hypothesize that SP-C may stabilize adjacent lipid layers that form during film compression and promote formation of surfactant reservoirs that maintain availability of phospholipids for surface tension reduction at the air-liquid interface.…”

Section: Discussionmentioning

confidence: 53%

Altered stability of pulmonary surfactant in SP-C-deficient mice

Glasser

Burhans

Korfhagen

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

266

192

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“…Surfactant protein B is important for the formation of the active surfactant surface film (Schürch et al, 1998) and is essential for normal lung function (Robertson et al, 1991). Surfactant protein B knock out mice show disruption of surfactant film and function and die from respiratory failure (Clark et al, 1995(Clark et al, , 1997.…”

mentioning

confidence: 99%

Surfactant protein B gene variations enhance susceptibility to squamous cell carcinoma of the lung in German patients

Seifart

Plagens

et al. 2002

Br J Cancer

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Genetic factors are thought to influence the risk for lung cancer. Since pulmonary surfactant mediates the response to inhaled carcinogenic substances, candidate genes may be among those coding for pulmonary surfactant proteins. In the present matched case -control study a polymorphism within intron 4 of the gene coding for surfactant specific protein B was analysed in 357 individuals. They were divided into 117 patients with lung cancer (40 patients with small cell lung cancer, 77 patients with non small cell lung cancer), matched controls and 123 healthy individuals. Surfactant protein B gene variants were analysed using specific PCR and cloned surfactant protein B sequences as controls. The frequency of the intron 4 variation was similar in both control groups (13.0% and 9.4%), whereas it was increased in the small cell lung cancer group (17.5%) and the non small cell lung cancer group (16.9%). The gene variation was found significantly more frequently in patients with squamous cell carcinoma (25.0%, P=0.016, odds ratio=3.2, 95%CI=1.24 -8.28) than in the controls. These results indicate an association of the surfactant protein B intron 4 variants and/or its flanking loci with mechanisms that may enhance lung cancer susceptibility, especially to squamous cell carcinoma of the lung.

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Formation and structure of surface films: captive bubble surfactometry

Cited by 242 publications

References 40 publications

Pulmonary Surfactant Protein-A (SP-A) Restores the Surface Properties of Surfactant after Oxidation by a Mechanism That Requires the Cys6 Interchain Disulfide Bond and the Phospholipid Binding Domain

Pulmonary Surfactant Protein-A (SP-A) Restores the Surface Properties of Surfactant after Oxidation by a Mechanism That Requires the Cys6 Interchain Disulfide Bond and the Phospholipid Binding Domain

Altered stability of pulmonary surfactant in SP-C-deficient mice

Surfactant protein B gene variations enhance susceptibility to squamous cell carcinoma of the lung in German patients

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