Hot Topics in and New Strategies for Surfactant Research

Jobe, Alan H.

doi:10.1159/000047028

Cited by 8 publications

(5 citation statements)

References 32 publications

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“…Langmuir monolayers at the air-water interface provide experimentally useful model systems for studies of lung surfactants and other amphiphilic molecules. Care is necessary to extrapolate Langmuir monolayer behavior to lung surfactant behavior in vivo, but general correlations between in vitro and in vivo behavior are starting to emerge (Bernhard et al, 2000;Cochrane and Revak, 1991;Goerke, 1998;Jobe, 1998;Lipp et al, 1996Lipp et al, , 1998. The phase behavior of surfactants in two dimensions is determined by pressure-area isotherms.…”

Section: Introductionmentioning

confidence: 99%

Effects of Lung Surfactant Proteins, SP-B and SP-C, and Palmitic Acid on Monolayer Stability

Ding

Takamoto

Nahmen

et al. 2001

Biophysical Journal

168

266

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Langmuir isotherms and fluorescence and atomic force microscopy images of synthetic model lung surfactants were used to determine the influence of palmitic acid and synthetic peptides based on the surfactant-specific proteins SP-B and SP-C on the morphology and function of surfactant monolayers. Lung surfactant-specific protein SP-C and peptides based on SP-C eliminate the loss to the subphase of unsaturated lipids necessary for good adsorption and respreading by inducing a transition between monolayers and multilayers within the fluid phase domains of the monolayer. The morphology and thickness of the multilayer phase depends on the lipid composition of the monolayer and the concentration of SP-C or SP-C peptide. Lung surfactant protein SP-B and peptides based on SP-B induce a reversible folding transition at monolayer collapse that allows all components of surfactant to be retained at the interface during respreading. Supplementing Survanta, a clinically used replacement lung surfactant, with a peptide based on the first 25 amino acids of SP-B also induces a similar folding transition at monolayer collapse. Palmitic acid makes the monolayer rigid at low surface tension and fluid at high surface tension and modifies SP-C function. Identifying the function of lung surfactant proteins and lipids is essential to the rational design of replacement surfactants for treatment of respiratory distress syndrome.

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Section: Introductionmentioning

confidence: 99%

Effects of Lung Surfactant Proteins, SP-B and SP-C, and Palmitic Acid on Monolayer Stability

Ding

Takamoto

Nahmen

et al. 2001

Biophysical Journal

168

266

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“…The small hydrophobic proteins SP‐B and SP‐C are important components of the pulmonary surfactant. Thus, SP‐B deficiency causes fatal respiratory distress syndrome [4], and SP‐C deficiency in humans is associated with childhood lung disease [5,6] and fatal respiratory distress syndrome [7]. It is also of interest that the therapeutic surfactants now on the market that include SP‐B and SP‐C are regarded as more effective than those that are purely lipidic [8].…”

Section: Sequences Of Sp‐c Variants and Partial Sequences Of Human Gmentioning

confidence: 99%

Structural model for an AxxxG‐mediated dimer of surfactant‐associated protein C

Kairys

Gilson

Luy³

2004

European Journal of Biochemistry

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The pulmonary surfactant prevents alveolar collapse and is required for normal pulmonary function. One of the important components of the surfactant besides phospholipids is surfactant‐associated protein C (SP‐C). SP‐C shows complex oligomerization behavior and a transition to β‐amyloid‐like fibril structures, which are not yet fully understood. Besides this nonspecific oligomerization, MS and chemical cross‐linking data combined with CD spectra provide evidence of a specific, mainly α‐helical, dimer at low to neutral pH. Furthermore, resistance to CNBr cleavage and dual NMR resonances of porcine and human recombinant SP‐C with Met32 replaced by isoleucine point to a dimerization site located at the C‐terminus of the hydrophobic α‐helix of SP‐C, where a strictly conserved heptapeptide sequence is found. Computational docking of two SP‐C helices, described here, reveals a dimer with a helix–helix interface that strikingly resembles that of glycophorin A and is mediated by an AxxxG motif similar to the experimentally determined GxxxG pattern of glycophorin A. It is highly likely that mature SP‐C adopts such a dimeric structure in the lamellar bilayer systems found in the surfactant. Dimerization has been shown in previous studies to have a role in sorting and trafficking of SP‐C and may also be important to the surfactant function of this protein.

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“…SP-B is essential for surfactant function via direct effects of surface tension and secondary effects on surfactant protein synthesis. Normal amounts of functional SP-B are needed for biosynthesis and catabolism of SP-C [10].…”

Section: Composition Of Surfactantsmentioning

confidence: 99%

Airway proteins?surfactants

Halliday¹

2004

Pediatr. Pulmonol.

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Hot Topics in and New Strategies for Surfactant Research

Cited by 8 publications

References 32 publications

Effects of Lung Surfactant Proteins, SP-B and SP-C, and Palmitic Acid on Monolayer Stability

Effects of Lung Surfactant Proteins, SP-B and SP-C, and Palmitic Acid on Monolayer Stability

Structural model for an AxxxG‐mediated dimer of surfactant‐associated protein C

Airway proteins?surfactants

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