Differential activity and lack of synergy of lung surfactant proteins SP-B and SP-C in interactions with phospholipids.

Wang, Z; Gurel, Okyanus; Baatz, John E.; Notter, Robert H.

doi:10.1016/s0022-2275(20)39118-5

Cited by 74 publications

(21 citation statements)

References 50 publications

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“…Thus surfactant apoprotein composition has a more important role in generating an effective reservoir than the rate of film formation. SP-C-based reconstituted surfactants show a limited ability to attain low tensions with Wilhelmy balance and pulsating bubble studies (18,36). However, SP-C-based surfactants tended to display lower ␥ max values during quasi-static and dynamic cycling, an observation consistent with the previous reports from this and other laboratories (21,30).…”

Section: Film Compressionsupporting

confidence: 88%

Surfactant protein interactions with neutral and acidic phospholipid films

Rodríguez-Capote

Nag

Schürch

et al. 2001

American Journal of Physiology-Lung Cellular and Molecular Phys

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The captive bubble tensiometer was employed to study interactions of phospholipid (PL) mixtures of dipalmitoylphosphatidylcholine (DPPC) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) or 1-palmitoyl-2-oleoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (POPG) at 50 microg/ml with physiological levels of the surfactant protein (SP) A SP-B, and SP-C alone and in combination at 37 degrees C. All surfactant proteins enhanced lipid adsorption to equilibrium surface tension (gamma), with SP-C being most effective. Kinetics were consistent with the presence of two adsorption phases. Under the conditions employed, SP-A did not affect the rate of film formation in the presence of SP-B or SP-C. Little difference in gamma(min) was observed between the acidic POPG and the neutral POPC systems with SP-B or SP-C with and without SP-A. However, gamma(max) was lower with the acidic POPG system during dynamic, but not during quasi-static, cycling. Considerably lower compression ratios were required to generate low gamma(min) values with SP-B than SP-C. DPPC-POPG-SP-B was superior to the neutral POPC-SP-B system. Although SP-A had little effect on film formation with SP-B, surface activity during compression was enhanced with both PL systems. In the presence of SP-C, lower compression ratios were required with the acidic system, and with this mixture, SP-A addition adversely affected surface activity. The results suggest specific interactions between SP-B and phosphatidylglycerol, and between SP-B and SP-A. These observations are consistent with the presence of a surface-associated surfactant reservoir which is involved in generating low gamma during film compression and lipid respreading during film expansion.

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Section: Film Compressionsupporting

confidence: 88%

Surfactant protein interactions with neutral and acidic phospholipid films

Rodríguez-Capote

Nag

Schürch

et al. 2001

American Journal of Physiology-Lung Cellular and Molecular Phys

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“…Previous reports suggest that the effects of the combined proteins on both structure and function result mostly from SP-B. That protein has the predominant effect on adsorption (56). Induction of the Q II phases with POPE also results mostly from SP-B (57).…”

Section: Discussionmentioning

confidence: 97%

An Anionic Phospholipid Enables the Hydrophobic Surfactant Proteins to Alter Spontaneous Curvature

Chavarha

Loney

Rananavare

et al. 2013

Biophysical Journal

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The hydrophobic surfactant proteins, SP-B and SP-C, greatly accelerate the adsorption of the surfactant lipids to an air/water interface. Previous studies of factors that affect curvature suggest that vesicles may adsorb via a rate-limiting structure with prominent negative curvature, in which the hydrophilic face of the lipid leaflets is concave. To determine if SP-B and SP-C might promote adsorption by inducing negative curvature, we used small-angle x-ray scattering to test whether the physiological mixture of the two proteins affects the radius of cylindrical monolayers in the inverse hexagonal phase. With dioleoyl phosphatidylethanolamine alone, the proteins had no effect on the hexagonal lattice constant, suggesting that the proteins fail to insert into the cylindrical monolayers. The surfactant lipids also contain ∼10% anionic phospholipids, which might allow incorporation of the cationic proteins. With 10% of the anionic dioleoyl phosphatidylglycerol added to dioleoyl phosphatidylethanolamine, the proteins induced a dose-related decrease in the hexagonal lattice constant. At 30°C, the reduction reached a maximum of 8% relative to the lipids alone at ∼1% (w/w) protein. Variation of NaCl concentration tested whether the effect of the protein represented a strictly electrostatic effect that screening by electrolyte would eliminate. With concentrations up to 3 M NaCl, the dose-related change in the hexagonal lattice constant decreased but persisted. Measurements at different hydrations determined the location of the pivotal plane and proved that the change in the lattice constant produced by the proteins resulted from a shift in spontaneous curvature. These results provide the most direct evidence yet that the surfactant proteins can induce negative curvature in lipid leaflets. This finding supports the model in which the proteins promote adsorption by facilitating the formation of a negatively curved, rate-limiting structure.

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“…The current study did not attempt to address the functional importance to surface activity of the hydrophobic surfactant protein-induced effects found here in spectroscopic experiments. Both SP-B and SP-C are known to enhance the surface properties of phospholipids, but SP-B is more effective in doing so on either a weight or molar basis (Curstedt et al, 1987;Revak et al, 1988;Yu and Possmayer, 1988;Sarin et al, 1990;Oosterlaken-Dijksterhuis et al, 1991a;Oosterlaken-Dijksterhuis et al, 1991b;Seeger et al, 1992;Wang et al, 1996;Johansson et al, 1998). SP-B has been shown to be more active than SP-C in increasing both adsorption and dynamic surface tension lowering when combined with phospholipids.…”

Section: Relationship Of the Current Study To Previous Surfactant Researchmentioning

confidence: 99%

“…From the time that lung surfactant extracts were first studied at the surface of a Langmuir-Wilhelmy film balance (Clements, 1957), researchers have used insoluble, monomolecular films spread at the A/W interface as models for pulmonary surfactant (Notter, 1984;Notter, 2000). Surface balance techniques have been used to study the monolayer properties of the hydrophobic proteins SP-B and SP-C and their mixtures with lipids at the A/W interface (Oosterlaken-Dijksterhuis et al, 1991a;Taneva and Keough, 1994c;Taneva and Keough, 1994b;Taneva and Keough, 1994a;Wang et al, 1995;Wang et al, 1996). In addition, microscopic techniques such as electron (Tchoreloff et al, 1991), Brewster angle (Discher et al, 1996;Lipp et al, 1997b;Discher et al, 1999), fluorescence (Kru ¨ger et al, 1999;Ding et al, 2001;Lipp et al, 1996;Nag et al, 1996a;Nag et al, 1997;Takamoto et al, 2001), and near-field (Kramer et al, 2000), as well as scanning probe methods (Panaiotov et al, 1996;von Nahmen et al, 1997;Krol et al, 2000a) have been used to study surfactant preparations and model monomolecular films relevant for pulmonary surfactant.…”

Section: Introductionmentioning

confidence: 99%

Effect of Hydrophobic Surfactant Proteins SP-B and SP-C on Binary Phospholipid Monolayers

Brockman

Wang

Notter

et al. 2003

Biophysical Journal

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In situ external reflection infrared spectroscopy at the air-water interface was used to study the influence on phospholipid structure of an endogenous mixture of the two hydrophobic surfactant proteins, SP-B and SP-C, which are thought to play pivotal roles in the adsorption and function of pulmonary surfactant. Mixtures studied were 1:1, 2:1, and 7:1 (mol:mol) DPPC-d(62):DPPG, and 7:1 DPPC-d(62):DOPG, alone and in the presence of 0.5-10 wt % mixed SP-B/C purified chromatographically from calf lung surfactant extract. Perdeuteration of DPPC produced a shift in vibrational frequencies so that it could be differentiated spectroscopically from the phosphoglycerol component in the surface monolayer. CH(2) antisymmetric and symmetric stretching bands ( approximately 2920 and 2852 cm(-1)) along with the analogous CD(2) stretching bands ( approximately 2194 and 2089 cm(-1)) were analyzed, and band heights and peak wavenumber positions were assessed as a function of monolayer surface pressure. Small, near-physiological contents of 1-2 wt % SP-B/C typically produced the maximum observed spectroscopic effects, which were abolished at high protein contents of 10 wt %. Analysis of CH(2) and CD(2) stretching bands and C-H/C-D band height ratios indicated that SP-B/C affected PC and PG lipids differently within the surface monolayer. SP-B/C had preferential interactions with DPPG in 1:1, 2:1, and 7:1 DPPC-d(62):DPPG films that increased its acyl chain order. SP-B/C also interacted specifically with DOPG in 7:1 DPPC-d(62):DOPG monolayers, but in this case an increase in CH(2) band heights and peak wavenumber positions indicated a further disordering of the already fluid DOPG acyl chains. CD(2) band height and peak wavenumber analysis indicated that SP-B/C had no significant effect on the structure of DPPC-d(62) chains in 7:1 films with DPPG or DOPG, and had only a slight tendency to increase the acyl chain order in 1:1 films of DPPC-d(62):DPPG. SP-B/C had no significant effect on DPPC-d(62) structure in films with DOPG. Infrared results also indicated that interactions involving SP-B/C and lipids led to exclusion of PC and PG lipids from the compressed interfacial monolayer, in agreement with our previous report on the phase morphology of lipid monolayers containing 1 wt % SP-B/C.

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Differential activity and lack of synergy of lung surfactant proteins SP-B and SP-C in interactions with phospholipids.

Cited by 74 publications

References 50 publications

Surfactant protein interactions with neutral and acidic phospholipid films

Surfactant protein interactions with neutral and acidic phospholipid films

An Anionic Phospholipid Enables the Hydrophobic Surfactant Proteins to Alter Spontaneous Curvature

Effect of Hydrophobic Surfactant Proteins SP-B and SP-C on Binary Phospholipid Monolayers

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