Interactions between plasma proteins and pulmonary surfactant: surface balance studies

1988 ◽  
Vol 66 (9) ◽  
pp. 1166-1173 ◽  
Author(s):  
Kevin M. W. Keough ◽  
Caroline S. Parsons ◽  
P. Terence Phang ◽  
Martin G. Tweeddale
Keyword(s):  
Surface Tension ◽  
Plasma Proteins ◽  
Pulmonary Surfactant ◽  
Dynamic Compression ◽  
Rate Of Change ◽  
Surfactant Monolayers ◽  
Human Fibrinogen ◽  
Compression And Expansion ◽  
Minimum Surface Tension ◽  
Surfactant Lipid

The influence of human fibrinogen, α-globulin, and albumin on the properties of monolayers of pulmonary surfactant under dynamic compression and expansion has been studied at 37 °C. Each of the proteins altered some of the properties of the normal compression and expansion isotherms of surfactant such that characteristics deemed desirable for proper lung function were impaired. The order of potency of these effects was fibrinogen>globulin>albumin. The proteins (a) decreased the maximum surface pressure (equivalent to the minimum surface tension) which the surfactant monolayers attained on compression, (b) decreased the areas occupied per mole of lipid phosphorus when the monolayers were at surface tensions of 20 and 12 mN∙m−1, (c) reduced the areas of the hysteresis between compression and expansion isotherms, and (d) decreased the rate of change of surface tension with area at the point of initial expansion of the monolayers. The proteins might compete with surfactant lipid for available space at the interface, especially at low film compression. They might also enhance the desorption of lipid from the monolayer. The findings are consistent with the loss of pulmonary function and presence of edema that occur in adult respiratory distress syndrome being contributed to by plasma proteins interfering with surfactant function.

The effect of methylation of phosphatidylethanolamine on the behaviour of lipid monolayers at the air–water interface

1988 ◽  
Vol 66 (5) ◽  
pp. 405-417 ◽  
Author(s):  
K. M. W. Keough ◽  
M. W. Hawco ◽  
C. S. Parsons
Keyword(s):  
Surface Tension ◽  
Dynamic Compression ◽  
High Surface ◽  
Head Group ◽  
Surface Tensions ◽  
Minimum Surface ◽  
Ideal Mixing ◽  
Compression And Expansion ◽  
Minimum Surface Tension ◽  
Mixed Systems

Monolayers of DPPE and its N-methylated derivatives including DPPC have been investigated at 23 and 37 °C using a modified Langmuir–Wilhelmy surface balance. The monolayers have been subjected to dynamic compression and expansion, and some characteristics of the surfaces have been determined. The minimum surface tension attained by surfaces containing the lipids (maximum surface pressures sustained by the films) depended on the extent of methylation of the head group. Monolayers of DPPE or N-MeDPPE collapsed at surface tensions of 12–16 mN∙m−1, whereas those containing N,N-diMeDPPE and DPPC could be compressed to near zero surface tension. The areas per molecule occupied by these lipids under high compression varied slightly and not systematically with head-group methylation. Monolayers containing mixtures of DPPC and DPPE were also studied under the same conditions. The monolayers showed some deviation from the behaviour expected if they were to have characteristics of ideally mixed systems. The minimum surface tensions attained suggested that monolayers containing 50 mol% or more DPPC might be further enriched during compression by some selective exclusion of the DPPE. At high surface pressures, some positive deviations in nominal areas per molecule from that expected for ideal mixing were observed in the monolayers made with 50 mol% or more DPPC. These deviations might be caused by packing disruptions associated with the explosion of lipid from the films.

Effects of fixatives on function of pulmonary surfactant

2002 ◽  
Vol 93 (3) ◽  
pp. 911-916 ◽  
Author(s):  
H. Bachofen ◽  
U. Gerber ◽  
S. Schürch
Keyword(s):  
Surface Tension ◽  
Pulmonary Surfactant ◽  
Osmium Tetroxide ◽  
Uranyl Acetate ◽  
Film Stability ◽  
Minimum Surface ◽  
Natural Surfactant ◽  
Equilibrium Surface Tension ◽  
Minimum Surface Tension ◽  
Surface Active

The structure of pulmonary surfactant films remains ill defined. Although plausible film fragments have been imaged by electron microscopy, questions about the significance of the findings and even about the true fixability of surfactant films by the usual fixatives glutaraldehyde (GA), osmium tetroxide (OsO4), and uranyl acetate (UA) have not been settled. We exposed functioning natural surfactant films to fixatives within a captive bubble surfactometer and analyzed the effect of fixatives on surfactant function. The capacity of surfactant to reach near-zero minimum surface tension on film compression was barely impaired after exposure to GA or OsO4. Although neither GA nor OsO4 prevented the surfactant from forming a surface active film, GA increased the equilibrium surface tension to above 30 mN/m, and both GA and OsO4 decreased film stability as seen in the slowly rising minimum surface tension from 1 to ∼5 mN/m in 10 min. In contrast, the effect of UA seriously impaired surface activity in that both adsorption and minimum surface tension were substantially increased. In conclusion, the fixatives tested in this study are not suitable to fix, i.e., to solidify, surfactant films. Evidently, however, OsO4 and UA may serve as staining agents.

Effect of oxygen breathing at atmospheric pressure on pulmonary surfactant

1965 ◽  
Vol 20 (5) ◽  
pp. 855-858 ◽  
Author(s):  
Samuel T. Giammona ◽  
Donald Kerner ◽  
Stuart Bondurant
Keyword(s):  
Surface Tension ◽  
Atmospheric Pressure ◽  
Pulmonary Surfactant ◽  
Species Difference ◽  
Foam Fractionation ◽  
Minimum Surface ◽  
Oxygen Breathing ◽  
Minimum Surface Tension ◽  
Effect Of Oxygen

To evaluate the effects of oxygen breathing at atmospheric pressure on pulmonary surfactant, cats, rabbits, and rats were continuously kept in 98% oxygen until death occurred. Pulmonary surfactant was extracted by mincing of the lung and by foam fractionation of the lung. Surface tension of the extracts was measured on a Wilhelmy balance. Lung extracts prepared by both methods from the cats and rabbits kept in oxygen had greater surface tension than lung extracts from control animals. Surface tension of extracts prepared by foam fractionation of lungs of rats kept in oxygen did not differ from that of extracts of lungs of control rats, whereas surface tension of extracts prepared by mincing lungs of rats kept in oxygen had minimum surface tension greater than that of lung extracts of control rats. This species difference in the effects of oxygen breathing on pulmonary surfactant may reflect a difference in the pathogenesis of oxygen intoxication. oxygen intoxication; surface tension Submitted on October 19, 1964

Dipalmitoyl lecithin: studies on surface properties

1965 ◽  
Vol 20 (4) ◽  
pp. 779-781 ◽  
Author(s):  
Marian C. Kuenzig ◽  
Robert W. Hamilton ◽  
Leonard F. Peltier
Keyword(s):  
Surface Tension ◽  
Pulmonary Surfactant ◽  
Surface Film ◽  
Ethanol Solution ◽  
Original Surface ◽  
Dipalmitoyl Lecithin ◽  
Minimum Surface Tension ◽  
Humidified Air ◽  
Surface Balance ◽  
Normal Lungs

A preparation of synthetic dipalmitoyl lecithin has been devised whose activity on a Wilhelmy surface balance is similar to that of extracts from normal lungs. An ethanol solution of lecithin is precipitated with albumin, and a drop of the suspension containing approximately 0.04 mg lecithin is spread on the surface of 0.9% NaCl in the trough of the balance. This preparation appears to be insensitive to oxidation and when run under humidified air gives reproducible results. It has a low minimum surface tension (5—10 dynes/cm) when compressed to 20% of the original surface area and exhibits considerable hysteresis on re-expansion. Addition of certain lipids to the surface film produces changes similar to those caused by addition of these lipids to cat lung extracts. surface tension; surface activity; pulmonary surfactant Submitted on September 8, 1964

Mechanisms of peroxynitrite-induced injury to pulmonary surfactants

1993 ◽  
Vol 265 (6) ◽  
pp. L555-L564 ◽  
Author(s):  
I. Y. Haddad ◽  
H. Ischiropoulos ◽  
B. A. Holm ◽  
J. S. Beckman ◽  
J. R. Baker ◽  
...  
Keyword(s):  
Surface Tension ◽  
Dynamic Compression ◽  
Lung Surfactant ◽  
Thiobarbituric Acid ◽  
Surfactant Protein ◽  
Surfactant Proteins ◽  
Minimum Surface ◽  
Surfactant Protein B ◽  
Minimum Surface Tension ◽  
By Products

Activated alveolar macrophages secrete both nitric oxide and superoxide in the alveolar lining fluid which combine rapidly to form peroxynitrite, a potent oxidizing agent capable of damaging lipids and proteins in biological membranes. Peroxynitrite (1 mM) plus 100 microM Fe3+EDTA inhibited calf lung surfactant extract (CLSE) from reaching a minimum surface tension below 10 mN/m on dynamic compression. Peroxynitrite and its by-products reacted with the unsaturated lipid components of CLSE, as evidenced by the appearance of conjugated dienes and thiobarbituric acid products, and damaged all surfactant proteins. A mixture of the hydrophobic proteins [surfactant protein B (SP-B) and surfactant protein C (SP-C)] exposed to peroxynitrite became incapable of lowering phospholipid minimum surface tension on dynamic compression. Exposure of SP-A to peroxynitrite decreased its ability to cause lipid aggregation and to act synergistically with SP-B and SP-C in lowering surface tension of surfactant lipids. Western blot analysis of SP-A exposed to peroxynitrite was consistent with fragmentation and polymerization of the 28- to 36-kDa triplet band, and amino acid analysis revealed the presence of significant levels of 3-nitro-L-tyrosine. We conclude that peroxynitrite and its reactive intermediates inhibit pulmonary surfactant function by lipid peroxidation and damaging surfactant proteins.

Disparity between tidal and static volumes of immature lungs treated with reconstituted surfactants

1996 ◽  
Vol 80 (1) ◽  
pp. 62-68 ◽  
Author(s):  
T. Kobayashi ◽  
W. Z. Li ◽  
K. Tashiro ◽  
R. Takahashi ◽  
Y. Waseda ◽  
...  
Keyword(s):  
Surface Tension ◽  
Pulmonary Surfactant ◽  
Static Pressure ◽  
Surfactant Adsorption ◽  
Minimum Surface ◽  
Natural Surfactant ◽  
Minimum Surface Tension ◽  
Volume Measurements ◽  
Porcine Lungs

We biologically assessed functions of several reconstituted surfactants with the same minimum surface tension (2-3 mN/m) as “complete” porcine pulmonary surfactant (natural surfactant) but with longer surface adsorption times. Administration of natural surfactant (adsorption time 0.29 s) into the lungs of surfactant-deficient immature rabbits brought a tidal volume of 16.1 +/- 4.4 (SD) ml/kg during mechanical ventilation with 40 breaths/min and 20 cmH2O insufflation pressure. In static pressure-volume recordings, these animals showed a lung volume of 62.4 +/- 9.7 ml/kg at 30 cmH2O airway pressure and maintained 55% of this volume when the pressure decreased to 5 cmH2O. With two reconstituted surfactants consisting of synthetic lipids or isolated lipids from porcine lungs plus surfactant-associated hydrophobic proteins (adsorption times 0.57 and 0.78 s, respectively), tidal volumes were < 38% of that with natural surfactant (P < 0.05), but static pressure-volume recordings were not different. Care is therefore needed in estimating the in vivo function of surfactant preparations from minimum surface tension or static pressure-volume measurements.

Interactions between plasma proteins and pulmonary surfactant: pulsating bubble studies

1989 ◽  
Vol 67 (6) ◽  
pp. 663-668 ◽  
Author(s):  
Kevin M. W. Keough ◽  
Caroline S. Parsons ◽  
Martin G. Tweeddale
Keyword(s):  
Surface Tension ◽  
Plasma Proteins ◽  
Pulmonary Surfactant ◽  
Distress Syndrome ◽  
Adsorption Process ◽  
Human Albumin ◽  
Water Interface ◽  
Dipalmitoyl Phosphatidylcholine ◽  
Air Water Interface ◽  
Surfactant Inhibition

The influence of human albumin, α-globulin, and fibrinogen on the actions of porcine pulmonary surfactant in a pulsating bubble surfactometer has been investigated. All three proteins detracted from the ability of the surfactant to adsorb to the air–water interface. The proteins also reduced the ability of surfactant to lower the opening pressures of bubbles cycling between different sizes in suspensions of surfactant. This was equivalent to restricting the ability of the surfactant to achieve low surface tension during compression of the surface. Of the three proteins, globulin competed most effectively with surfactant during the adsorption process, and albumin competed the least effectively. The proteins also may have interfered with the processes of surface refinement, which usually yields a monolayer enriched enough in dipalmitoyl phosphatidylcholine to achieve very low surface tension (very low opening pressures in the bubbles). Of the three proteins tested, albumin was least deleterious to surface refining whereas globulin and fibrinogen appeared to be about equally detrimental to the process.Key words: pulmonary surfactant, surface tension, adsorption, adult respiratory distress syndrome, surfactant inhibition.

Inhibition of pulmonary surfactant by oleic acid: mechanisms and characteristics

1992 ◽  
Vol 72 (5) ◽  
pp. 1708-1716 ◽  
Author(s):  
S. B. Hall ◽  
R. Z. Lu ◽  
A. R. Venkitaraman ◽  
R. W. Hyde ◽  
R. H. Notter
Keyword(s):  
Surface Tension ◽  
Oleic Acid ◽  
Pulmonary Surfactant ◽  
Dynamic Compression ◽  
Molar Ratio ◽  
Surface Films ◽  
Dipalmitoyl Phosphatidylcholine ◽  
Rat Lungs ◽  
Tissue Compliance ◽  
Volume Characteristics

The inhibitory effects of oleic acid (OA) on the surface activity of pulmonary surfactant were characterized by use of the oscillating bubble surfactometer, the Wilhelmy balance, and excised rat lungs. Oscillating bubble studies showed that OA prevented lavaged calf surfactant [0.5 mM phospholipid (PL)] from lowering surface tension below 15 mN/m at or above a molar ratio of OA/PL = 0.5. In contrast to inhibition of surfactant by plasma proteins, increasing the surfactant concentration did not eliminate inhibition by oleic acid, which occurred at OA/PL greater than 0.67 on the oscillating bubble even at surfactant concentrations of 1.5 and 12 mM PL. Studies of surfactant adsorption showed that preformed films of OA had little effect on the adsorption of pulmonary surfactant. Wilhelmy balance studies showed that OA did interfere with the ability of spread films of surfactant to reach low surface tensions during dynamic compression. Further balance experiments with binary films of OA and dipalmitoyl phosphatidylcholine showed that these compounds were miscible in surface films. Together these findings suggested that OA inhibited pulmonary surfactant activity by disrupting the rigid interfacial film responsible for the generation of very low surface tension during dynamic compression. Mechanical studies in excised rat lungs showed that instillation of OA gave altered deflation pressure-volume characteristics with decreased quasi-static compliance, indicating disruption of pulmonary surfactant function in situ. This alteration of mechanics occurred without major changes in the composition of lavaged PLs or in the tissue compliance of the lungs defined by mechanical measurements during inflation-deflation with saline.(ABSTRACT TRUNCATED AT 250 WORDS)

Dependence of surfactant function on extracellular pH: mechanisms and modifications

1994 ◽  
Vol 76 (2) ◽  
pp. 657-662 ◽  
Author(s):  
I. Y. Haddad ◽  
B. A. Holm ◽  
L. Hlavaty ◽  
S. Matalon
Keyword(s):  
Surface Tension ◽  
Ph Value ◽  
Dynamic Compression ◽  
Lung Surfactant ◽  
Protein A ◽  
Lung Mechanics ◽  
Normal Lung ◽  
Surfactant Mixtures ◽  
Minimum Surface ◽  
Minimum Surface Tension

We investigated alterations in pH on the surface properties of natural lung surfactant and the calf lung surfactant extract (CLSE), suspended in 10 mM N-2-hydroxyethylpiperazine-N′-2-ethanesulfonic acid, using a pulsating bubble surfactometer. Increasing the pH value of the medium to > 7.4 decreased the ability of CLSE, but not of natural lung surfactant mixtures (2 mg phospholipid/ml), to achieve a low minimum surface tension during dynamic compression and enhanced their sensitivity to albumin inactivation. These detrimental effects on surface tension were reversed by addition of surfactant protein A (SP-A; 3% by weight) or by increasing the lipid concentration to 4 mg/ml. SP-A-induced lipid aggregation at pH 10 was not different than at pH 7.4. Alkalinization impaired the ability of CLSE to restore normal lung mechanics in excised surfactant-deficient rats lungs. These results indicate that cooperation between SP-A and the hydrophobic surfactant proteins has an important role in achieving low minimum surface tension at pH > or = 7.6.

Alterations in pulmonary surfactant after rapid arousal from torpor in the marsupial Sminthopsis crassicaudata

1999 ◽  
Vol 86 (6) ◽  
pp. 1959-1970 ◽  
Author(s):  
Olga V. Lopatko ◽  
Sandra Orgeig ◽  
David Palmer ◽  
Samuel Schürch ◽  
Christopher B. Daniels
Keyword(s):  
Surface Tension ◽  
Minimal Surface ◽  
Surface Activity ◽  
Lipid Composition ◽  
Pulmonary Surfactant ◽  
Total Phospholipid ◽  
Sminthopsis Crassicaudata ◽  
Rapid Changes ◽  
Surfactant Lipid ◽  
Surfactant Composition

Torpor in the dunnart, Sminthopsis crassicaudata, alters surfactant lipid composition and surface activity. Here we investigated changes in surfactant composition and surface activity over 1 h after rapid arousal from torpor (15–30°C at 1°C/min). We measured total phospholipid (PL), disaturated PL (DSP), and cholesterol (Chol) content of surfactant lavage and surface activity (measured at both 15 and 37°C in the captive bubble surfactometer). Immediately after arousal, Chol decreased (from 4.1 ± 0.05 to 2.8 ± 0.3 mg/g dry lung) and reached warm-active levels by 60 min after arousal. The Chol/DSP and Chol/PL ratios both decreased to warm-active levels 5 min after arousal because PL, DSP, and the DSP/PL ratio remained elevated over the 60 min after arousal. Minimal surface tension and film compressibility at 17 mN/m at 37°C both decreased 5 min after arousal, correlating with rapid changes in surfactant Chol. Therefore, changes in lipids matched changes in surface activity during the postarousal period.

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