Interactions between plasma proteins and pulmonary surfactant: surface balance studies.
The influence of human fibrinogen, alpha-globulin, and albumin on the properties of monolayers of pulmonary surfactant under dynamic compression and expansion has been studied at 37 degrees 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 greater than globulin greater than 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.
Keough
K M
KM
Department of Biochemistry, Memorial University of Newfoundland, St. John's, Canada.
Parsons
C S
CS
Phang
P T
PT
Tweeddale
M G
MG
D000510:Alpha-Globulins / Q000378:metabolism; D001798:Blood Proteins / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism; D006801:Humans; D011663:Pulmonary Surfactants / Q000378:metabolism*; D012709:Serum Albumin / Q000378:metabolism; D013499:Surface Properties
D000510:Alpha-Globulins; D001798:Blood Proteins; D011663:Pulmonary Surfactants; D012709:Serum Albumin; D005340:Fibrinogen