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Journal of Lipid Research, Vol 37, 1749-1760, Copyright © 1996 by Lipid Research, Inc.
Z Wang, O Gurel, JE Baatz and RH Notter
This study shows that the hydrophobic lung surfactant proteins (SP)-B and
SP-C are not synergistic in enhancing functionally relevant surface
behaviors in films and dispersions with phospholipids, and that SP-B is
more effective than SP-C in facilitating surface activity. Purified bovine
SP-B, SP. C, or SP-B/C (1/1 by wt) were combined with chroma tographically
purified calf lung surfactant phospholipids (PPL), or with dipalmitoyl
phosphatidylcholine (DPPC) or complex phospholipid mixtures containing 75%
or 50% DPPC (75% SPL or 50% SPL). Adsorption was consistently better in
corresponding mixtures of phospholipids plus SP-B versus SP-C, but was not
improved further by substitution of SP- B/C for SP-B. Interfacial films of
DPPC or SPL plus 1.3% SP-B or 1.3% SP-C had improved respreading compared
to phospholipids alone (Wilhelmy balance, 23 degrees C and 37 degrees C),
but substitution of mixed SP- B/C for either pure apoprotein did not
increase respreading further. Surface-excess films of phospholipids plus
SP-B had higher maximum surface pressures, or maintained a high maximum
pressure through more consecutive compressions, than corresponding films
with SP-C. Dispersions of phospholipids plus 1.3% SP-B or mixed (1/1)
SP-B/C (2.6%) rapidly lowered surface tension to < 1 mN/m in oscillating
bubble studies (20 cpm, 37 degrees C), while corresponding dispersions
containing SP-C reduced surface tension more slowly or reached higher
minima. Mixtures of 50% SPL with SP-B versus SP-C were also better able to
resist inhibition by serum albumin in bubble and adsorption studies, and
inhibition resistance was not significantly improved in mixtures containing
2.6% SP-B/C (1/1) versus 1.3% SP-B. The lack of synergy in hydrophobic
apoprotein function, coupled with the greater effectiveness of SP-B in
improving phospholipid adsorption, dynamic surface activity, and inhibition
resistance, suggests that mixtures of phospholipids plus SP-B or related
peptides may be particularly relevant its clinical exogenous surfactants.
ARTICLES
Differential activity and lack of synergy of lung surfactant proteins SP-B and SP-C in interactions with phospholipids
Department of Pediatrics, University of Rochester, NY 14642, USA.
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