Skip to main content

Some NLM-NCBI services and products are experiencing heavy traffic, which may affect performance and availability. We apologize for the inconvenience and appreciate your patience. For assistance, please contact our Help Desk at info@ncbi.nlm.nih.gov.

Biophysical Journal logoLink to Biophysical Journal
. 1997 Nov;73(5):2595–2602. doi: 10.1016/S0006-3495(97)78289-4

Effect of calcium on phospholipid interaction with pulmonary surfactant protein C.

A S Dico 1, S Taneva 1, M R Morrow 1, K M Keough 1
PMCID: PMC1181162  PMID: 9370454

Abstract

Porcine pulmonary surfactant-associated protein SP-C was incorporated into bilayers of chain-perdeuterated dipalmitoylphosphatidylglycerol (DPPG-d62) and chain-perdeuterated dipalmitoyl-phosphatidylcholine (DPPC-d62) and into bilayers containing 70 mol% dipalmitoyl-phosphatidylcholine (DPPC) and 30 mol% DPPG-d62 or 70 mol% DPPC-d62 and 30 mol% dipalmitoylphosphatidylglycerol (DPPG). The effect of SP-C on the phase behavior, lipid chain order, and dynamics in these bilayers was examined by using deuterium nuclear magnetic resonance. SP-C was found to have a similar effect on the chain order and phase behavior of DPPC-d62 and DPPG-d62 in bilayers with a single lipid component. In gel phase DPPC/DPPG (7:3) bilayers with one or the other lipid component chain-perdeuterated, SP-C was found to affect first spectral moment more strongly for DPPG-d62 than for DPPC-d62. This may indicate that SP-C induced a nonrandom lateral distribution in the mixed lipid bilayer. SP-C was also found to influence motions responsible for deuteron transverse relaxation in both the gel and liquid crystalline phases. The presence of 5 mM Ca2+ in the aqueous phase substantially altered the effect of SP-C on transverse relaxation in the bilayer.

Full text

PDF
2595

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BARTLETT G. R. Phosphorus assay in column chromatography. J Biol Chem. 1959 Mar;234(3):466–468. [PubMed] [Google Scholar]
  2. Davis J. H. The description of membrane lipid conformation, order and dynamics by 2H-NMR. Biochim Biophys Acta. 1983 Mar 21;737(1):117–171. doi: 10.1016/0304-4157(83)90015-1. [DOI] [PubMed] [Google Scholar]
  3. Dico A. S., Hancock J., Morrow M. R., Stewart J., Harris S., Keough K. M. Pulmonary surfactant protein SP-B interacts similarly with dipalmitoylphosphatidylglycerol and dipalmitoylphosphatidylcholine in phosphatidylcholine/phosphatidylglycerol mixtures. Biochemistry. 1997 Apr 8;36(14):4172–4177. doi: 10.1021/bi962693v. [DOI] [PubMed] [Google Scholar]
  4. Johansson J., Curstedt T., Robertson B. The proteins of the surfactant system. Eur Respir J. 1994 Feb;7(2):372–391. doi: 10.1183/09031936.94.07020372. [DOI] [PubMed] [Google Scholar]
  5. Kahn M. C., Anderson G. J., Anyan W. R., Hall S. B. Phosphatidylcholine molecular species of calf lung surfactant. Am J Physiol. 1995 Nov;269(5 Pt 1):L567–L573. doi: 10.1152/ajplung.1995.269.5.L567. [DOI] [PubMed] [Google Scholar]
  6. Keough K. M., Kariel N. Differential scanning calorimetric studies of aqueous dispersions of phosphatidylcholines containing two polyenoic chains. Biochim Biophys Acta. 1987 Aug 7;902(1):11–18. doi: 10.1016/0005-2736(87)90130-1. [DOI] [PubMed] [Google Scholar]
  7. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  8. Morrow M. R., Davis J. H. Differential scanning calorimetry and 2H NMR studies of the phase behavior of gramicidin-phosphatidylcholine mixtures. Biochemistry. 1988 Mar 22;27(6):2024–2032. doi: 10.1021/bi00406a032. [DOI] [PubMed] [Google Scholar]
  9. Morrow M. R. Transverse nuclear spin relaxation in phosphatidylcholine bilayers containing gramicidin. Biochim Biophys Acta. 1990 Apr 13;1023(2):197–205. doi: 10.1016/0005-2736(90)90414-j. [DOI] [PubMed] [Google Scholar]
  10. Morrow M. R., Whitehead J. P. A phenomenological model for lipid-protein bilayers with critical mixing. Biochim Biophys Acta. 1988 Jun 22;941(2):271–277. doi: 10.1016/0005-2736(88)90188-5. [DOI] [PubMed] [Google Scholar]
  11. Mouritsen O. G., Bloom M. Mattress model of lipid-protein interactions in membranes. Biophys J. 1984 Aug;46(2):141–153. doi: 10.1016/S0006-3495(84)84007-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Oosterlaken-Dijksterhuis M. A., Haagsman H. P., van Golde L. M., Demel R. A. Interaction of lipid vesicles with monomolecular layers containing lung surfactant proteins SP-B or SP-C. Biochemistry. 1991 Aug 20;30(33):8276–8281. doi: 10.1021/bi00247a024. [DOI] [PubMed] [Google Scholar]
  13. Pastrana B., Mautone A. J., Mendelsohn R. Fourier transform infrared studies of secondary structure and orientation of pulmonary surfactant SP-C and its effect on the dynamic surface properties of phospholipids. Biochemistry. 1991 Oct 15;30(41):10058–10064. doi: 10.1021/bi00105a033. [DOI] [PubMed] [Google Scholar]
  14. Pauls K. P., MacKay A. L., Söderman O., Bloom M., Tanjea A. K., Hodges R. S. Dynamic properties of the backbone of an integral membrane polypeptide measured by 2H-NMR. Eur Biophys J. 1985;12(1):1–11. doi: 10.1007/BF00254089. [DOI] [PubMed] [Google Scholar]
  15. Prosser R. S., Davis J. H., Mayer C., Weisz K., Kothe G. Deuterium NMR relaxation studies of peptide-lipid interactions. Biochemistry. 1992 Oct 6;31(39):9355–9363. doi: 10.1021/bi00154a005. [DOI] [PubMed] [Google Scholar]
  16. Pérez-Gil J., Casals C., Marsh D. Interactions of hydrophobic lung surfactant proteins SP-B and SP-C with dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylglycerol bilayers studied by electron spin resonance spectroscopy. Biochemistry. 1995 Mar 28;34(12):3964–3971. doi: 10.1021/bi00012a014. [DOI] [PubMed] [Google Scholar]
  17. Pérez-Gil J., Tucker J., Simatos G., Keough K. M. Interfacial adsorption of simple lipid mixtures combined with hydrophobic surfactant protein from pig lung. Biochem Cell Biol. 1992 May;70(5):332–338. doi: 10.1139/o92-051. [DOI] [PubMed] [Google Scholar]
  18. Simatos G. A., Forward K. B., Morrow M. R., Keough K. M. Interaction between perdeuterated dimyristoylphosphatidylcholine and low molecular weight pulmonary surfactant protein SP-C. Biochemistry. 1990 Jun 19;29(24):5807–5814. doi: 10.1021/bi00476a023. [DOI] [PubMed] [Google Scholar]
  19. Taneva S. G., Keough K. M. Dynamic surface properties of pulmonary surfactant proteins SP-B and SP-C and their mixtures with dipalmitoylphosphatidylcholine. Biochemistry. 1994 Dec 13;33(49):14660–14670. doi: 10.1021/bi00253a003. [DOI] [PubMed] [Google Scholar]
  20. Udenfriend S., Stein S., Böhlen P., Dairman W., Leimgruber W., Weigele M. Fluorescamine: a reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range. Science. 1972 Nov 24;178(4063):871–872. doi: 10.1126/science.178.4063.871. [DOI] [PubMed] [Google Scholar]
  21. Vandenbussche G., Clercx A., Curstedt T., Johansson J., Jörnvall H., Ruysschaert J. M. Structure and orientation of the surfactant-associated protein C in a lipid bilayer. Eur J Biochem. 1992 Jan 15;203(1-2):201–209. doi: 10.1111/j.1432-1033.1992.tb19848.x. [DOI] [PubMed] [Google Scholar]
  22. Weaver T. E., Whitsett J. A. Function and regulation of expression of pulmonary surfactant-associated proteins. Biochem J. 1991 Jan 15;273(Pt 2):249–264. doi: 10.1042/bj2730249. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Yue J., Thewalt J. L., Cushley R. J. Deuterium nuclear magnetic resonance study of the interaction of branched chain compounds (phytanic acid, phytol) with a phospholipid model membrane. Chem Phys Lipids. 1988 Dec;49(3):205–213. doi: 10.1016/0009-3084(88)90008-4. [DOI] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES