Analysis of binding and membrane destabilization of phospholipid membranes by surfactant apoprotein B

Biochimica et Biophysica Acta - Biomembranes

Volumn 1371, Issue 2, 1998, Pages 254-264

  Chang, Rupert ^a,b   Nir, Shlomo ^c   Poulain, Francis R ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c HEBREW UNIVERSITY OF JERUSALEM   (Israel)

Author keywords

Lipid protein interaction; Pulmonary surfactant; SP B; Surfactant apoprotein; Tubular myelius

Indexed keywords

APOLIPOPROTEIN B; FLUORESCENT DYE; LIPOSOME; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID; SURFACTANT;

ARTICLE; BINDING AFFINITY; FLUORESCENCE; MEMBRANE BINDING; MEMBRANE FUSION; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION;

ANIMALS; APOPROTEINS; CHICKENS; DOGS; HUMANS; LIPOSOMES; MEMBRANE FUSION; MEMBRANES, ARTIFICIAL; PHOSPHATIDYLCHOLINES; PHOSPHATIDYLGLYCEROLS; PHOSPHOLIPIDS; PROTEIN BINDING; PULMONARY SURFACTANT-ASSOCIATED PROTEINS; PULMONARY SURFACTANTS;

EID: 0001759382     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(98)00031-5     Document Type: Article

References (36)

1. Nogee M.L., DeMello D.E., Dehner L.P., Colten H.R. Brief report: deficiency of pulmonary surfactant protein B in congenital alveolar proteinosis. N. Engl. J. Med. 328:1993;406-410.
2. Clark J.C., Wert S.E., Bachurski C.J., Stahlman M.T., Stripp B.R., Weaver T.E., Whitsett J.A. Targeted disruption of the surfactant protein B gene disrupts surfactant homeostasis, causing respiratory failure in newborn mice. Proc. Natl. Acad. Sci. U.S.A. 92:1995;7794-7798.
3. Andersson M., Curstedt T., Jornvall H., Johansson J. An amphipathic helical motif common to tumourolytic polypeptide NK-lysin and pulmonary surfactant polypeptide SP-B. FEBS Lett. 362:1995;328-332.
4. Weaver T.E., Whitsett J.A. Processing of hydrophobic pulmonary surfactant protein B in rat type II cells. Am. J. Physiol. 257:1989;L100-L108.
5. Hawgood S., Latham D., Borchelt J., Damm D., White T., Benson B., Wright J.R. Cell-specific posttranslational processing of the surfactant-associated protein SP-B. Am. J. Physiol. 264:1993;L290-L299.
6. Munford R.S., Sheppard P.O., O'Hara P.J. Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure. J. Lipid Res. 36:1995;1653-1663.
7. O'Brien J.S., Kishimoto Y. Saposin proteins: structure, function, and role in human lysosomal storage disorders. FASEB J. 5:1991;301-308.
8. Leippe M., Andrä J., Nickel R., Tannich E., Müller-Eberhard H.J. Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeba histolytica: isolation, primary structure, and pore formation in bacterial cytoplasmic membranes. Mol. Microbiol. 14:1994;895-904.
9. Pena S.V., Hanson D.A., Carr B.A., Goralski T.J., Krensky A.M. Processing, subcellular localization, and function of 519 (granulysin), a human late T cell activation molecule with homology to small, lytic, granule proteins. J. Immunol. 158:1997;2680-2688.
10. Poulain F.R., Allen L., Williams M.C., Hamilton R.L., Hawgood S. Effects of surfactant apolipoproteins on liposome structure: implications for tubular myelin formation. Am. J. Physiol. 262:1992;L730-L739.
11. Poulain F.R., Nir S., Hawgood S. Kinetics of phospholipid membrane fusion induced by surfactant apoproteins A and B. Biochim. Biophys. Acta. 1278:1996;169-175.
12. Touchstone J.C., Chen J.C., Beaver K.M. Improved separation of phospholipids in thin layer chromatography. Lipids. 15:1979;61-62.
13. Warr R.G., Hawgood S., Buckley D.I., Crisp T.M., Schilling J., Benson B.J., Ballard P.L., Clements J.A., White R.T. Low molecular weight human pulmonary surfactant protein (SP5): isolation, characterization, and cDNA and amino acid sequences. Proc. Natl. Acad. Sci. U.S.A. 84:1987;7915-7919.
14. Hawgood S., Benson B.J., Schilling J., Damm D., Clements J.A., White R.T. Nucleotide and amino acid sequences of pulmonary surfactant protein SP 18 and evidence for cooperation between SP 18 and SP 28-36 in surfactant lipid adsorption. Proc. Natl. Acad. Sci. U.S.A. 84:1987;66-70.
15. Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193:1951;265-275.
16. Böhlen P., Stein S., Dairman W., Udenfriend S. Fluorometric assay of proteins in the nanogram range. Arch. Biochem. Biophys. 155:1973;213-220.
17. Rapaport D., Shai Y. Interaction of fluorescently labeled pardaxin and its analogues with lipid bilayers. J. Biol. Chem. 266:1991;23769-23775.
18. van Eijk M., De Haas C.G., Haagsman H.P. Quantitative analysis of pulmonary surfactant proteins B and C. Anal. Biochem. 232:1995;231-237.
19. Bartlett G.R. Phosphorus assay in column chromatography. J. Biol. Chem. 234:1959;466-468.
20. Frey S., Tamm L.K. Membrane insertion and lateral diffusion of fluorescence-labelled cytochrome C oxidase subunit IV signal peptide in charged and uncharged phospholipid bilayers. Biochem. J. 272:1990;713-719.
21. Rapaport D., Peled R., Nir S., Shai Y. Reversible surface aggregation in pore formation by pardaxin. Biophys. J. 70:1996;2502-2512.
22. Struck D.K., Hoekstra D., Pagano R.E. Use of resonance energy transfer to monitor membrane fusion. Biochemistry. 20:1981;4093-4099.
23. Smolarsky M., Teitelbaum D., Sela M., Gitler C. A simple fluorescent method to determine complement-mediated liposome immune lysis. J. Immunol. Meth. 15:1977;255-265.
24. Parente R.A., Nir S., Szoka F.C.J. Mechanism of leakage of phospholipid vesicle contents induced by the peptide GALA. Biochemistry. 29:1990;8720-8728.
25. Nir S., Peled R., Lee K.D. Analysis of particle uptake by cells - binding to several receptors, equilibration time, endocytosis. Colloids Surf. A - Physicochem. Eng. Aspects. 89:1994;45-57.
26. Baatz J.E., Elledge B., Whitsett J.A. Surfactant protein SP-B induces ordering at the surface of model membrane bilayers. Biochemistry. 29:1990;6714-6720.
27. Yu S.H., Possmayer F. Role of bovine pulmonary surfactant-associated proteins in the surface-active property of phospholipid mixtures. Biochim. Biophys. Acta. 1046:1990;233-241.
28. Oosterlaken-Dijksterhuis M.A., van Eijk M., van Golde L.M.G., Haagsman H.P. Lipid mixing is mediated by the hydrophobic surfactant protein SP-B but not by SP-C. Biochim. Biophys. Acta. 1110:1992;45-50.
29. Akinbi H.T., Breslin J.S., Ikegami M., Iwamoto H.S., Clark J.C., Whitsett J.A., Jobe A.H., Weaver T.E. Rescue of SP-B knockout mice with a truncated SP-B proprotein. Function of the C-terminal propeptide. J. Biol. Chem. 272:1997;9640-9647.
30. Nir S., Bentz J., Wilschut J., Duzgunes N. Aggregation and fusion of phospholipid vesicles. Prog. Surf. Sci. 13:1983;1-124.
31. S. Nir, in: J. Wilschut, D. Hoekstra (Eds.), Membrane Fusion, Vol. 1, 17th edn., Dekker, New York, 1991, pp. 127-153.
32. Suzuki Y., Fujita Y., Kogishi K. Reconstitution of tubular myelin from synthetic lipids and proteins associated with pig pulmonary surfactant. Am. Rev. Respir. Dis. 140:1989;75-81.
33. R.J. King, in: B. Robertson, L.M.G. van Golde (Eds.), Pulmonary Surfactant, Elsevier, Amsterdam, 1984, pp. 1-11.
34. Shiffer K., Hawgood S., Haagsman H.P., Benson B., Clements J.A., Goerke J. Lung surfactant proteins, SP-B and SP-C, alter the thermodynamic properties of phospholipid membranes: a differential calorimetry study. Biochemistry. 32:1993;590-597.
35. Taneva S., Keough K.M. Cholesterol modifies the properties of surface films of dipalmitoylphosphatidylcholine plus pulmonary surfactant-associated protein B or C spread or adsorbed at the air-water interface. Biochemistry. 36:1997;912-922.
36. 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. 36:1997;4172-4177.