Removal of a dimeric form of surfactant protein C from mouse lungs: Its acceleration by reduction

Journal of Applied Physiology

Volumn 84, Issue 2, 1998, Pages 471-478

  Li, Zhong Yuan ^a   Suzuki, Yasuhiro ^a   Kurozumi, Mafumi ^a   Shen, Hui Qing ^a   Duan, Chen Xia ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

Alveolar proteinosis; Diamide; Glutathione; L buthionine (S,R) sulfoximine

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); BUTHIONINE SULFOXIMINE; DIAMIDE; DIMER; DIPALMITOYLPHOSPHATIDYLCHOLINE; GLUTATHIONE; GLUTATHIONE REDUCTASE; HEXANOIC ACID DERIVATIVE; LACTATE DEHYDROGENASE; LIPOSOME; LUNG SURFACTANT EXTRACT; PHOSPHATIDYLGLYCEROL; REDUCING AGENT;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; FEMALE; INTRAPERITONEAL DRUG ADMINISTRATION; INTRATRACHEAL DRUG ADMINISTRATION; LUNG ALVEOLUS PROTEINOSIS; LUNG CLEARANCE; LUNG HOMOGENATE; LUNG LAVAGE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; REDUCTION; SUBCUTANEOUS DRUG ADMINISTRATION;

EID: 0031940348     PISSN: 87507587     EISSN: None     Source Type: Journal    
DOI: 10.1152/jappl.1998.84.2.471     Document Type: Article

References (31)

1. Baatz, J. E., K. L. Smyth, J. A. Whitsett, C. Baxter, and D. R. Absolom. Structure and function of a dimeric form of surfactant protein SP-C: a Fourier transform infrared and surfactometry study. Chem. Phys. Lipids 63: 91-104, 1992.
2. Bartlett, G. R. Phosphorus assay in column chromatography. J. Biol. Chem. 234: 466-468, 1959.
3. Bates, S. R., M. F. Beers, and A. B. Fisher. Binding and uptake of surfactant protein B by alveolar type II cells. Am. J. Physiol. 263 (Lung Cell. Mol. Physiol. 7): L333-L341, 1992.
4. Bates, S. R., and A. B. Fisher. Degradation of surfactant protein B by alveolar type II cells. Am. J. Physiol. 265 (Lung Cell. Mol. Physiol. 9): L448-L455, 1993.
5. Creuwels, L. A. J. M., R. A. Demel, L. M. G. van Golde, and H. P. Haagsman. Characterization of a dimeric canine form of surfactant protein C (SP-C). Biochim. Biophys. Acta 1254: 326-332, 1995.
6. Curstedt, T., H. Jornvall, B. Robertson, T. Bergman, and P. Berggren. Two hydrophobic low-molecular-mass protein fractions of pulmonary surfactant. Characterization and biological activity. Eur. J. Biochem. 168: 255-262, 1987.
7. Dobbs, L. G., J. R. Wright, S. Hawgood, R. Gonzalez, K. Venstrom, and J. Nellenbogen. Pulmonary surfactant and its components inhibit secretion of phosphatidylcholine from cultured rat alveolar type II cells. Proc. Natl. Acad. Sci. USA 84: 1010-1014, 1987.
8. Folch, J., M. Lees, and G. H. Sloane Stanley. A simple method for the isolation and purification of total lipids from animal tissues. J. Biol. Chem. 226: 497-509, 1957.
9. Gilmore, L. B., F. A. Talley, and E. R. Hook. Classification and morphometric quantification of insoluble materials from the lungs of patients with alveolar proteinosis. Am. J. Pathol. 133: 252-264, 1988.
10. Goto, Y., and K. Hamaguchi. Formation of the interchain disulfide bond in the constant fragment of the immunoglobulin light chain. J. Mol. Biol. 146: 321-340, 1981.
11. Griffith, O. W. Mechanism of action, metabolism, and toxicity of buthionine sulfoximine and its higher homologs, potent inhibitors of glutathione synthesis. J. Biol. Chem. 257: 13704-13712, 1982.
12. Horowitz, A. D., J. E. Baatz, and J. A. Whitsett. Lipid effects on aggregation of pulmonary surfactant protein SP-C studied by fluorescence energy transfer. Biochemistry 32: 9513-9523, 1993.
13. Huffman, J. A., W. M. Hull, G. Dranoff, R. C. Mulligan, and J. A. Whitsett. Pulmonary epithelial cell expression of GM-CSF corrects the alveolar proteinosis in GM-CSF-deficient mice. J. Clin. Invest. 97: 649-655, 1996.
14. Ikegami, M., T. Ueda, W. Hull, J. A. Whitsett, R. C. Mulligan, G. Dranoff, and A. H. Jobe. Surfactant metabolism in transgenic mice after granulocyte macrophage-colony stimulating factor ablation. Am. J. Physiol. 270 (Lung Cell. Mol. Physiol. 14): L650-L658, 1996.
15. Pettenazzo, A., A. H. Jobe, M. Ikegami, E. Rider, S. R. Seider, and T. Yamada. Cumulative effects of repeated surfactant treatments in the rabbit. Exp. Lung Res. 16: 131-143, 1990.
16. Pinto, R. A., J. R. Wright, D. Lesikar, B. J. Benson, and J. A. Clements. Uptake of pulmonary surfactant protein C into adult rat lung lamellar bodies. J. Appl. Physiol. 74: 1005-1011, 1993.
17. Suzuki, Y. Effect of protein, cholesterol, and phosphatidylglycerol on the surface activity of the lipid protein complex reconstituted from pig pulmonary surfactant. J. Lipid Res. 23: 62-69, 1982.
18. Suzuki, Y., H. Q. Shen, A. Sato, and Y. Fujita. Characterization of surfactant apoproteins in pulmonary alveolar proteinosis. J. Jpn. Med. Soc. Biol. Interface 24: 93-98, 1993.
19. Suzuki, Y., H. Q. Shen, A. Sato, and S. Nagai. Analysis of fused-membrane structures in bronchoalveolar lavage fluid from patients with alveolar proteinosis. Am. J. Respir. Cell Mol. Biol. 12: 238-249, 1995.
20. Tenner, A. J., S. L. Robinson, J. Borchelt, and J. R. Wright. Human pulmonary surfactant protein (SP-A), a protein structurally homologous to C1q, can enhance FcR-and CR-1 mediated phagocytosis. J. Biol. Chem. 264: 13923-13928, 1989.
21. Thompson, J. F., and G. R. Morrison. Determination of organic nitrogen. Control of variables in the use of Nessler's reagent. Anal. Chem. 23: 1153-1157, 1951.
22. Tietze, F. Enzymatic method for quantitative determination of nanogram amounts of total and oxidized glutathione: application to mammalian blood and other tissues. Anal. Biochem. 27: 502-522, 1969.
23. Tomaro, M. L., J. Frydman, and R. B. Frydman. The in vivo and in vitro oxidation of molecular form 1 of biliverdin reductase to molecular form 3 by diamide. FEBS Lett. 263: 38-42, 1990.
24. Ueda, T., M. Ikegami, M. Henry, and A. H. Jobe. Clearance of surfactant protein B from rabbit lungs. Am. J. Physiol. 268 (Lung Cell. Mol. Physiol. 12): L636-L641, 1995.
25. Ueda, T., M. Ikegami, and A. H. Jobe. Clearance of surfactant protein A from rabbit lungs. Am. J. Respir. Cell Mol. Biol. 12: 89-94, 1995.
26. Voss, T., K. P. Schafer, P. F. Nielsen, A. Schafer, C. Maier, E. Hannappel, J. Maassen, B. Landis, K. Klemm, and M. Przybylski. Primary structure difference of human surfactant-associated proteins isolated from normal and proteinosis lung. Biochim. Biophys. Acta 1138: 261-267, 1992.
27. Warr, R. G., S. Hawgood, D. I. Buckley, T. M. Crisp, J. Schilling, B. J. Benson, P. L. Ballard, J. A. Clements, and R. T. White. Low molecular weight human surfactant protein (SP5): isolation, characterization, and cDNA and amino acid sequences. Proc. Natl. Acad. Sci. USA 84: 7915-7919, 1987.
28. Weber, K., and M. Osborn. The reliability of molecular weight determination by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244: 4406-4412, 1969.
29. Weibel, E. R. Morphological basis of alveolar-capillary gas exchange. Physiol. Rev. 53: 419-495, 1973.
30. Wright, J. R., and D. C. Youmans. Degradation of surfactant lipids and surfactant protein A by alveolar macrophages in vitro. Am. J. Physiol. 268 (Lung Cell. Mol. Physiol. 12): L772-L780, 1995.
31. Yu, S. H., and F. Possmayer. Role of bovine pulmonary surfactant-associated proteins in the surface-active property of phospholipid mixtures. Biochim. Biophys. Acta 1046: 233-241, 1990.