Effect of mycobacterial lipids on surface properties of Curosurf™: Implications for lung surfactant dysfunction in tuberculosis

Respiratory Physiology and Neurobiology

Volumn 162, Issue 1, 2008, Pages 73-79

  Chimote, G ^a   Banerjee, R ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY BOMBAY   (India)

Author keywords

Curosurf ; Lung surfactant inhibition; Pulmonary tuberculosis; Wilhelmy balance

Indexed keywords

CORD FACTOR; LIPID; LUNG SURFACTANT; MYCOLIC ACID; PORACTANT;

ADSORPTION; ARTICLE; ATELECTASIS; ATOMIC FORCE MICROSCOPY; BACTERIAL CELL WALL; IN VIVO STUDY; LUNG TUBERCULOSIS; MYCOBACTERIUM; NONHUMAN; PRIORITY JOURNAL; SURFACE PROPERTY; SURFACE TENSION;

ADJUVANTS, IMMUNOLOGIC; ANIMALS; CORD FACTORS; LIPIDS; MICROSCOPY, ATOMIC FORCE; MODELS, BIOLOGICAL; MYCOBACTERIUM; MYCOLIC ACIDS; PULMONARY SURFACTANTS; SURFACE PROPERTIES; SWINE;

EID: 44849119113     PISSN: 15699048     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.resp.2008.04.004     Document Type: Article

References (37)

1. Almong R., and Mannella C. Molecular packing of cord factor and its interactions with phosphatidylinositol in mixed monolayers. Biophys. J. 71 (1996) 3311-3319
2. Amirkhanian J.D., Bruni R., Waring A.J., Navar C., and Taeusch H.W. Full length synthetic surfactant proteins, SP-B and SP-C reduce surfactant inactivation by serum. Biochim. Biophys. Acta 1168 (1993) 315-320
3. Amrein M., Knebel D., and Haufs M.G. Structure and function of the molecular film of pulmonary surfactant at the air-alveolar interface: the role of SP-C. Lung Biol. Health Dis. 201 (2005) 301-316
4. Brennan P., and Nikaido H. The envelope of mycobacteria. Ann. Rev. Biochem. 64 (1995) 29-64
5. Chimote G., and Banerjee R. Lung surfactant dysfunction in tuberculosis: effect of mycobacterial tubercular lipids on dipalmitoylphosphatidylcholine surface activity. Colloids Surf. B 45 (2005) 215-223
6. Cho D., Narsimhan G., and Franses E.I. Interactions of spread lecithin monolayer with bovine serum albumin in aqueous solutions. Langmuir 13 (1997) 4710-4715
7. Clements J.A. Surface tension of lung extracts. Proc. Soc. Exp. Biol. Med. 95 (1957) 170-172
8. Crouch E., and Wright J. Surfactant proteins A and D and pulmonary host defense. Annu. Rev. Physiol. 63 (2001) 521-554
9. Durand E., Gillois M., Tocanne J.F., and Lanelle G. Property and activity of mycolyl esters of methyl glucoside and trehalose: effect of mitochondrial oxidative phosphorylation related to organization of suspensions and acyl-chain structure. Eur. J. Biochem. 94 (1979) 109-118
10. Enhorning G. Pulmonary surfactant function in alveoli and conducting airways. Can. Respir. J. 3 (1996) 21-27
11. Gross T., Zmora E., Levi-Kalisman Y., Regev A., and Bearman A. Lung surfactant-meconium interaction: in vitro study in bulk and at the air-solution interface. Langmuir 22 (2006) 3234-3250
12. Hall S.B., Lu R.Z., Venkitaraman A.R., Hyde R.W., and Notter R.H. Inhibition of pulmonary surfactant by oleic acid: mechanisms and characteristics. J. Appl. Physiol. 72 (1992) 1708-1716
13. Hasegawa T., and Leblanc R. Aggregation properties of mycolic acid molecules in monolayer films: a comparative study of compounds from various acid-fast bacterial species. Biochim. Biophys. Acta 1617 (2003) 89-95
14. Hasegawa T., Nishjo J., and Watanbe M. Conformational characterization of α-mycolic acid in a monolayer film by the Langmuir-Blodgett technique and atomic force microscopy. Langmuir 16 (2000) 7325-7330
15. Helenius A., and Simon K. Solubilization of membranes by detergents. Biochim. Biophys. Acta 415 (1975) 27-29
16. Holm B.A., Enhorning G., and Notter R.H. A biophysical mechanism by which plasma proteins inhibit lung surfactant activity. Chem. Phys. Lipids 49 (1988) 49-55
17. Holm B.A., and Notter R.H. Effects of haemoglobin and cell membrane lipids on pulmonary surfactant activity. J. Appl. Physiol. 63 (1987) 1434-1442
18. Holm B.A., Wang Z., and Notter R.H. Multiple mechanisms of Lung surfactant inhibition. Pediatr. Res. 46 (1999) 85-93
19. Johansson J., Curstedt T., and Robertson B. The proteins of the surfactant system. Eur. Respir. J. 7 (1994) 372-391
20. Kim S.H., and Franses E.I. Competitive adsorption of fibrinogen and dipalmitoylphosphatidylcholine at the air/aqueous interface. J. Colloid Interface Sci. 295 (2006) 84-92
21. Kolattukudy P., Fernendez N., Azad A., Fitzmaurice A., and Sirakova T. Biochemistry and molecular genetics of cell wall lipid biosynthesis in mycobacteria. Mol. Microbiol. 24 (1997) 263-270
22. Lemassu A., and Daffe M. Structural features of the exocellular polysaccharides of Mycobacterium tuberculosis. Biochem. J. 297 (1994) 351-357
23. Liau D.F., Barrett C.R., Bell A.L.L., and Ryan S.F. Functional abnormalities of lung surfactant in experimental acute alveolar injury in the dog. Am. Rev. Respir. Dis. 136 (1987) 395-401
24. Mbagwu N., Bruni R., Hernández-Juviel J.M., Waring A.J., and Walther F.J. Sensitivity of Synthetic Surfactants to Albumin Inhibition in Preterm Rabbits. Mol. Genet. Metab. 66 (1999) 40-48
25. Nag K., Hillier A., Parsons K., and Garcia M.F. Interactions of serum with lung surfactant extract in the bronchiolar and alveolar airway models. Respi. Physiol. Neurobiol. 157 (2007) 411-424
26. Notter R.H., and Wang Z. Pulmonary surfactant: physical chemistry, physiology and replacement. Revs. Chem. Eng. 13 (1997) 2-118
27. Notter R.H., Tabak S.A., and Mavis R.D. Surface properties of binary mixtures of some pulmonary surfactant components. J. Lipid Res. 21 (1980) 10-22
28. Notter R.H., Wang Z., Egan E.A., and Holm B.A. Component-specific surface and physiological activity in bovine-derived lung surfactants. Chem. Phys. Lipids 114 (2002) 21-34
29. Rachana, and Banerjee R. Interactions between hematological derivatives and dipalmitoyl phosphatidyl choline: implications for adult respiratory distress syndrome. Colloids Surf. B 34 (2004) 95-104
30. Rachana, and Banerjee R. Effects of albumin and erythrocyte membranes on spread monolayers of lung surfactant lipids. Colloids Surf. B 50 (2006) 9-17
31. Seeger W., Gunther A., and Thede C. Differential sensitivity to fibrinogen inhibition of SP-C vs. SP-B-based surfactants. Am. J. Physiol. 261 (1992) L286-L291
32. Taneva S., and Keough K.M. Pulmonary surfactant proteins SP-B and SP-C in spread monolayers at the air-water interface: I. Monolayers of pulmonary surfactant protein SP-B and phospholipids. Biophys. J. 66 (1994) 1137-1148
33. van Glode L.M.G., Batenburg J.J., and Robertson B. The pulmonary surfactant system: biochemical aspects and functional significance. Physiol. Rev. 68 (1988) 374-455
34. Villeneuve M., Kawai M., Kanashima H., Watanabe M., Minnikin D.E., and Nakahara H. Temperature dependence of the Langmuir monolayer packing of mycolic acids from Mycobacterium tuberculosis. Biochim. Biophys. Acta 1715 (2005) 71-80
35. Vroman L., and Adams A.L. Adsorption of proteins out of plasma and solutions in narrow spaces. J. Colloid Interface Sci. 111 (1986) 391-402
36. Wang Z., Schwab U., Rhoades E., Chess P., Russell D., and Notter R. Peripheral cell wall lipids of Mycobacterium tuberculosis are inhibitory to surfactant function. Tuberculosis 88 (2007) 175-186
37. Weltzein H.U. Cytolytic and membrane perturbing properties of lysophosphatidylcholine. Biochim. Biophys. Acta 559 (1979) 259-287