Lipid composition greatly affects the in vitro surface activity of lung surfactant protein mimics

2007 ◽  
Vol 57 (1) ◽  
pp. 37-55 ◽  
Author(s):  
Shannon L. Seurynck-Servoss ◽  
Nathan J. Brown ◽  
Michelle T. Dohm ◽  
Cindy W. Wu ◽  
Annelise E. Barron
Keyword(s):  
Surface Activity ◽  
Lipid Composition ◽  
Lung Surfactant ◽  
Surfactant Protein ◽  
Protein Mimics ◽  
Lung Surfactant Protein

Interaction of transferrin saturated with iron with lung surfactant in respiratory failure

1994 ◽  
Vol 77 (2) ◽  
pp. 757-766 ◽  
Author(s):  
M. Hallman ◽  
A. Sarnesto ◽  
K. Bry
Keyword(s):  
Respiratory Failure ◽  
Surface Activity ◽  
Lung Surfactant ◽  
Protein A ◽  
Surfactant Protein ◽  
Lung Damage ◽  
Epithelial Lining ◽  
Surface Absorption ◽  
Epithelial Lining Fluid

Proteins that decrease the surface activity of surfactant accumulate in epithelial lining fluid in respiratory failure. The aim of this study was to isolate a surfactant inhibitor from the airways of rabbits in acute respiratory failure induced by bronchoalveolar lavage (BAL). This inhibitor was identified as being transferrin (TF). Unlike serum TF, TF recovered in respiratory failure was saturated with iron (Fe(3+)-TF). Fe(3+)-TF decreased the surface activity of normal surfactant in vitro, whereas iron-free TF had no effect. In the presence of H2O2 and a reducing agent, Fe(+3)-TF inactivated the surfactant complex: the surface absorption rate was decreased, immunoreactive surfactant protein A was decreased, and malondialdehyde was formed. The acute effects of Fe(3+)-TF and iron-free TF applied to the airways were studied in animal models. In respiratory failure induced by BAL, Fe(3+)-TF deteriorated respiratory failure, whereas iron-free TF had no effect. In respiratory failure induced by hyperoxia for 48 h, administration of iron-free TF ameliorated the respiratory failure and improved the surface activity in BAL. We propose that Fe(3+)-TF accumulating in epithelial lining fluid during lung damage contributes to surfactant inhibition and promotes the formation of free radicals that inactivate the surfactant system.

Membrane Activity of (Cys48Ser) Lung Surfactant Protein B Increases with Dimerisation

2001 ◽  
Vol 382 (6) ◽  
pp. 933-939 ◽  
Author(s):  
Shahparak Zaltash ◽  
William J. Griffiths ◽  
David Beck ◽  
Chen-Xia Duan ◽  
Timothy E. Weaver ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Transgenic Mice ◽  
Ion Pairs ◽  
Lung Surfactant ◽  
Surfactant Protein ◽  
Cd Spectroscopy ◽  
Surfactant Protein B ◽  
Lung Surfactant Protein ◽  
Protein B

Abstract One of the possible functions of lung surfactant protein B (SPB), an hydrophobic membraneassociated saposinlike protein, is to reduce the alveolar surface tension by promoting insertion of phospholipids into the air/liquid interface of the lung. SPB is a covalent homodimer; Cys48 of two polypeptides form an intermolecular disulphide bond. In order to test whether dimerisation of SPB is important for surfactant function, transgenic mice which express (Cys48Ser) human SPB in a mouse SPB null background were generated. In previous studies (Cys48Ser)SPB showed a concentrationdependent in vitro activity, suggesting that it may form noncovalent dimers. Here (Cys48Ser)SPB isolated from bronchoalveolar lavage of transgenic mice was studied at different concentrations by circular dichroism (CD) spectroscopy, pulsating bubble surfactometry, mass spectrometry and reversedphase HPLC. The results indicate that (Cys48Ser)SPB, both in a phospholipid environment and in organic solvents, is largely monomeric and exhibits low activity at concentrations lower than 1 2 M, while at higher concentrations it forms noncovalent dimers, which are nearly functionally equivalent to native SPB in vitro. Furthermore, electrospray mass spectrometry showed that more dimers were found relative to the monomer when the polarity of the solvent was decreased, and when the concentration of SPB increased. (Cys48Ser)SPB also eluted earlier than native SPB in reversedphase HPLC. Taken together, these results indicate that a polar surface is buried upon dimerisation, thereby promoting formation of interchain ion pairs between Glu51 Arg52 and Glu51Arg52.

Content-dependent activity of lung surfactant protein B in mixtures with lipids

2002 ◽  
Vol 283 (5) ◽  
pp. L897-L906 ◽  
Author(s):  
Z. Wang ◽  
J. E. Baatz ◽  
B. A. Holm ◽  
R. H. Notter
Keyword(s):  
Surface Activity ◽  
Physiological Activity ◽  
Lung Surfactant ◽  
Dynamic Surface Tension ◽  
Surfactant Protein ◽  
Surface Tensions ◽  
Dynamic Surface ◽  
Minimum Surface ◽  
Dependent Activity ◽  
Lung Surfactant Protein

The content-dependent activity of surfactant protein (SP)-B was studied in mixtures with dipalmitoyl phosphatidylcholine (DPPC), synthetic lipids (SL), and purified phospholipids (PPL) from calf lung surfactant extract (CLSE). At fixed SP-B content, adsorption and dynamic surface tension lowering were ordered as PPL/SP-B ≈ SL/SP-B > DPPC/SP-B. All mixtures were similar in having increased surface activity as SP-B content was incrementally raised from 0.05 to 0.75% by weight. SP-B had small but measurable effects on interfacial properties even at very low levels ≤0.1% by weight. PPL/SP-B (0.75%) had the highest adsorption and dynamic surface activity, approaching the behavior of CLSE. All mixtures containing 0.75% SP-B reached minimum surface tensions <1 mN/m in pulsating bubble studies at low phospholipid concentration (1 mg/ml). Mixtures of PPL or SL with SP-B (0.5%) also had minimum surface tensions <1 mN/m at 1 mg/ml, whereas DPPC/SP-B (0.5%) reached <1 mN/m at 2.5 mg/ml. Physiological activity also was strongly dependent on SP-B content. The ability of instilled SL/SP-B mixtures to improve surfactant-deficient pressure-volume mechanics in excised lavaged rat lungs increased as SP-B content was raised from 0.1 to 0.75% by weight. This study emphasizes the crucial functional activity of SP-B in lung surfactants. Significant differences in SP-B content between exogenous surfactants used to treat respiratory disease could be associated with substantial activity variations.

Donor lung surfactant protein gene expression predicts early and long-term outcome

2005 ◽  
Vol 24 (2) ◽  
pp. S99-S100
Author(s):  
F. D’Ovidio ◽  
H. Kaneda ◽  
C. Andrade ◽  
M. Mura ◽  
H. Takahashi ◽  
...  
Keyword(s):  
Gene Expression ◽  
Protein Gene ◽  
Lung Surfactant ◽  
Surfactant Protein ◽  
Term Outcome ◽  
Long Term Outcome ◽  
Donor Lung ◽  
Lung Surfactant Protein

scholarly journals Porcine Lung Surfactant Protein D: Complementary DNA Cloning, Chromosomal Localization, and Tissue Distribution

2000 ◽  
Vol 164 (3) ◽  
pp. 1442-1450 ◽  
Author(s):  
Martin van Eijk ◽  
Henk P. Haagsman ◽  
Thomas Skinner ◽  
Alan Archibold ◽  
Kenneth B. M. Reid ◽  
...  
Keyword(s):  
Tissue Distribution ◽  
Chromosomal Localization ◽  
Lung Surfactant ◽  
Surfactant Protein ◽  
Surfactant Protein D ◽  
Dna Cloning ◽  
Complementary Dna ◽  
Complementary Dna Cloning ◽  
Lung Surfactant Protein

Studies of the structure of lung surfactant protein SP-A

1989 ◽  
Vol 257 (6) ◽  
pp. L421-L429 ◽  
Author(s):  
H. P. Haagsman ◽  
R. T. White ◽  
J. Schilling ◽  
K. Lau ◽  
B. J. Benson ◽  
...  
Keyword(s):  
Pulmonary Surfactant ◽  
Triple Helix ◽  
Lung Surfactant ◽  
Surfactant Protein ◽  
Gene Encoding ◽  
Protein Subunits ◽  
Terminal Domain ◽  
Human Lungs ◽  
Fibroblast Line ◽  
Lung Surfactant Protein

SP-A, a glycoprotein of pulmonary surfactant, consists of an NH2-terminal domain containing a collagen-like sequence and a COOH-terminal domain with sequence homology to several Ca2(+)-dependent lectins. We have compared the size, thermal stability, and secondary structure of recombinant SP-A, the product of a fibroblast line transfected with a single human gene encoding SP-A, with natural SP-A isolated from canine and human lungs. Our results suggest both recombinant and natural SP-A are assembled as large oligomers. More variability in the degree of oligomerization was observed with recombinant human SP-A than with natural canine SP-A. As shown by collagenase digestion, the full assembly of protein subunits was dependent on an intact collagen-like domain. The cysteines in the noncollagen domain of SP-A form intrachain bonds between residues 135-226 and 204-218. The circular dichroism spectra of both recombinant and natural SP-A were consistent with the presence of a collagen-like triple helix. As determined by the change in ellipticity at 205 nm, the thermal transition temperatures of canine, natural human, and recombinant SP-A were 51.5, 52.3, and 42.0 degrees C, respectively. These results suggest differences in the assembly and stability of the natural and recombinant proteins.

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