N-Terminally Extended Surfactant Protein (SP) C Isolated from SP-B-Deficient Children Has Reduced Surface Activity and Inhibited Lipopolysaccharide Binding†

Biochemistry ◽  
2004 ◽  
Vol 43 (13) ◽  
pp. 3891-3898 ◽  
Author(s):  
Jing Li ◽  
Machiko Ikegami ◽  
Cheng-Lun Na ◽  
Aaron Hamvas ◽  
Quentin Espinassous ◽  
...  
Keyword(s):  
Surface Activity ◽  
Surfactant Protein ◽  
Extended Surfactant ◽  
Lipopolysaccharide Binding ◽  
Reduced Surface

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.

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

A Synthetic Segment of Surfactant Protein A: Structure, in Vitro Surface Activity, and in Vivo Efficacy

1996 ◽  
Vol 39 (6) ◽  
pp. 938-946 ◽  
Author(s):  
Frans J Walther ◽  
Remedios David-Cu ◽  
Carol Leung ◽  
Roberta Bruni ◽  
José Hernández-Juviel ◽  
...  
Keyword(s):  
Surface Activity ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
In Vivo Efficacy

scholarly journals Surface Activity of Surfactant Protein SP-B and SP-C in Different Lipid Environments

2010 ◽  
Vol 98 (3) ◽  
pp. 55a-56a
Author(s):  
Olga Lucia Ospina Ramirez ◽  
Jesus Perez-Gil
Keyword(s):  
Surface Activity ◽  
Surfactant Protein

scholarly journals Surfactant protein interactions with neutral and acidic phospholipid films

2001 ◽  
Vol 281 (1) ◽  
pp. L231-L242 ◽  
Author(s):  
Karina Rodriguez-Capote ◽  
Kaushik Nag ◽  
Samuel Schürch ◽  
Fred Possmayer
Keyword(s):  
Surface Tension ◽  
Surface Activity ◽  
Protein Interactions ◽  
Film Formation ◽  
Surfactant Protein ◽  
Surfactant Proteins ◽  
Specific Interactions ◽  
Equilibrium Surface ◽  
Equilibrium Surface Tension ◽  
Lipid Adsorption

The captive bubble tensiometer was employed to study interactions of phospholipid (PL) mixtures of dipalmitoylphosphatidylcholine (DPPC) and 1-palmitoyl-2-oleoyl- sn-glycero-3-phosphocholine (POPC) or 1-palmitoyl-2-oleoyl- sn-glycero-3-[phospho- rac-(1-glycerol)] (POPG) at 50 μg/ml with physiological levels of the surfactant protein (SP) A SP-B, and SP-C alone and in combination at 37°C. All surfactant proteins enhanced lipid adsorption to equilibrium surface tension (γ), with SP-C being most effective. Kinetics were consistent with the presence of two adsorption phases. Under the conditions employed, SP-A did not affect the rate of film formation in the presence of SP-B or SP-C. Little difference in γmin was observed between the acidic POPG and the neutral POPC systems with SP-B or SP-C with and without SP-A. However, γmax was lower with the acidic POPG system during dynamic, but not during quasi-static, cycling. Considerably lower compression ratios were required to generate low γminvalues with SP-B than SP-C. DPPC-POPG-SP-B was superior to the neutral POPC-SP-B system. Although SP-A had little effect on film formation with SP-B, surface activity during compression was enhanced with both PL systems. In the presence of SP-C, lower compression ratios were required with the acidic system, and with this mixture, SP-A addition adversely affected surface activity. The results suggest specific interactions between SP-B and phosphatidylglycerol, and between SP-B and SP-A. These observations are consistent with the presence of a surface-associated surfactant reservoir which is involved in generating low γ during film compression and lipid respreading during film expansion.

scholarly journals Production and characterisation of recombinant forms of human pulmonary surfactant protein C (SP-C): Structure and surface activity

2006 ◽  
Vol 1758 (4) ◽  
pp. 509-518 ◽  
Author(s):  
Dunja Lukovic ◽  
Inés Plasencia ◽  
Francisco J. Taberner ◽  
Jesús Salgado ◽  
Juan J. Calvete ◽  
...  
Keyword(s):  
Surface Activity ◽  
Pulmonary Surfactant ◽  
Protein C ◽  
Surfactant Protein ◽  
Surfactant Protein C ◽  
Pulmonary Surfactant Protein

A mechanism of nitric oxide-induced surfactant dysfunction

1996 ◽  
Vol 80 (6) ◽  
pp. 2035-2043 ◽  
Author(s):  
M. Hallman ◽  
K. Bry ◽  
U. Lappalainen
Keyword(s):  
Nitric Oxide ◽  
Surface Activity ◽  
High Surface ◽  
Surfactant Protein ◽  
Lung Compliance ◽  
Exogenous Surfactant ◽  
Lung Edema ◽  
Natural Surfactant ◽  
Inhaled No

Inhaled nitric oxide (NO) may modify surfactant either by interacting with the surfactant complex or by changing the capacity of the proteins of the epithelial lining fluid to inhibit the surface activity. Natural surfactant was exposed to NO (80 parts/million) in air in vitro while the gas-liquid surface was cycled. In the presence or absence of oxidants (Fe2+, xanthine, xanthine oxidase), surfactant exposed to NO retained the high surface activity significantly better than control surfactants exposed to air. Two surfactant inhibitors, hemoglobin (Hb) and albumin, were separately exposed to NO. In contrast to albumin, NO-exposed Hb and methemoglobin (MetHb; 16-125 micrograms/ml) decreased the surface activity at low surfactant concentrations, whereas native Hb had no effect. Surfactant recovered by sedimentation after exposure to MetHb had decreased surface activity and contained MetHb, whereas Hb did not bind to surfactant. Acidic phospholipid phosphatidylglycerol increased the binding of MetHb to surfactant. The MetHb-induced decrease in surface activity was elicited in the presence of surfactant proteins, including a peptide mimicking surfactant protein B. MetHb (but not Hb) added to a low dose of exogenous surfactant decreased the efficacy of surfactant to improve the lung compliance of premature rabbits. We propose that inhaled NO promotes the surface activity of surfactant during tidal ventilation and that, in high-permeability lung edema and surfactant deficiency, inhaled NO increases the inhibition of surface activity by converting Hb to MetHb in the alveolar space.

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.

Sign in / Sign up

Export Citation Format

Share Document