Two Hydrophobic Protein Fractions of Ovine Pulmonary Surfactant: Isolation, Characterization, and Biophysical Activity

2001 ◽  
Vol 23 (2) ◽  
pp. 319-327 ◽  
Author(s):  
Harald Bünger ◽  
Ralph-Peter Krüger ◽  
Sylvia Pietschmann ◽  
Nadeshda Wüstneck ◽  
Lutz Kaufner ◽  
...  
Keyword(s):  
Pulmonary Surfactant ◽  
Protein Fractions ◽  
Hydrophobic Protein ◽  
Biophysical Activity

Two hydrophobic low-molecular-mass protein fractions of pulmonary surfactant. Characterization and biophysical activity

1987 ◽  
Vol 168 (2) ◽  
pp. 255-262 ◽  
Author(s):  
Tore CURSTEDT ◽  
Hans JORNVALL ◽  
Bengt ROBERTSON ◽  
Tomas BERGMAN ◽  
Per BERGGREN
Keyword(s):  
Molecular Mass ◽  
Pulmonary Surfactant ◽  
Protein Fractions ◽  
Biophysical Activity

scholarly journals Secondary structure and biophysical activity of synthetic analogues of the pulmonary surfactant polypeptide SP-C

1995 ◽  
Vol 307 (2) ◽  
pp. 535-541 ◽  
Author(s):  
J Johansson ◽  
G Nilsson ◽  
R Strömberg ◽  
B Robertson ◽  
H Jörnvall ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Pulmonary Surfactant ◽  
Transmembrane Helix ◽  
Helical Structure ◽  
Helical Conformation ◽  
Synthetic Analogues ◽  
Charged Amino Acids ◽  
Phospholipid Micelles ◽  
Helical Content ◽  
Biophysical Activity

Native pulmonary-surfactant-associated lipopolypeptide SP-C, its chemically depalmitoylated form and several synthetic analogues lacking the palmitoylcysteine residues were analysed for secondary structure in phospholipid micelles and for biophysical activity in 1,2-dipalmitoyl-sn-glycero-3- phosphocholine/phosphatidylglycerol/palmitic acid (68:22:9, by wt.). Compared with the native molecule, with the entire poly-valyl part in a known alpha-helical conformation, depalmitoylated SP-C was found to be still mainly alpha-helical, but with an approx. 20% decrease in the helical content. A synthetic hybrid polypeptide where the entire poly-valyl alpha-helical part of native SP-C had been replaced with the amino acid sequence of a transmembrane helix of bacteriorhodopsin is also predominantly alpha-helical. In contrast, synthetic SP-C analogues lacking only the palmitoyl groups, by replacement of the palmitoylcysteine residues with cysteine, phenylalanine or serine, or lacking the positively charged amino acids by replacement with alanine, are considerably less alpha-helical than both native and depalmitoylated SP-C. The data indicate that the SP-C palmitoyl groups are important for maintenance of the alpha-helical conformation in parts of the polypeptide, and that the poly-valyl alpha-helical conformation is not fully formed in synthetic SP-C polypeptides. Furthermore, the helical structure of both native and depalmitoylated SP-C in dodecylphosphocholine micelles is very resistant to thermal denaturation, exhibiting ordered structure at 90 degrees C. The alpha-helical content grossly parallels the peptide-induced acceleration of the spreading of phospholipids at an air/water interface and the increase of surface pressure. The data suggest that the alpha-helical conformation itself, rather than just the covalent structure, is of prime importance for the biological function of synthetic pulmonary-surfactant peptides.

scholarly journals Effect of Reconstituted Pulmonary Surfactant Containing the 6000-Dalton Hydrophobic Protein on Lung Compliance of Prematurely Delivered Rabbit Fetuses

1988 ◽  
Vol 23 (1) ◽  
pp. 23-30 ◽  
Author(s):  
Shou-Haw Yu ◽  
Duncan Wallace ◽  
Bhagu Bhavnani ◽  
Goran Enhorning ◽  
Paul G R Harding ◽  
...  
Keyword(s):  
Pulmonary Surfactant ◽  
Lung Compliance ◽  
Hydrophobic Protein ◽  
Rabbit Fetuses

Effect of hydrophobic protein SP-C on structure and dilatational properties of the model monolayers of pulmonary surfactant

1996 ◽  
Vol 6 (4-5) ◽  
pp. 243-260 ◽  
Author(s):  
I. Panaiotov ◽  
Tz. Ivanova ◽  
J. Proust ◽  
F. Boury ◽  
B. Denizot ◽  
...  
Keyword(s):  
Pulmonary Surfactant ◽  
Hydrophobic Protein

Inhibition of pulmonary surfactant function by phospholipases

1991 ◽  
Vol 71 (1) ◽  
pp. 317-321 ◽  
Author(s):  
B. A. Holm ◽  
L. Keicher ◽  
M. Y. Liu ◽  
J. Sokolowski ◽  
G. Enhorning
Keyword(s):  
Surface Tension ◽  
Lung Injury ◽  
Pulmonary Surfactant ◽  
Detrimental Effect ◽  
Surface Film ◽  
Intratracheal Administration ◽  
Low Concentrations ◽  
Surfactant Activity ◽  
Inhibitory Agents ◽  
Biophysical Activity

Previous studies have shown that respiratory failure associated with disorders such as acute pancreatitis correlates well with increased levels of phospholipase A2 (PLA2) in lung lavages and that intratracheal administration of PLA2 generates an acute lung injury. In addition, bacteria such as Pseudomonas have been shown to secrete phospholipase C (PLC). We studied the effects of these phospholipases on pulmonary surfactant activity using a pulsating bubble surfactometer. Concentrations greater than or equal to 0.1 unit/ml PLA2 destroyed surfactant biophysical activity, increasing surface tension at minimum bubble size from less than 1 to 15 mN/m. This surfactant inactivation was predominantly related to the effect of lysophosphatidylcholine on the surface film, although the fatty acids released with higher PLA2 concentrations also had a detrimental effect on surfactant function. Similarly, as little as 0.1 unit PLC increased the surface tension at minimal size of an oscillating bubble from less than 1 to 15 mN/m, an effect that could be mimicked by the addition of dipalmitin to surfactant in the absence of PLC. Moreover, lower, noninhibitory concentrations (0.01 unit/ml) of PLA2 and PLC increased the sensitivity of surfactant to other inhibitory agents, such as albumin. Thus, relatively low concentrations of PLC and PLA2 can cause severe breakdown of surfactant function and may contribute significantly to some forms of lung injury.

Alteration of biophysical activity of pulmonary surfactant by aluminosilicate nanoparticles

2013 ◽  
Vol 25 (2) ◽  
pp. 77-83 ◽  
Author(s):  
Dorota Kondej ◽  
Tomasz R. Sosnowski
Keyword(s):  
Pulmonary Surfactant ◽  
Biophysical Activity

scholarly journals Critical Dependence of the Biophysical Activity of Pulmonary Surfactant Films on Temperature

2010 ◽  
Vol 98 (3) ◽  
pp. 480a
Author(s):  
M. Victoria Picardi ◽  
Jesús Pérez Gil
Keyword(s):  
Pulmonary Surfactant ◽  
Biophysical Activity

l-glutamate and γ-aminobutyrate binding to hydrophobic protein fractions from leg muscle of fly (Musca domestica)

1977 ◽  
Vol 8 (2) ◽  
pp. 133-137 ◽  
Author(s):  
S. Fiszer de Plazas ◽  
E. De Robertis ◽  
G.G. Lunt
Keyword(s):  
Musca Domestica ◽  
Protein Fractions ◽  
Hydrophobic Protein ◽  
Leg Muscle

scholarly journals The relationships between biophysical activity and the secondary structure of synthetic peptides from the pulmonary surfactant protein SP-B

IUBMB Life ◽  
1996 ◽  
Vol 40 (3) ◽  
pp. 617-627
Author(s):  
Joo Hyun Kang ◽  
Myung Kyu Lee ◽  
Kil Lyong Kim ◽  
Kyung-Soo Hahm
Keyword(s):  
Secondary Structure ◽  
Synthetic Peptides ◽  
Pulmonary Surfactant ◽  
Surfactant Protein ◽  
Biophysical Activity ◽  
Pulmonary Surfactant Protein

scholarly journals Phospholipid binding and biophysical activity of pulmonary surfactant-associated protein (SAP)-35 and its non-collagenous COOH-terminal domains.

1986 ◽  
Vol 261 (30) ◽  
pp. 14283-14291 ◽  
Author(s):  
G F Ross ◽  
R H Notter ◽  
J Meuth ◽  
J A Whitsett
Keyword(s):  
Pulmonary Surfactant ◽  
Phospholipid Binding ◽  
Biophysical Activity ◽  
Terminal Domains
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