Characterization of lipid insertion into monomolecular layers mediated by lung surfactant proteins SP-B and SP-C

Biochemistry ◽  
1991 ◽  
Vol 30 (45) ◽  
pp. 10965-10971 ◽  
Author(s):  
Marja A. Oosterlaken-Dijksterhuis ◽  
Henk P. Haagsman ◽  
Lambert M. G. Van Golde ◽  
Rudy A. Demel
Keyword(s):  
Lung Surfactant ◽  
Surfactant Proteins ◽  
Monomolecular Layers

Interaction of lipid vesicles with monomolecular layers containing lung surfactant proteins SP-B or SP-C

Biochemistry ◽  
1991 ◽  
Vol 30 (33) ◽  
pp. 8276-8281 ◽  
Author(s):  
Marja A. Oosterlaken-Dijksterhuis ◽  
Henk P. Haagsman ◽  
Lambert M. G. Van Golde ◽  
Rudy A. Demel
Keyword(s):  
Lung Surfactant ◽  
Lipid Vesicles ◽  
Surfactant Proteins ◽  
Monomolecular Layers

Effects of Keratin and Lung Surfactant Proteins on the Surface Activity of Meibomian Lipids

2013 ◽  
Vol 54 (4) ◽  
pp. 2571 ◽  
Author(s):  
Chendur K. Palaniappan ◽  
Burkhardt S. Schütt ◽  
Lars Bräuer ◽  
Martin Schicht ◽  
Thomas J. Millar
Keyword(s):  
Surface Activity ◽  
Lung Surfactant ◽  
Surfactant Proteins

Strategies for analysis of gene expression: pulmonary surfactant proteins

1990 ◽  
Vol 259 (4) ◽  
pp. L185-L197
Author(s):  
B. R. Stripp ◽  
J. A. Whitsett ◽  
D. L. Lattier
Keyword(s):  
Gene Expression ◽  
Dna Sequences ◽  
Pulmonary Surfactant ◽  
Transcriptional Control ◽  
Lung Surfactant ◽  
Surfactant Protein ◽  
Biologically Active ◽  
Surfactant Proteins ◽  
Regulatory Sequences ◽  
Control Mechanisms

Gene transcription is regulated by the formation of protein-DNA complexes that influence the rate of specific initiation of transcription by RNA polymerase. Recent experimental advances allowing the identification of cis regulatory sequences that specify the binding of trans acting protein factors have made significant contributions to our understanding of the mechanistic complexities of transcriptional regulation. These methodologies have prompted the use of similar strategies to elucidate transcriptional control mechanisms involved in the tissue specific and developmental regulation of pulmonary surfactant protein gene expression. The purpose of this review is to describe various methodologies by which molecular biologists identify and subsequently assay regions of nucleic acids presumed to be integral in gene regulation at the level of transcription. It is well established that genes encoding surfactant proteins are subject to regulation by hormones, cytokines, and a variety of biologically active reagents. Perhaps future studies utilizing molecular tools outlined in this review will be valuable in identification of DNA sequences and protein factors required for the regulation of lung surfactant genes.

Physicochemical Characterization of Tetraetherlipids from Thermoplasma acidophilum

1985 ◽  
Vol 40 (9-10) ◽  
pp. 606-611 ◽  
Author(s):  
Detlef Blöcher ◽  
Raymund Gutermann ◽  
Birgit Henkel ◽  
Klaus Ring
Keyword(s):  
Physicochemical Characterization ◽  
Thermoplasma Acidophilum ◽  
Transition Range ◽  
Maximum Heat ◽  
Dipalmitoyl Phosphatidylcholine ◽  
Excess Water ◽  
Tetraether Lipid ◽  
High Proton ◽  
Monomolecular Layers

Abstract By means of differential thermoanalysis, the miscibility of the main polar tetraether lipid of Thermoplasma acidophilum with two ester lipids, dipalmitoyl phosphatidylcholine and dipalmitoyl phosphatidylglycerol, resp., in the presence of excess water was studied. It is shown that with increasing fraction of tetraether lipid in the mixture, the transition range of dipalmitoyl phosphatidylcholine is broadened and the temperature of the maximum heat flow (Tm) is shifted to lower temperatures; furthermore, the enthaply change (ΔH) of the transition declines. Similar results were obtained with mixtures of tetraether lipid with dipalmitoyl phosphatidylglycerol. It is therefore concluded that the main polar tetraether lipid of Thermoplasma acidophilum , which essentially forms monomolecular layers, is able to form stable common phases with bilayer-forming ester lipids. Miscibility of the tetraether lipid with dipalmitoyl phosphatidylglycerol, which are both monovalent anions at neutral pH, is also observed in the presence of high proton or calcium ion concentrations.

Deficiencies in Lung Surfactant Proteins A and D Are Associated with Lung Infection in Very Premature Neonatal Baboons

2001 ◽  
Vol 163 (2) ◽  
pp. 389-397 ◽  
Author(s):  
SHANJANA AWASTHI ◽  
JACQUELINE J. COALSON ◽  
BRADLEY A. YODER ◽  
ERIKA CROUCH ◽  
RICHARD J. KING
Keyword(s):  
Lung Surfactant ◽  
Lung Infection ◽  
Surfactant Proteins

Lung surfactant proteins involved in innate immunity

1999 ◽  
Vol 11 (1) ◽  
pp. 28-33 ◽  
Author(s):  
Paul Eggleton ◽  
Kenneth BM Reid
Keyword(s):  
Innate Immunity ◽  
Lung Surfactant ◽  
Surfactant Proteins

scholarly journals Expression of hydrophilic surfactant proteins by mesentery cells in rat and man

1997 ◽  
Vol 328 (1) ◽  
pp. 251-256 ◽  
Author(s):  
Bernadette CHAILLEY-HEU ◽  
Sandrine RUBIO ◽  
Jean-Philippe ROUGIER ◽  
Robert DUCROC ◽  
Anne-Marie BARLIER-MUR ◽  
...  
Keyword(s):  
Lung Surfactant ◽  
Surfactant Protein ◽  
Mesothelial Cells ◽  
Surfactant Proteins ◽  
Two Dimensional ◽  
Western Blots ◽  
Mrna Species ◽  
Visceral Peritoneum ◽  
Rat Mesentery

Human peritoneal dialysis effluent (PDE) contains a phosphatidylcholine-rich compound similar to the surfactant that lines lung alveoli. This material is secreted by mesothelial cells. Lung surfactant is also characterized by four proteins essential to its function. After having long been considered as lung-specific, some of them have been found in gastric and intestinal epithelial cells. To explore further the similarity between lung and peritoneal surfactants, we investigated whether mesothelial cells also produce surfactant proteins. We used rat transparent mesentery, human visceral peritoneum biopsies and PDE. Surfactant proteins were searched for after one- and two-dimensional SDS/PAGE and Western blotting. On a one-dimensional Western blot, bands at 38 and 66 kDa in rat mesentery, and at 38 and 66 kDa in human peritoneal mesothelial cells (in vivo and in vitro) and PDE, corresponded to monomeric and dimeric forms of lung surfactant protein A (SP-A). On two-dimensional Western blots, the 32 and 38 kDa spots in mesentery and PDE localized at the acidic pH appropriate to the SP-A monomer's isoelectric point. SP-D was also identified at the same 43 kDa molecular mass as in lung. SP-B was not detected in mesenteric samples. Expression of SP mRNA species was also assessed by reverse transcriptase-PCR, which was performed with specific primers of surfactant protein cDNA sequences. With primers of SP-A and SP-D, DNA fragments of the same size were amplified in lung and mesentery, indicating the presence of SP-A and SP-D mRNA species. These fragments were labelled by appropriate probes in a Southern blot. No amplification was obtained for SP-B. These results show that mesentery cells produce SP-A and SP-D, although they are of embryonic origin (mesodermal) and are different from those of the lung and digestive tract (endodermal) that secrete these surfactants.

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