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

Surface activity of a synthetic lung surfactant containing a phospholipase-resistant phosphonolipid analog of dipalmitoyl phosphatidylcholine

2003 ◽  
Vol 285 (3) ◽  
pp. L550-L559 ◽  
Author(s):  
Z. Wang ◽  
A. L. Schwan ◽  
L. L. Lairson ◽  
J. S. O'Donnell ◽  
G. F. Byrne ◽  
...  
Keyword(s):  
Serum Albumin ◽  
Surface Activity ◽  
Dynamic Compression ◽  
Lung Surfactant ◽  
Dynamic Surface Tension ◽  
Surfactant Proteins ◽  
Chemical Degradation ◽  
Dynamic Surface ◽  
Dipalmitoyl Phosphatidylcholine ◽  
Surfactant Dysfunction

Surface activity and sensitivity to inhibition from phospholipase A2 (PLA2), lysophosphatidylcholine (LPC), and serum albumin were studied for a synthetic C16:0 diether phosphonolipid (DEPN-8) combined with 1.5% by weight of mixed hydrophobic surfactant proteins (SP)-B/C purified from calf lung surfactant extract (CLSE). Pure DEPN-8 had better adsorption and film respreading than the major lung surfactant phospholipid dipalmitoyl phosphatidylcholine and reached minimum surface tensions <1 mN/m under dynamic compression on the Wilhelmy balance and on a pulsating bubble surfactometer (37°C, 20 cycles/min, 50% area compression). DEPN-8 + 1.5% SP-B/C exhibited even greater adsorption and had overall dynamic surface tension lowering equal to CLSE on the bubble. In addition, films of DEPN-8 + 1.5% SP-B/C on the Wilhelmy balance had better respreading than CLSE after seven (but not two) cycles of compression-expansion at 23°C. DEPN-8 is structurally resistant to degradation by PLA2, and DEPN-8 + 1.5% SP-B/C maintained high adsorption and dynamic surface activity in the presence of this enzyme. Incubation of CLSE with PLA2 led to chemical degradation, generation of LPC, and reduced surface activity. DEPN-8 + 1.5% SP-B/C was also more resistant than CLSE to direct biophysical inhibition by LPC, and the two were similar in their sensitivity to biophysical inhibition by serum albumin. These findings indicate that synthetic surfactants containing DEPN-8 combined with surfactant proteins or related synthetic peptides have potential utility for treating surfactant dysfunction in inflammatory lung injury.

High-Yield Purification of Lung Surfactant Proteins SP-B and SP-C and the Effects on Surface Activity

2001 ◽  
Vol 23 (1) ◽  
pp. 180-190 ◽  
Author(s):  
John E. Baatz ◽  
Yong Zou ◽  
J.Thomas Cox ◽  
Zhengdong Wang ◽  
Robert H. Notter
Keyword(s):  
Surface Activity ◽  
Lung Surfactant ◽  
Surfactant Proteins ◽  
High Yield

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

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.

Alterations in the surface properties of lung surfactant in the torpid marsupial Sminthopsis crassicaudata

1998 ◽  
Vol 84 (1) ◽  
pp. 146-156 ◽  
Author(s):  
Olga V. Lopatko ◽  
Sandra Orgeig ◽  
Christopher B. Daniels ◽  
David Palmer
Keyword(s):  
Surface Tension ◽  
Surface Properties ◽  
Surface Activity ◽  
Pulmonary Surfactant ◽  
Lung Surfactant ◽  
Lung Compliance ◽  
Equilibrium Surface Tension ◽  
Sminthopsis Crassicaudata

Lopatko, Olga V., Sandra Orgeig, Christopher B. Daniels, and David Palmer. Alterations in the surface properties of lung surfactant in the torpid marsupial Sminthopsis crassicaudata. J. Appl. Physiol. 84(1): 146–156, 1998.—Torpor changes the composition of pulmonary surfactant (PS) in the dunnart Sminthopsis crassicaudata [C. Langman, S. Orgeig, and C. B. Daniels. Am. J. Physiol. 271 ( Regulatory Integrative Comp. Physiol. 40): R437–R445, 1996]. Here we investigated the surface activity of PS in vitro. Five micrograms of phospholipid per centimeter squared surface area of whole lavage (from mice or from warm-active, 4-, or 8-h torpid dunnarts) were applied dropwise onto the subphase of a Wilhelmy-Langmuir balance at 20°C and stabilized for 20 min. After 4 h of torpor, the adsorption rate increased, and equilibrium surface tension (STeq), minimal surface tension (STmin), and the %area compression required to achieve STmin decreased, compared with the warm-active group. After 8 h of torpor, STmin decreased [from 5.2 ± 0.3 to 4.1 ± 0.3 (SE) mN/m]; %area compression required to achieve STmindecreased (from 43.4 ± 1.0 to 27.4 ± 0.8); the rate of adsorption decreased; and STeqincreased (from 26.3 ± 0.5 to 38.6 ± 1.3 mN/m). ST-area isotherms of warm-active dunnarts and mice at 20°C had a shoulder on compression and a plateau on expansion. These disappeared on the isotherms of torpid dunnarts. Samples of whole lavage (from warm-active and 8-h torpor groups) containing 100 μg phospholipid/ml were studied by using a captive-bubble surfactometer at 37°C. After 8 h of torpor, STmin increased (from 6.4 ± 0.3 to 9.1 ± 0.3 mN/m) and %area compression decreased in the 2nd (from 88.6 ± 1.7 to 82.1 ± 2.0) and 3rd (from 89.1 ± 0.8 to 84.9 ± 1.8) compression-expansion cycles, compared with warm-active dunnarts. ST-area isotherms of warm-active dunnarts at 37°C did not have a shoulder on compression. This shoulder appeared on the isotherms of torpid dunnarts. In conclusion, there is a strong correlation between in vitro changes in surface activity and in vivo changes in lipid composition of PS during torpor, although static lung compliance remained unchanged (see Langman et al. cited above). Surfactant from torpid animals is more active at 20°C and less active at 37°C than that of warm-active animals, which may represent a respiratory adaptation to low body temperatures of torpid dunnarts.

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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