A novel method of purifying lung surfactant proteins A and D from the lung lavage of alveolar proteinosis patients and from pooled amniotic fluid

1998 ◽  
Vol 220 (1-2) ◽  
pp. 139-149 ◽  
Author(s):  
Peter Strong ◽  
Uday Kishore ◽  
Cliff Morgan ◽  
Andres Lopez Bernal ◽  
Mamta Singh ◽  
...  
Keyword(s):  
Amniotic Fluid ◽  
Lung Surfactant ◽  
Lung Lavage ◽  
Surfactant Proteins ◽  
Novel Method ◽  
Alveolar Proteinosis

Surfactant protein A is degraded by alveolar macrophages

1996 ◽  
Vol 271 (2) ◽  
pp. L258-L266 ◽  
Author(s):  
S. R. Bates ◽  
A. B. Fisher
Keyword(s):  
Alveolar Macrophages ◽  
Lung Surfactant ◽  
Protein A ◽  
Surfactant Protein ◽  
Lung Lavage ◽  
Surfactant Protein A ◽  
Cell Association ◽  
Lag Period ◽  
Alveolar Proteinosis ◽  
Lung Surfactant Protein

The metabolism of iodinated lung surfactant protein A (SP-A) by alveolar macrophages in primary culture was examined to determine the role these cells play in the degradation of this surfactant protein. SP-A was isolated from lung lavage obtained from normal bovines, patients with alveolar proteinosis, and silica-treated rats. SP-A (0.5 microgram/ml) was incubated for 3 h with rat alveolar macrophages obtained by lung lavage. Cell association and degradation of human and rat SP-A was three times greater than that of bovine SP-A. During the 3-h period, 50% of total macrophage-associated SP-A was degraded. Degradation was time-, temperature-, and concentration-dependent after a 1-h lag period. SP-A degradation was intracellular, since NH4Cl inhibited degradation > 50%, and macrophage-conditioned medium was ineffective. Tenfold more SP-A was degraded by macrophages than by type II cells isolated after elastase digestion of rat lungs. There was little degradation of SP-A by HeLa cells. We conclude that alveolar macrophages take up and degrade SP-A and thus could contribute to the catabolism of SP-A in the lung.

How to do whole lung lavage for treatment of pulmonary alveolar proteinosis

2020 ◽  
Vol 90 (5) ◽  
pp. 877-878
Author(s):  
Tovi Vo ◽  
Justin C. Y. Chan ◽  
Michael Worthington
Keyword(s):  
Pulmonary Alveolar Proteinosis ◽  
Lung Lavage ◽  
Whole Lung Lavage ◽  
Alveolar Proteinosis

scholarly journals A novel procedure for the rapid isolation of surfactant protein A with retention of its alveolar-macrophage-stimulating properties

1995 ◽  
Vol 309 (2) ◽  
pp. 551-555 ◽  
Author(s):  
J F van Iwaarden ◽  
F Teding van Berkhout ◽  
J A Whitsett ◽  
R S Oosting ◽  
L M G van Golde
Keyword(s):  
Alveolar Macrophage ◽  
Alveolar Macrophages ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Normal Rat ◽  
Normal Human ◽  
Novel Method ◽  
Alveolar Proteinosis ◽  
Simplex Virus

Previous studies have shown that surfactant protein A (SP-A) derived from alveolar-proteinosis patients activates rat alveolar macrophages. However, it is not known if normal rat, dog and human SP-A can also stimulate alveolar macrophages. As alveolar-proteinosis SP-A has a slightly different structure from ordinary SP-A, it would be possible that the ascribed alveolar-macrophage-stimulating properties of SP-A are restricted to alveolar-proteinosis SP-A. To clarify this issue, we isolated SP-A from normal rat and dog pulmonary surfactants, using the same isolation technique commonly used for the isolation of alveolar-proteinosis SP-A, i.e. by butanol precipitation. In contrast with human alveolar-proteinosis SP-A, rat and dog SP-A obtained thus could not activate rat alveolar macrophages to produce oxygen radicals or enhance the phagocytosis of fluorescein isothiocyanate-labelled herpes simplex virus. However, rat, dog and normal human SP-A isolated by a novel method, involving extraction from pulmonary surfactant by using n-octyl beta-D-glucopyranoside and subsequent purification by cation-exchange chromatography, were able to elicit an oxidative burst in rat as well as normal human alveolar macrophages. In addition, dog and rat SP-A obtained thus stimulated the phagocytosis of herpes simplex virus by rat alveolar macrophages. These findings indicate that normal human, rat and dog SP-A have the same alveolar-macrophage-stimulating properties as human alveolar proteinosis SP-A. Dog and rat SP-A isolated by this novel method had the same Ca(2+)-dependent self-aggregation and lipid-aggregation properties as SP-A isolated by butanol precipitation. The new and milder isolation procedure yielded SP-A of high purity, as judged by SDS/PAGE and ELISA.

scholarly journals The Clinical Clues of Pulmonary Alveolar Proteinosis: A Report of 11 Cases and Literature Review

2016 ◽  
Vol 2016 ◽  
pp. 1-5 ◽  
Author(s):  
Qiongya Mo ◽  
Bingbin Wang ◽  
Nian Dong ◽  
Lianmin Bao ◽  
Xiaoqiong Su ◽  
...  
Keyword(s):  
Bronchoalveolar Lavage Fluid ◽  
Clinical Symptoms ◽  
Pulmonary Alveolar Proteinosis ◽  
Relevant Literature ◽  
Neuron Specific Enolase ◽  
Lavage Fluid ◽  
Lung Lavage ◽  
Serum Markers ◽  
Open Lung Biopsy ◽  
Alveolar Proteinosis

Pulmonary alveolar proteinosis (PAP) is a rare interstitial lung disease characterized by the abnormal alveolar accumulation of surfactant components. The diagnosis of PAP can be easily missed since it is rare and lacks specific clinical symptoms. It is of great importance to have a better understanding of the crucial clue to clinically diagnose PAP and take PAP into consideration in the differential diagnosis of interstitial pulmonary diseases or other diseases with similar manifestations. Here, we analyze the clinical characteristics of 11 cases of PAP patients in local hospital and review the relevant literature in order to provide more information in diagnosis and management of PAP. In our observation, cyfra21-1 and neuron-specific enolase (NSE) known as tumor markers probably can be useful serum markers for diagnosis of PAP. As for the method of pathologic diagnosis, open-lung biopsy was the gold standard but now it is less required because findings on examination of bronchoalveolar lavage fluid (BALF) can help to make the diagnosis. We also have deep experience about when and how to carry out lung lavage.

scholarly journals Pulmonary alveolar proteinosis treatment by whole-lung lavage

2012 ◽  
Vol 88 (1042) ◽  
pp. 492-493 ◽  
Author(s):  
Chang Cai ◽  
Min Ye ◽  
Honglei Xu ◽  
Yuping Li
Keyword(s):  
Pulmonary Alveolar Proteinosis ◽  
Lung Lavage ◽  
Whole Lung Lavage ◽  
Alveolar Proteinosis

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

Prostaglandins mediate the fetal pulmonary response to intrauterine inflammation

2012 ◽  
Vol 302 (7) ◽  
pp. L664-L678 ◽  
Author(s):  
Alana J. Westover ◽  
Stuart B. Hooper ◽  
Megan J. Wallace ◽  
Timothy J. M. Moss
Keyword(s):  
Amniotic Fluid ◽  
Lung Inflammation ◽  
Lung Surfactant ◽  
Fetal Lung ◽  
Surfactant Protein ◽  
Fetal Plasma ◽  
Pulmonary Response ◽  
Surfactant Production ◽  
Prostaglandin Dehydrogenase ◽  
Prostaglandin H

Intra-amniotic (IA) lipopolysaccharide (LPS) induces intrauterine and fetal lung inflammation and increases lung surfactant and compliance in preterm sheep; however, the mechanisms are unknown. Prostaglandins (PGs) are inflammatory mediators, and PGE2 has established roles in fetal lung surfactant production. The aim of our first study was to determine PGE2 concentrations in response to IA LPS and pulmonary gene expression for PG synthetic [prostaglandin H synthase-2 (PGHS-2) and PGE synthase (PGES)] and PG-metabolizing [prostaglandin dehydrogenase (PGDH)] enzymes and PGE2 receptors. Our second study aimed to block LPS-induced increases in PGE2 with a PGHS-2 inhibitor (nimesulide) and determine lung inflammation and surfactant protein mRNA expression. Pregnant ewes received an IA saline or LPS injection at 118 days of gestation. In study 1, fetal plasma and amniotic fluid were sampled before and at 2, 4, 6, 12, and 24 h after injection and then daily, and fetuses were delivered 2 or 7 days later. Amniotic fluid PGE2 concentrations increased ( P < 0.05) 12 h and 3–6 days after LPS. Fetal lung PGHS-2 mRNA and PGES mRNA increased 2 ( P = 0.0084) and 7 ( P = 0.014) days after LPS, respectively. In study 2, maternal intravenous nimesulide or vehicle infusion began immediately before LPS or saline injection and continued until delivery 2 days later. Nimesulide inhibited LPS-induced increases in PGE2 and decreased fetal lung IL-1β and IL-8 mRNA ( P ≤ 0.002) without altering lung inflammatory cell infiltration. Nimesulide decreased surfactant protein (SP)-A ( P = 0.05), -B ( P = 0.05), and -D ( P = 0.0015) but increased SP-C mRNA ( P = 0.023). Thus PGHS-2 mediates, at least in part, fetal pulmonary responses to inflammation.

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
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