Myeloperoxidase in human lung lavage

Inflammation ◽  
1990 ◽  
Vol 14 (4) ◽  
pp. 447-454 ◽  
Author(s):  
Birgitta Schmekel ◽  
S. E. Karlsson ◽  
M. Linden ◽  
C. Sundstr�m ◽  
H. Tegner ◽  
...  
Keyword(s):  
Human Lung ◽  
Lung Lavage

Isolation and chemical composition of surface-active material from human lung lavage

Lipids ◽  
1988 ◽  
Vol 23 (6) ◽  
pp. 551-558 ◽  
Author(s):  
T. Sadana ◽  
K. Dhall ◽  
S. N. Sanyal ◽  
A. Wali ◽  
R. Minocha ◽  
...  
Keyword(s):  
Chemical Composition ◽  
Human Lung ◽  
Active Material ◽  
Lung Lavage ◽  
Surface Active ◽  
Surface Active Material

Extracellular Elastolytic Activity in Human Lung Lavage: A Comparative study between Smokers and Non-Smokers

1985 ◽  
Vol 69 (1) ◽  
pp. 17-27 ◽  
Author(s):  
S. F. Smith ◽  
A. Guz ◽  
N. T. Cooke ◽  
G. H. Burton ◽  
T. D. Tetley
Keyword(s):  
Proteinase Inhibitor ◽  
Protease Activity ◽  
Human Lung ◽  
Lung Lavage ◽  
Low Molecular Weight ◽  
Elastase Activity ◽  
Significant Difference ◽  
Elastolytic Activity ◽  
Bronchial Mucus ◽  
Extracellular Protease Activity

1. Unrestrained proteolysis in the lung is believed to initiate emphysema, a disease common among tobacco smokers. However, few studies have found extracellular protease activity in human lung lavage. 2. In this investigation, elastase and serine protease activities were measured in broncho-alveolar lavage supernatants (BAL) from patients undergoing routine investigations. Significantly more elastolytic activity (against insoluble [3H]-elastin) was recovered in the lavage of smokers than that of non-smokers. However, no significant difference was found when the levels of serine proteolytic activity (against N-succinyl-L-trialanyl-p-nitroanilide) were compared. 3. The elastolytic component of the protease activity rose from 5% in non-smokers’ BAL to over 30% in that of smokers, suggesting that elastase activity is selectively enhanced by smoking. In lavages from most smokers, 80% or more of the elastase activity was serine-dependent, whereas lavages from non-smokers contained variable proportions of serine elastase. 4. Both α1-proteinase inhibitor (α1-PI) and a low molecular weight antiprotease, bronchial mucus proteinase inhibitor (BMPI) were detectable in the lavage samples, the latter contributing up to 76% of the total antiprotease quantified in the lavage. Functional antiprotease was detected in 85% of the lavages. 5. Since there were no differences in either antiprotease levels or functional inhibitory capacities between lavages from smokers and controls, it is concluded that the imbalance in the protease/antiprotease profile of the smokers’ lung results from an enhancement of proteases, specifically of elastolytic activity, rather than a reduction in inhibitory capacity.

An assay for the assessment of lipocortin 1 levels in human lung lavage fluid

1990 ◽  
Vol 131 (1) ◽  
pp. 119-125 ◽  
Author(s):  
Susan F. Smith ◽  
Nicolas J. Goulding ◽  
Jane L. Godolphin ◽  
Teresa D. Tetley ◽  
C. Michael Roberts ◽  
...  
Keyword(s):  
Human Lung ◽  
Lavage Fluid ◽  
Lung Lavage

Fine airborne urban particles (PM2.5) sequester lung surfactant and amino acids from human lung lavage

2007 ◽  
Vol 293 (4) ◽  
pp. L1053-L1058 ◽  
Author(s):  
Michaela Kendall
Keyword(s):  
Amino Acids ◽  
Fine Particles ◽  
Human Lung ◽  
Lung Surfactant ◽  
Statistical Technique ◽  
Lung Lavage ◽  
Chemical Components ◽  
Isoleucine Leucine ◽  
Analysis Technique ◽  
Lung Lining Fluid

Components of surfactant act as opsonins and enhance phagocytosis of bacteria; whether this process occurs with atmospheric fine particles has not been shown. We have studied the interactions of fine particles (urban PM2.5) and surfactant removed from normal human lungs by lavage, using a surface analysis technique. The aim was to identify which of the chemical components of brochoalveolar lavage (BAL) deposit on the surfaces of urban PM2.5. Deposition of surfactant components on urban PM2.5 surfaces was reported in previous studies, but molecular identification and relative quantification was not possible using simple data analysis. In this study, we were able to identify adsorbed components by applying an appropriate statistical technique, factor analysis. In this study, the most strongly associated mass fragment on PM2.5 surfaces exposed to BAL (and undetected on both untreated samples and saline controls) was di-palmitoyl-phosphatidylcholine, a component of lung surfactant. Amino acids were also strongly associated with BAL-exposed PM2.5 surfaces and not other sample types. Thirteen mass fragments were identified, diagnostic of the amino acids alanine, arginine, asparagine, aspartic acid, glutamic acid, glutamine, glycine, histidine, isoleucine, leucine, lysine, methionine, serine, and valine. This study provides evidence that lung surfactant and amino acids related to opsonin proteins adsorb to nonbiological particle surfaces exposed to human lung lining fluid. Disruption of normal surfactant function, both physical and immunological, is possible but unproven. Further work on this PM-opsonin interaction is recommended.

Analysis of leukotriene B4 in human lung lavage by HPLC and mass spectrometry

1986 ◽  
Vol 31 (2) ◽  
pp. 227-237 ◽  
Author(s):  
Jay Y. Westcott ◽  
Kurt R. Stenmark ◽  
Robert C. Murphy
Keyword(s):  
Mass Spectrometry ◽  
Human Lung ◽  
Lung Lavage ◽  
Leukotriene B4

Multi-platform metabolomics assays for human lung lavage fluids in an air pollution exposure study

2016 ◽  
Vol 408 (17) ◽  
pp. 4751-4764 ◽  
Author(s):  
Izabella Surowiec ◽  
Masoumeh Karimpour ◽  
Sandra Gouveia-Figueira ◽  
Junfang Wu ◽  
Jon Unosson ◽  
...  
Keyword(s):  
Air Pollution ◽  
Human Lung ◽  
Lung Lavage ◽  
Exposure Study ◽  
Air Pollution Exposure ◽  
Pollution Exposure

scholarly journals Compromised inhibition of human lung lavage cell elastases

FEBS Letters ◽  
1996 ◽  
Vol 390 (2) ◽  
pp. 187-190 ◽  
Author(s):  
S.F. Smith ◽  
N.A. Roberts ◽  
A. Guz ◽  
T.D. Tetley
Keyword(s):  
Human Lung ◽  
Lung Lavage

scholarly journals Adsorption of surfactant protein D from human respiratory secretions by carbon nanotubes and polystyrene nanoparticles depends on nanomaterial surface modification and size

2015 ◽  
Vol 370 (1661) ◽  
pp. 20140038 ◽  
Author(s):  
Magda Marchetti ◽  
Milo S. P. Shaffer ◽  
Martina Zambianchi ◽  
Shu Chen ◽  
Fabiana Superti ◽  
...  
Keyword(s):  
Carbon Nanotubes ◽  
Surface Modification ◽  
Human Lung ◽  
Surfactant Protein ◽  
Lung Lavage ◽  
Surfactant Protein D ◽  
Main Function ◽  
Immune Defence ◽  
Polystyrene Nanoparticles ◽  
Macrophage Phagocytosis

The alveolar respiratory unit constitutes one of the main targets of inhaled nanoparticles; the effect of engineered nanomaterials (NMs) on human health is largely unknown. Surfactant protein D (SP-D) is synthesized by alveolar type II epithelial cells and released into respiratory secretions; its main function is in immune defence, notably against inhaled microbes. SP-D also plays an important role in modulating an appropriate inflammatory response in the lung, and reduced SP-D is associated with a number of inflammatory lung diseases. Adsorption of SP-D to inhaled NMs may facilitate their removal via macrophage phagocytosis. This study addresses the hypothesis that the chemistry, size and surface modification of engineered NMs will impact on their interaction with, and adsorption of, SP-D. To this purpose, we have examined the interactions between SP-D in human lung lavage and two NMs, carbon nanotubes and polystyrene nanoparticles, with different surface functionalization. We have demonstrated that particle size, functionalization and concentration affect the adsorption of SP-D from human lung lavage. Functionalization with negatively charged groups enhanced the amount of SP-D binding. While SP-D binding would be expected to enhance macrophage phagocytosis, these results suggest that the degree of binding is markedly affected by the physicochemistry of the NM and that deposition of high levels of some nanoparticles within the alveolar unit might deplete SP-D levels and affect alveolar immune defence mechanisms.

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