Profile of Elastase Activity Released by Human Lung Lavage Cells in Culture

1987 ◽  
Vol 72 (s16) ◽  
pp. 84P-84P
Author(s):  
S.F. Smith ◽  
A. Guz ◽  
T.D. Tetley
Keyword(s):  
Human Lung ◽  
Lung Lavage ◽  
Elastase Activity ◽  
Cells In Culture

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.

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

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

Detection of Antileucoprotease and Elastase Activity in Peripheral Lung Lavage

1983 ◽  
Vol 64 (2) ◽  
pp. 11P-11P ◽  
Author(s):  
T. Tetley ◽  
N. Cooke ◽  
G. Burton ◽  
A. Guz ◽  
S. Smith
Keyword(s):  
Lung Lavage ◽  
Elastase Activity ◽  
Peripheral Lung

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
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