Back to Search
Start Over
Comparison of in vitro neutrophil elastase release in nonsmokers and smokers
- Source :
- The American review of respiratory disease. 128(3)
- Publication Year :
- 1983
-
Abstract
- Protease-antiprotease imbalance in the lung is considered a likely pathogenetic mechanism in the development of emphysema. To assess whether differences in enzyme release from stimulated neutrophils could be a factor leading to increased elastase release in the lung, we compared the in vitro release of elastase and a lysosomal enzyme, β-glucosaminidase, from neutrophils of nonsmokers and smokers. Neutrophils were stimulated in vitro by zymosan as a phagocytic stimulus, and the synthetic polypeptide, N-formyl-methionyl-leucyl-phenyl-alanine (FMLP) as chemotactic factor. We studied 54 male subjects, 24 nonsmokers (mean age, 39.5 ± SD 14.4 yr) and 30 smokers (mean age, 45.4 ± SD 8.2 yr). Smokers were divided into 2 groups according to results of their lung function, 17 with normal and 13 with abnormal lung function. Smokers with abnormal lung function were older (59.8 ± SD 11.8 yr) and had smoked more (45.6 ± SD 18.2 pack-years) than smokers with normal lung function (mean age, 39.8 ± SD 11.0 yr; smoking, 22...
- Subjects :
- Pulmonary and Respiratory Medicine
Adult
Lung Diseases
Male
medicine.medical_specialty
Neutrophils
Enzyme release
Vital Capacity
In Vitro Techniques
chemistry.chemical_compound
Internal medicine
Forced Expiratory Volume
Medicine
Humans
Lung function
Lung
N-Formylmethionine
biology
Pancreatic Elastase
business.industry
Respiration
Zymosan
Elastase
Smoking
Chemotaxis
Forced Expiratory Flow Rates
Middle Aged
In vitro
respiratory tract diseases
N-Formylmethionine Leucyl-Phenylalanine
Endocrinology
medicine.anatomical_structure
Hexosaminidases
chemistry
Neutrophil elastase
Immunology
biology.protein
business
Oligopeptides
Subjects
Details
- ISSN :
- 00030805
- Volume :
- 128
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- The American review of respiratory disease
- Accession number :
- edsair.doi.dedup.....5430ae3ad453e4de665ac26512e9adf6