Biomedical Science Letters (대한의생명과학회지)

The Korean Society for Biomedical Laboratory Sciences (대한의생명과학회)
권호 표지

Analysis of Protease and Antiprotease Concentrations in Retired Workers Exposed to Inorganic Dusts

  • Shin, Jae-Hoon (Department of Biomedical Laboratory Science, Graduate School of Health Science, Eulji University) ;
  • Hwang, Joo-Hwan (Center for Occupational Lung Diseases, KWAMCO) ;
  • Lee, Kyung-Myung (Center for Occupational Lung Diseases, KWAMCO) ;
  • Lee, Jong-Seong (Center for Occupational Lung Diseases, KWAMCO) ;
  • Lee, Jeong-Oh (Center for Occupational Lung Diseases, KWAMCO) ;
  • Choi, Byung-Soon (Center for Occupational Lung Diseases, KWAMCO) ;
  • Kim, In-Sik (Department of Biomedical Laboratory Science, Graduate School of Health Science, Eulji University)
  • Published : 2009.12.31
Download PDF
⟨ Previous Next ⟩

Abstract

Occupational exposure to inorganic dusts such as coal and silica has been identified as a chronic obstructive pulmonary disease (COPD) risk factor. This risk factor causes lung inflammation and protease-antiprotease imbalance. This abnormal inflammatory response of the lung induces parenchymal tissue destruction and leads to progressive airflow limitation that is characteristics of COPD. The aim of this study was to determine the relationship of proteases such as neutrophil elastase (NE) and matrix metalloproteinase (MMP)-9 and antiproteases such as alpha-1 antitrypsin (AAT) and tissue inhibitors of metalloproteinase (TIMP)-1 with lung function. The study population contained 223 retired workers exposed to inorganic dusts. We performed lung function test, including percent of forced expiratory volume in one second ($%FEV_1$) predicted and $%FEV_1$/forced vital capacity (FVC). We analyzed serum MMP-9, AAT, TIMP-1 and plasma NE concentrations by sandwich enzyme immunoassay. NE, AAT, and TIMP-1 concentrations in workers, who had $%FEV_1$<80% predicted, were higher than those of workers who had $%FEV_1{\geq}80%$ (P<0.05). Both AAT and TIMP-1 concentrations in workers with airflow limitation were higher than those of workers with normal airflow (P<0.05). $%FEV_1$ predicted showed significant negative correlation with AAT (r=-0.255, P<0.0l), TIMP-1 (r=-0.232, P<0.01), and NE (r=-0.196, P<0.01). $%FEV_1$/FVC predicted showed significant negative correlation with NE (r=-0.172, P<0.05). From the results of stepwise multiple regression analysis about $%FEV_1$ and $%FEV_1$/FVC, significant independents were NE (r=-0.135, P=0.001) and AAT (r=-0.100, P=0.013) in $%FEV_1$, and NE (r=-0.160, P=0.014) in $%FEV_1$/FVC. In the present study, there were significant correlations between airflow limitation and protease concentration and between airflow limitation and antiprotease concentration. Serum protease and antiprotease concentrations, however, may be affected by the biological and inflammatory responses. It is necessary to evaluate specimens more reflected the effects of proteases and antiproteases in the lung such as lung tissue, bronchoalveolar lavage fluid, and exhaled breath condensate (EBC).

Keywords

References

  1. Abboud RT, Fera T, Johal S, Richter A, Gibson N. Effect of smoking on plasma neutrophil elastase levels. J Lab Clin Med. 1986. 108: 294-300.
  2. Barnes PJ, Shapiro SD, Pauwels RA. Chronic obstructive pulmonary disease: molecular and cellular mechanisms. Eur Respir J. 2003. 22: 672-688. https://doi.org/10.1183/09031936.03.00040703
  3. Barnes PJ. Mediators of chronic obstructive pulmonary disease. Pharmachol Rev. 2004. 56: 515-548. https://doi.org/10.1124/pr.56.4.2
  4. Beeh KM, Beier J, Kornmann O, Buhl R. Sputum matrix metalloproteinase-9, tissue inhibitor of metalloprotinease-1, and their molar ratio in patients with chronic obstructive pulmonary disease, idiopathic pulmonary fibrosis and healthy subjects. Respir Med. 2003. 97: 634-639. https://doi.org/10.1053/rmed.2003.1493
  5. Betsuyaku T, Nishimura M, Takeyabu K, Tanino M, Miyamoto K, Kawakami Y. Decline in FEV(1) in community-based older volunteers with higher levels of neutrophil elastase in bronchoalveolar lavage fluid. Respiration 2000. 67: 261-267. https://doi.org/10.1159/000029508
  6. Carp H, Miller F, Hoidal JR, Janoff A. Potential mechanism of emphysema: alpha 1-proteinase inhibitor recovered from lungs of cigarette smokers contains oxidized methionine and has decreased elastase inhibitory capacity. Proc Natl Acad Sci U S A. 1982. 79: 2041-2045. https://doi.org/10.1073/pnas.79.6.2041
  7. Cataldo D, Munaut C, Noël A, Frankenne F, Bartsch P, Foidart JM, Louis R. MMP-2- and MMP-9-linked gelatinolytic activity in the sputum from patients with asthma and chronic obstructive pulmonary disease. Int Arch Allergy Immunol. 2000. 123: 259-267. https://doi.org/10.1159/000024452
  8. Eriksson S. Studies in ${\alpha}1$ antitrypsin deficiency. Acta Med Scand. Suppl. 1965. 432: 1-85.
  9. Fera T, Abboud RT, Richter A, Johal SS. Acute effect of smoking on elastaselike esterase activity and immunologic neutrophil elastase levels in bronchoalveolar lavage fluid. Am Rev Respir Dis. 1986. 133: 568-573.
  10. Fujita J, Nelson NL, Daughton DM, Dobry CA, Spurzem JR, Irino S, Rennard SI. Evaluation of elastase and antielastase balance in patients with chronic bronchitis and pulmonary emphysema. Am Rev Respir Dis. 1990. 142: 57-62. https://doi.org/10.1164/ajrccm/142.1.57
  11. Gross P, Pfitzer EA, Tolker E, Babyak MA, Kasxhak M. Experimental emphysema: its production with papain in normal and silicotic rats. Arch Environ Health. 1965. 11: 50-58. https://doi.org/10.1080/00039896.1965.10664169
  12. Hnizdo E. Loss of lung function associated with exposure to silica dust and with smoking and its relation to disability and mortality in South Africa gold miners. Br J Ind Med. 1992. 49: 472-479.
  13. Hnizdo E, Sullivan PA, Bang KM, Wagner G. Association between chronic obstructive pulmonary disease and employment by industry and occupation in the US population: a study of data from the Third National Health and Nutrition Examination Survey. Am J Epidemiol. 2002. 156: 738-746. https://doi.org/10.1093/aje/kwf105
  14. Hogg JC. Pathophysiology of airflow limitation in chronic obstructive pulmonary disease. Lancet 2004. 364: 709-721. https://doi.org/10.1016/S0140-6736(04)16900-6
  15. Laurell CB, Eriksson A. The electrophoresis alpha 1-globulin pattern of serum in alpha 1-antitrypsin deficiency. Scand J Clin Lab Invest. 1963. 15: 132-140. https://doi.org/10.1080/00365516309051324
  16. MacNee W. Pathogenesis of chronic obstructive pulmonary disease. Clin Chest Med. 2007. 28: 479-513. https://doi.org/10.1016/j.ccm.2007.06.008
  17. Opdenakker G, Van den Steen PE, Dubois B, Nelissen I, Van Coillie E, Masure S, Proost P, Van Damme J. Gelatinase B functions as regulator and effector in leukocyte biology. J Leukoc Biol. 2001. 69: 851-859.
  18. Paczek L, Michalska W, Bartlomiejcyk I. Trypsin, elastase, plasmin and MMP-9 activity in the srum concentration during the ageing process. Age Ageing 2008. 37: 318-323. https://doi.org/10.1093/ageing/afn039
  19. Rabe KF, Hurd S, Anzueto A, Barnes PJ, Buist SA, Calverley P, Fukuchi Y, Jenkins C, Rodriguez-Roisin R, van Weel C, Zielinski J. Global Initiative for Chronic Obstructive Lung Disease. Global strategy for the diagnosis, management, and prevention of chronic obstructive pulmonary disease: GOLD executive summary. Am J Respir Crit Care Med. 2007. 176: 532-555. https://doi.org/10.1164/rccm.200703-456SO
  20. Yoshioka A, Betsuyaku T, Nishimura M, Miyamoto K, Kondo T, Kawakami Y. Excessive neutrophil elastase in bronchoalveolar lavage fluid in subclinical emphysema. Am J Respir Crit Care Med. 1995. 152: 2127-2132. https://doi.org/10.1164/ajrccm.152.6.8520785