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Am J Physiol Lung Cell Mol Physiol (June 21, 2002). doi:10.1152/ajplung.00020.2002
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Articles in PresS, published online ahead of print June 21, 2002
Am J Physiol Lung Cell Mol Physiol, 10.1152/ajplung.00020.2002
Submitted on January 16, 2002
Accepted on June 4, 2002

Alveolar Macrophage Mediated Elastolysis: roles of Matrix Metalloproteinases, Cysteine and Serine Proteases

Richard EK Russell1, Andrew Thorley2, Sarah V. Culpitt1, Sara Dodd2, Louise E. Donnelly1, Carmen DeMattos1, Mary Fitzgerald2, and Peter J. Barnes1*

1 Department of Thoracic Medicine, National Heart and Lung Institute, London, UK, United Kingdom
2 Stoke Court, Bayer Pharmaceuticals, Stoke Poges, Buckinghamshire, United Kingdom

* To whom correspondence should be addressed. E-mail: p.j.barnes{at}ic.ac.uk.

Chronic obstructive pulmonary disease (COPD) is a common lung disease with cigarette smoking as the major etiological factor but only 15% of smokers develop COPD. Destruction of lung elastin observed in COPD is mediated by many enzymes including cysteine-, serine- and matrix metallo-proteinases (MMP). The contribution of these enzymes to the lung elastolytic load, released from alveolar macrophages collected from non-smokers, healthy smokers and COPD patients was examined using radio-labelled elastin as substrate in the presence of specific enzyme inhibitors. The activity of MMP's was further examined using zymography and Western blotting. COPD macrophages degraded more elastin than either of the other groups. Elastolysis was greatest in the initial 24h. Through the 72-h culture period the contribution to elastolysis of serine elastases decreased, MMP increased and cysteine elastases remained constant. The increased release of elastolytic enzymes in COPD subjects may explain why some smokers develop COPD. This difference may be due to unknown susceptibility factors. Serine proteases play a significant role however other enzymes, particularly the MMP's deserve further investigation.




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