ERJ
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Braun, J
Right arrow Articles by Wiessmann, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Braun, J
Right arrow Articles by Wiessmann, K.
Eur Respir J 1994; 7: 127-133
Copyright © ERS Journals Ltd 1994


Original Articles

Characterization of protein-antiproteinase imbalance in bronchoalveolar lavage from patients with pneumonia

J Braun, K Dalhoff, B Schaaf, WG Wood, and KJ Wiessmann

In order to clarify the mode of inactivation of alpha1-proteinase inhibitor (alpha 1-PI) in pneumonia, 21 immunocompetent patients and 19 immunocompromised patients with acute pneumonia (Groups I and II) were studied. Nine patients successfully treated for pneumonia and 10 healthy volunteers served as controls (Groups III and IV, respectively). The concentrations of alpha 1-PI, elastase and myeloperoxidase (MPO) in bronchoalveolar lavage fluid (BALF) were determined using a luminometric assay. Elastase inhibition capacity was determined using a colorimetric assay. Thus, the functional activity of alpha 1-PI was calculated. Both elastase and MPO were significantly higher in group I, when compared with the other groups. The mean concentration of alpha 1-PI was significantly higher in patients with acute pneumonia (Group I 13 mg.l-1, Group II 4.22 mg.l-1) than in Groups III and IV (2.65 and 0.33 mg.l-1, respectively), whereas, the proportion of active alpha 1-PI was significantly lower in Group I than in the other groups. Only a small proportion was present as a complex with elastase (ca. 5.9%) or in oxidised form (ca. 4.8%), 85% of alpha 1-PI was irreversibly proteolyzed. This resulted in free elastase activity in 7 of the 40 patients (18%) with acute pneumonia. We conclude that functional activity of alpha 1-PI is markedly impaired due to irreversible proteolysis in acute pneumonia, despite high immunological concentrations.


This article has been cited by other articles:


Home page
Am. J. Respir. Cell Mol. Bio.Home page
M. Brantly
{alpha}1-Antitrypsin: Not Just an Antiprotease: Extending the Half-Life of a Natural Anti-Inflammatory Molecule by Conjugation with Polyethylene Glycol
Am. J. Respir. Cell Mol. Biol., December 1, 2002; 27(6): 652 - 654.
[Full Text] [PDF]


Home page
PediatricsHome page
Y. Y. Koh, Y. Park, H. J. Lee, and C. K. Kim
Levels of Interleukin-2, Interferon-{gamma}, and Interleukin-4 in Bronchoalveolar Lavage Fluid From Patients With Mycoplasma Pneumonia: Implication of Tendency Toward Increased Immunoglobulin E Production
Pediatrics, March 1, 2001; 107(3): 39e - 39.
[Abstract] [Full Text]


Home page
Am. J. Respir. Crit. Care Med.Home page
J. HIRSCH, A. ELSSNER, G. MAZUR, K. L. MAIER, I. BITTMANN, J. BEHR, M. SCHWAIBLMAIR, H. REICHENSPURNER, H. FÜRST, J. BRIEGEL, et al.
Bronchiolitis Obliterans Syndrome after (Heart-)Lung Transplantation . Impaired Antiprotease Defense and Increased Oxidant Activity
Am. J. Respir. Crit. Care Med., November 1, 1999; 160(5): 1640 - 1646.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
C. Taggart, D. Cervantes-Laurean, G. Kim, N. G. McElvaney, N. Wehr, J. Moss, and R. L. Levine
Oxidation of either Methionine 351 or Methionine 358 in alpha 1-Antitrypsin Causes Loss of Anti-neutrophil Elastase Activity
J. Biol. Chem., August 25, 2000; 275(35): 27258 - 27265.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1994 by the European Respiratory Society.