1. Determination of proteinase 3—α1-antitrypsin complexes in inflammatory fluids
- Author
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Bart A. van de Wiel, James C. Powers, Koert M. Dolman, Albert E. G. Kr. von dem Borne, A. Sonnenberg, J. J. Abbink, Chih-Min Kam, C. Erik Hack, Roel Goldschmeding, and Other departments
- Subjects
C-ANCA ,Proteinase 3 ,Protein Conformation ,Myeloblastin ,Biophysics ,Radioimmunoassay ,Inflammation ,Bacteremia ,Biochemistry ,Arthritis, Rheumatoid ,Structural Biology ,In vivo ,Inflammatory fluid ,Genetics ,medicine ,Synovial fluid ,Humans ,cardiovascular diseases ,Molecular Biology ,biology ,Chemistry ,Elastase ,Serine Endopeptidases ,Cell Biology ,α1-Antitrypsin ,Enzyme inhibitor ,alpha 1-Antitrypsin ,biology.protein ,medicine.symptom - Abstract
Physiological inhibitors were tested for their in vitro interaction with neutrophil proteinase 3 (PR3). The major plasma proteinase inhibitor of PR3 is alpha 1AT. We have developed a radioimmunoassay (RIA) for quantitative detection of PR3-alpha 1AT complexes formed in vivo in inflammatory exudates such as synovial fluid and plasma from patients with sepsis. Levels of PR3-alpha 1AT complexes correlated significantly with levels of human neutrophil elastase (HNE)-alpha 1AT complexes. Thus, in vivo alpha 1AT not only protects against excessive HNE activity, but also against excessive PR3 activity.
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