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Antineutrophil elastase activity in cystic fibrosis serum
Author(s) -
Cantin André M.,
Lafrenaye Sylvie,
Bégin Raymond O.
Publication year - 1991
Publication title -
pediatric pulmonology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.866
H-Index - 106
eISSN - 1099-0496
pISSN - 8755-6863
DOI - 10.1002/ppul.1950110311
Subject(s) - elastase , cystic fibrosis , medicine , pancreatic elastase , polyacrylamide gel electrophoresis , antigen , mole , endocrinology , neutrophil elastase , microbiology and biotechnology , immunology , chromatography , biochemistry , enzyme , chemistry , biology , inflammation
The antigenic concentrations of alpha‐1‐antitrypsin (α1AT) were measured in 13 patients with cystic fibrosis (CF) and in 11 healthy subjects. Serum α1AT was purified by immunoaffinity chromatography and the antielastase activity of the purified α1AT was determined by measuring the molar ratio necessary to inhibit human neutrophil elastase (HNE). The association rate constant of α1AT with HNE was determined in a timed assay. The capacity of CF serum α1AT to form complexes with porcine pancreatic elastase was studied by polyacrylamide gel electrophoresis. Antigenic concentrations of α1AT μmol/L were markedly increased in the serum of all patients with CF (61.9 ± 4.3 μmol/L) in comparison to a reference standard (36.7 ± 1.8 μmol/L; P < 0.0001). CF serum α1AT was fully active against HNE, and its association rate constant in the presence of HNE was similar to that of healthy subjects. In addition, CF serum α1AT formed complexes with porcine pancreatic elastase that were electrophoretically indistinguishable from those of normal serum α1AT. These results indicate that patients with CF have increased serum α1AT concentrations and that this antiprotease, when purified from serum, functions normally.