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Allotypes of α 1 ‐antitrypsin in patients with cystic fibrosis, homozygous and heterozygous for deltaF508
Author(s) -
Döring Gerd,
KroghJohansen Helle,
Weidinger Sebastian,
Høiby Niels
Publication year - 1994
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.1950180104
Subject(s) - cystic fibrosis , pseudomonas aeruginosa , medicine , heterozygote advantage , compound heterozygosity , lung , respiratory disease , carriage , serine , immunology , lung infection , mutation , microbiology and biotechnology , gastroenterology , pathology , genotype , biology , bacteria , gene , genetics , enzyme , biochemistry
In cystic fibrosis (CF) neutrophil released serine proteinase activity may facilitate Pseudomonas aeruginosa lung colonization, leading to chronic infection. Since such activity is mostly controlled by α 1 ‐antitrypsin (α 1 ‐AT), we postulated that patients with CF carrying deficient α 1 ‐AT variants might be at higher risk for P. aeruginosa acquisition and might reveal other phenomena, specific for serine proteinase activity. In 215 Danish patients with CF, homozygous (80%) or heterozygous (20%) for the major CF mutation deltaF508, α 1 ‐AT variants were determined. Carriage of deficient α‐AT variants was correlated to an earlier onset of P. aeruginosa lung infection ( P < 0.001), higher total IgG ( P < 0.001), and P. aeruginosa‐specific serum antibodies ( P < 0.0001). The two groups did not differ in lung function, probably due to intensive antimicrobial treatment. Pediatr Pulmonol. 1994; 18:3–7. © 1994 Wiley‐Liss. Inc.