We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Could the Oxidation of α1-Antitrypsin Prevent the Binding of Human Neutrophil Elastase in COVID-19 Patients?
- Authors
D'Amato, Maura; Campagnoli, Monica; Iadarola, Paolo; Bignami, Paola Margherita; Fumagalli, Marco; Chiarelli, Laurent Roberto; Stelitano, Giovanni; Meloni, Federica; Linciano, Pasquale; Collina, Simona; Pietrocola, Giampiero; Vertui, Valentina; Aliberti, Anna; Fossali, Tommaso; Viglio, Simona
- Abstract
Human neutrophil elastase (HNE) is involved in SARS-CoV-2 virulence and plays a pivotal role in lung infection of patients infected by COVID-19. In healthy individuals, HNE activity is balanced by α1-antitrypsin (AAT). This is a 52 kDa glycoprotein, mainly produced and secreted by hepatocytes, that specifically inhibits HNE by blocking its activity through the formation of a stable complex (HNE–AAT) in which the two proteins are covalently bound. The lack of this complex, together with the detection of HNE activity in BALf/plasma samples of COVID-19 patients, leads us to hypothesize that potential functional deficiencies should necessarily be attributed to possible structural modifications of AAT. These could greatly diminish its ability to inhibit neutrophil elastase, thus reducing lung protection. The aim of this work was to explore the oxidation state of AAT in BALf/plasma samples from these patients so as to understand whether the deficient inhibitory activity of AAT was somehow related to possible conformational changes caused by the presence of abnormally oxidized residues.
- Subjects
LEUCOCYTE elastase; COVID-19; ELASTASES; OXIDATION states; LUNG infections; OXIDATION
- Publication
International Journal of Molecular Sciences, 2023, Vol 24, Issue 17, p13533
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms241713533