Characterization of serine/cysteine protease inhibitor α1-antitripsin from meconium-instilled rabbit lungs
✍ Scribed by A.M. Zagariya; R. Bhat; E. Zhabotynsky; G. Chari; S. Navale; Q. Xu; T.A. Keiderling; D. Vidyasagar
- Book ID
- 102301288
- Publisher
- John Wiley and Sons
- Year
- 2005
- Tongue
- English
- Weight
- 138 KB
- Volume
- 96
- Category
- Article
- ISSN
- 0730-2312
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✦ Synopsis
Abstract
We have recently purified from meconium‐instilled rabbit lungs a novel serine proteinase inhibitor, with an apparent molecular mass of 50 kDa, which we assign to be α~1~‐antitripsin. We hypothesize that serpin may attenuate pulmonary inflammation and improve surfactant function after meconium aspiration. α~1~‐antitripsin is a member of the proteinase inhibitor (serpin) superfamily and inhibitor of neutrophil elastase, and it can be identified as a member of the family by its amino acid sequence due to the high degree of conserved residues. α~1~‐antitripsin is synthesized by epithelial cells, macrophages, monocytes, and neutrophils. Deficiency in α~1~‐antitripsin leads to exposure of lungs to uncontrolled proteolytic attack from neutrophil elastase or other damaging factors culminating in lung destruction and cell apoptosis. We hypothesize that accumulation of α~1~‐antitripsin in the lungs serves as a predisposed protection against meconium‐induced lung injury. In this paper, we show how this knowledge can lead to the development of novel therapeutic approaches for treatment of MAS. © 2005 Wiley‐Liss, Inc.