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Characterization of serine/cysteine protease inhibitor α 1 ‐antitripsin from meconium‐instilled rabbit lungs
Author(s) -
Zagariya A.M.,
Bhat R.,
Zhabotynsky E.,
Chari G.,
Navale S.,
Xu Q.,
Keiderling T.A.,
Vidyasagar D.
Publication year - 2005
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.20492
Subject(s) - serpin , neutrophil elastase , slpi , serine proteinase inhibitors , serine protease , protease inhibitor (pharmacology) , inflammation , meconium , serine , lung , elastase , biology , microbiology and biotechnology , chemistry , immunology , protease , biochemistry , enzyme , medicine , fetus , gene , virus , pregnancy , genetics , antiretroviral therapy , viral load
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.