The expression and characterization of five recombinant murine alpha 1-protease inhibitor proteins

Biochem Biophys Res Commun. 1996 Feb 6;219(1):64-9. doi: 10.1006/bbrc.1996.0182.


The Mus musculus alpha 1-protease inhibitor gene cluster encodes five highly related proteins. The most significant amino acid polymorphisms lie within the reactive-site loop which is important in determining serpin substrate specificity. All five genes are transcribed in M. musculus adult liver and presumably secreted into plasma. In an attempt to characterize their protein products all five cDNAs were expressed in recombinant mammalian cells and the protease inhibition activity of each determined. Only two of the proteins were efficient inhibitors of neutrophil elastase, the major physiological target of the sole human alpha 1-protease inhibitor (antitrypsin). Four of the proteins were active against chymotrypsin, while no substrate could be identified for the fifth.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • CHO Cells
  • Cell Line
  • Chlorocebus aethiops
  • Chymotrypsin / antagonists & inhibitors
  • Cricetinae
  • Gene Expression*
  • Humans
  • Kidney
  • Leukocyte Elastase / antagonists & inhibitors
  • Liver / metabolism*
  • Mice
  • Molecular Sequence Data
  • Pancreatic Elastase / antagonists & inhibitors
  • Plasmids
  • Recombinant Proteins / biosynthesis*
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / pharmacology
  • Substrate Specificity
  • Transfection
  • Trypsin / metabolism
  • alpha 1-Antitrypsin / biosynthesis*
  • alpha 1-Antitrypsin / isolation & purification
  • alpha 1-Antitrypsin / pharmacology*


  • Recombinant Proteins
  • alpha 1-Antitrypsin
  • Chymotrypsin
  • Pancreatic Elastase
  • Leukocyte Elastase
  • Trypsin