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(Chest. 1996;110:278S-283S.)
© 1996 American College of Chest Physicians

Bioengineering: agr1-Proteinase Inhibitor Site-Specific Mutagenesis

The Prospect for Improving the Inhibitor

Maurizio Luisetti MD, FCCP1 and James Travis PhD2

1 From the Istituto di Tisiologia e Malattie Apparato Respiratorio, Università di Pavia, IRCCS Policlinico San Matteo, Pavia, Italy
2 From the Department of Biochemistry, University of Georgia, Athens

agr1-Proteinase inhibitor (agr1-PI) augmentation therapy has been licensed for treatment of agr1-PI-deficient individuals with pulmonary emphysema. The currently available product is purified from pooled human plasma. To obtain larger amounts of protein free from possible unknown plasma contaminants, human agr1-PI has been produced by recombinant DNA. Since wild-type agr1-PI is susceptible to oxidative impairment, several agr1-PI variants in which the active site oxidation-sensitive residue is replaced by inert residues have been constructed. This article is aimed at reviewing the history, biological efficacy, advantages, disadvantages, and concerns linked to agr1-PI recombinant DNA and site-specific mutagenesis technology.

Key Words: agr1-PI deficiency • neutrophil elastase • oxidants • pulmonary emphysema • recombinant DNA






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Copyright © 1996 by the American College of Chest Physicians.