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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Augmentation of lung antineutrophil elastase capacity with recombinant human alpha-1-antitrypsin.

To evaluate the potential use of recombinant DNA-produced alpha-1-antitrypsin (alpha-1-AT) to augment the lung antineutrophil elastase defenses in alpha-1-AT deficiency, we compared the kinetics of intravenously administered recombinant produced alpha-1-AT (r alpha-1-AT) and purified normal human plasma alpha-1-AT (p alpha-1-AT) in the blood and lung of rhesus monkeys. The r alpha-1-AT was produced in yeast transformed with an expressing plasmid containing a full-length human alpha-1-AT complementary deoxyribonucleic acid and purified to greater than 99% homogeneity. The r alpha-1-AT has a molecular weight of 45,000, no carbohydrates, and is identical in sequence to normal plasma alpha-1-AT except for an additional N-terminal acetylmethionine. Despite its lack of carbohydrates, the r alpha-1-AT inhibited human neutrophil elastase with an association rate constant similar to that of p alpha-1-AT. Rhesus monkeys were infused intravenously with 120 mg/kg of r alpha-1-AT (n = 13) or p alpha-1-AT (n = 12) and the serum, urine, and lung epithelial lining fluid (ELF) concentrations of these molecules quantified at various intervals.(ABSTRACT TRUNCATED AT 250 WORDS)[1]

References

  1. Augmentation of lung antineutrophil elastase capacity with recombinant human alpha-1-antitrypsin. Casolaro, M.A., Fells, G., Wewers, M., Pierce, J.E., Ogushi, F., Hubbard, R., Sellers, S., Forstrom, J., Lyons, D., Kawasaki, G. J. Appl. Physiol. (1987) [Pubmed]
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