Publication Type	Academic Article
Authors	Casolaro M, Fells G, Wewers M, Pierce J, Ogushi F, Hubbard R, Sellers S, Forstrom J, Lyons D, Kawasaki G
Journal	J Appl Physiol (1985)
Volume	63
Issue	5
Pagination	2015-23
Date Published	11/01/1987
ISSN	8750-7587
Keywords	Blood Proteins, Bronchoalveolar Lavage Fluid, Protease Inhibitors, alpha 1-Antitrypsin
Abstract	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)
DOI	10.1152/jappl.1987.63.5.2015
PubMed ID	3500941