Augmentation of lung antineutrophil elastase capacity with recombinant human alpha-1-antitrypsin. Academic Article Article uri icon

Overview

MeSH

  • Animals
  • Electrophoresis, Polyacrylamide Gel
  • Epithelium
  • Half-Life
  • Humans
  • Lung
  • Macaca mulatta
  • Molecular Weight

MeSH Major

  • 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)

publication date

  • November 1987

has subject area

  • Animals
  • Blood Proteins
  • Bronchoalveolar Lavage Fluid
  • Electrophoresis, Polyacrylamide Gel
  • Epithelium
  • Half-Life
  • Humans
  • Lung
  • Macaca mulatta
  • Molecular Weight
  • Protease Inhibitors
  • alpha 1-Antitrypsin

Research

keywords

  • Comparative Study
  • Journal Article

Identity

Language

  • eng

PubMed ID

  • 3500941

Additional Document Info

start page

  • 2015

end page

  • 2023

volume

  • 63

number

  • 5