INCORPORATION OF GLUCOSAMINE BY ACTIVATED HUMAN-NEUTROPHILS - A MYELOPEROXIDASE-MEDIATED PROCESS

  • 1 January 1980
    • journal article
    • research article
    • Vol. 96  (5) , 893-902
Abstract
Zymosan-activated neutrophils incorporated large amounts of [3H]glucosamine into TCA[trichloroacetic acid]-precipitable material as compared with resting cells. The burst of glucosamine incorporation began 2 min after zymosan exposure and lasted 3-5 min, after which the incorporation rate returned to that of resting cells. Studies with cells from patients with chronic granulomatous disease and hereditary myeloperoxidase deficiency as well as experiments with inhibitors indicated that glucosamine incorporation required both the respiratory burst and the myeloperoxidase system. SDS[sodium dodecyl sulfate]-polyacrylamide gel electrophoresis of [3H]glucosamine-containing TCA precipitates from zymosan-activated cells revealed radioactivity migrating throughout the length of the gel. The radioactivity in precipitates from resting cells or cells activated in the presence of a small amount of a myeloperoxidase inhibitor was found in a peak migrating close to the tracking dye. Zymosan-activated neutrophils are able to incorporate glucosamine into protein by a process dependent on H2O2 and myeloperoxidase. The biosynthetic significance of this phenomenon is not certain, but it most likely represents the reaction of amino sugar with macromolecular degradation products formed by the action of the myeloperoxidase system on cellular and particulate constituents.