Phagocytosing XXXX neutrophils inactivate their own granular enzymes.

@entity1 @entity4514 @entity2769 @entity26 @entity2041 @entity2196 @entity224 @entity34201 @entity1117
During @entity34201 , neutrophils generate reactive @entity26 metabolites and release lysosomal enzymes into the extracellular medium. We have investigated the possibility that these enzyme are inactivated by the @entity26 compounds. Phagocytosing neutrophils from 12 @entity1 with @entity1117 , which do not generate these @entity26 metabolites, released two to three times more activity of lysozyme and beta-glucuronidase than did normal neutrophils. This difference proved to be due to a decrease of approximately 20% of the total activity of these enzymes in normal neutrophils, but not in neutrophils of @entity1 with @entity1117 . This inactivation of enzymes took place during @entity34201 of opsonized zymosan particles as well as during stimulation of normal cells with @entity4514 . The inactivation was not due to formation of inhibitors. The lysosomal enzymes were not activated when the neutrophils were stimulated under anaerobic conditions. Addition of @entity2196 , @entity224 dismutase, or albumin gave no protection against the oxidative damage; reduced @entity2041 gave partial protection. The oxidative inactivation was more pronounced in the presence of @entity2769 . Measurement of the activity and the amount of protein of acid alpha-glucosidase in the cells showed that the specific activity of this enzyme decreased by approximately 50% during 30 min of @entity34201 . This indicates that the inactivation of the lysosomal enzymes takes place in the phagolysosomes, before the enzymes have leaked into the extracellular medium.
