Cathepsin D-like activity in neutrophils and monocytes

Monocytes-macrophages and polymorphonuclear leukocytes contain an acid proteolytic enzyme that cleaves tritiated hemoglobin. The monocyte-macrophage-derived enzymatic activity was completely inhibited by pepstatin A, a property of cathepsin D. Monocyte-derived macrophages developed detectable cathepsin D-like activity after 5 days in culture, and this activity coincided with the appearance of other known indicators of macrophage maturation. The cathepsin D activity further increased significantly with time after day 5 of culture. The proteinase activity extracted from neutrophils was only partially inhibitable by pepstatin A, which indicates that this activity is contributed by more than one proteolytic enzyme, including cathepsin D. Cathepsin D activity demonstrated in neutrophils and macrophages may be an important marker of phagocyte function.