Modulation of lysosomal protease-esterase and lysozyme in Kupffer cells and peritoneal macrophages infected with Nocardia asteroides.
Virulent Nocardia asteroides reduces lysosomal acid phosphatase activity in murine macrophages. A computer-assisted imaging photometry system was used to quantitate lysozyme and nonspecific esterase-neutral protease levels within individual macrophages following ingestion of nocardiae. In contrast to acid phosphatase, lysozyme and esterase-neutral protease activity was either unchanged or increased following infection by increasing numbers of nocardial cells.
D000135:Acid Phosphatase / Q000378:metabolism; D000818:Animals; D043182:Carboxylesterase; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism; D007728:Kupffer Cells / Q000201:enzymology* / Q000382:microbiology; D008247:Lysosomes / Q000201:enzymology; D008264:Macrophages / Q000201:enzymology*; D051379:Mice; D009113:Muramidase / Q000378:metabolism; D009617:Nocardia Infections / Q000201:enzymology*; D009616:Nocardia asteroides; D010447:Peptide Hydrolases / Q000378:metabolism; D010529:Peritoneal Cavity
D002265:Carboxylic Ester Hydrolases; D043182:Carboxylesterase; D000135:Acid Phosphatase; D009113:Muramidase; D010447:Peptide Hydrolases