Effect of muramyldipeptide, a synthetic bacterial adjuvant, on enzyme release from cultured mouse macrophages.
Monolayer cultures of macrophages obtained by peritoneal lavage of normal or thioglycollate-stimulated mice spontaneously secreted lysosomal enzymes into the culture medium. When the elicited macrophages were cultured in the presence of muramyldipeptide (MDP), a 20-30% increase in the release of beta-glucuronidase was consistently observed and the intracellular activity decreased to about 45% of that of control cells after 6-8 days' culture. A stimulatory effect of MDP on lysozyme secretion, though less profound, was also observed. In contrast, release of neither enzyme was stimulated in resident macrophages by the addition of MDP. A neutral alpha-glucosidase, which has recently been found to localize also in granules of macrophages, remained inside the cells and neither its activity nor its release was affected by the addition of MDP to either type of macrophages. A large amount of lactic dehydrogenase was released only when the resident, not the elicited, macrophages were cultured for 3-4 days and then phagocytosed zymosan.
D000119:Acetylmuramyl-Alanyl-Isoglutamine / Q000494:pharmacology*; D000818:Animals; D002478:Cells, Cultured; D005260:Female; D005947:Glucose / Q000378:metabolism; D005966:Glucuronidase / Q000378:metabolism; D006020:Glycopeptides / Q000494:pharmacology*; D006867:Hydrolases / Q000378:metabolism*; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D008264:Macrophages / Q000187:drug effects / Q000201:enzymology*; D051379:Mice; D008807:Mice, Inbred BALB C; D009113:Muramidase / Q000378:metabolism; D010587:Phagocytosis; D000520:alpha-Glucosidases / Q000378:metabolism
D006020:Glycopeptides; D000119:Acetylmuramyl-Alanyl-Isoglutamine; D007770:L-Lactate Dehydrogenase; D006867:Hydrolases; D009113:Muramidase; D000520:alpha-Glucosidases; D005966:Glucuronidase; D005947:Glucose