Induction of macrophage lysosomal enzyme secretion by agents acting at the plasma membrane.
Cultured mouse peritoneal macrophages were shown to secrete the lysosomal enzyme N-acetyl-glucosaminidase (N-ac-Glu) in response to IgG-Sepharose and some other non-endocytosable particles without substantial release of the cytoplasmic enzyme, lactate dehydrogenase. The interaction with IgG-Sepharose was studied in some detail, and was shown to be time- and dose-dependent, and to leave the cells viable. Ovalbumin and glycine insolubilised on Sepharose did not induce secretion. By means of several control experiments, it was demonstrated that the IgG-Sepharose exerted its effects directly on the plasma membrane. Thus, normal macrophages can secrete in response to certain agents which act solely on the plasma membrane. This mechanism of induction of secretion is probably quite distinct from those previously established, which involve secretion during phagocytosis, during intracellular storage of phagocytosed materials or during pharmacological intervention by cytochalasin B.
D000118:Acetylglucosaminidase / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000502:physiology; D006596:Hexosaminidases / Q000378:metabolism*; D007074:Immunoglobulin G; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D008247:Lysosomes / Q000201:enzymology*; D008264:Macrophages / Q000201:enzymology* / Q000648:ultrastructure; D051379:Mice; D011961:Receptors, Fc; D012685:Sepharose
D007074:Immunoglobulin G; D011961:Receptors, Fc; D012685:Sepharose; D007770:L-Lactate Dehydrogenase; D006596:Hexosaminidases; D000118:Acetylglucosaminidase