INDUCTION OF LYSOSOMAL ENZYME ACTIVITIES WITH GLUCOCORTICOIDS DURING DIFFERENTIATION OF CULTURED MOUSE MYELOID LEUKEMIA CELLS

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  • Induction of Lysosomal Enzyme Activitie

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The activities of lysosomal enzymes, such as lysozyme, acid protease, and β-glucuronidase, were induced with glucocorticoids during differentiation of cultured mouse myeloid leukemia line cells (M1). The induction of lysozyme activity accompanied by phagocytosis in M1 cells was most pronounced in these lysosomal enzymes. Although lysozyme activity could not be detected in undifferentiated cells, it showed a marked increase from the second day of incubation of M1 cells with dexamethasone. On the 5th day of incubation, the activity was about one-half that of mouse peritoneal macrophages.<br>There was a competitive interaction among different steroids on induction of lysozyme activity in M1 cells. 11β-Hydroxyprogesterone and 11-deoxycortisol could not induce the maximal level of the activity, and cortisone and fluoxymesterone were not active in inducing the enzyme activity. However, these steroids inhibited the induction of enzyme activity with dexamethasone, prednisolone, or hydrocortisone. Induction of lysozyme activity and phagocytic activity of M1 cells with dexamethasone was inhibited by 5-bromodeoxyuridine or puromycin at a concentration that did not interfere with the growth of cells. Differentiation could not be induced in DR-6 cells isolated from M1 cells even in a high concentration of dexamethasone. Neither lysozyme activity nor other lysosomal enzyme activities could be induced in DR-6 cells with dexamethasone.<br>These results indicate that glucocorticoids are capable of inducing some lysosomal enzyme activities as well as morphological and functional differentiation in M1 cells, and among these enzymes, lysozyme activity is a fairly suitable biochemical marker for the differentiation of M1 cells.

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