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Reversible inhibition of the norepinephrine induction of lactate dehydrogenase by cytochalasin B in rat glial C6 cells
Author(s) -
Bennett Kimberly,
De Vellis Jean
Publication year - 1977
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1040930211
Subject(s) - cytochalasin b , lactate dehydrogenase , cytochalasin , intracellular , norepinephrine , cytochalasin d , chemistry , biology , enzyme , microbiology and biotechnology , medicine , endocrinology , biochemistry , cell , cytoskeleton , dopamine
Abstract The cyclic AMP mediated induction of lactate dehydrogenase (LDH: E.C. 1.1.1.27) activity by norepinephrine in the rat glial cell line C6 is inhibited by cytochalasin B. Doses of 5, 15, and 25 μg/ml of cytochalasin B inhibited the induction equally. Twenty‐five μg/ml of cytochalasin B inhibited the induction reversibly, and had no effect on basal enzyme level. No effect of cytochalasin B on general protein synthesis was found, nor did it increase the rate of decline of enzyme activity in deinduced cells. It therefore appears to block LDH induction by selectively inhibiting its synthesis. Cytochalasin B had no effect on the transient (intracellular and extracellular) rise in cyclic AMP generated in response to norepinephrine treatment. Cytochalasin B was effective when added during the transcription dependent phase (first 3 hours) but not during the translation dependent phase (after 3 hours) of LDH induction. The suggestion is discussed that cytochalasin B inhibits one of the early events of the inductive process.