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Reversible inhibition of the norepinephrine induction of lactate dehydrogenase by cytochalasin B in rat glial C6 cells

✍ Scribed by Kimberly Bennett; Jean De Vellis

Publisher
John Wiley and Sons
Year
1977
Tongue
English
Weight
673 KB
Volume
93
Category
Article
ISSN
0021-9541

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✦ Synopsis

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.

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