Abstract

(Na + + K +)ATPase activity in cerebral cortex was modulated by insulin action depending on the Mg 2+ concentration. Thus, in homogenates in the presence of 1–3 mM Mg 2+, insulin stimulated the enzyme, whereas in the presence of 4–6 mM Mg 2+ inhibition was observed. Exposure of synaptosomal membranes to the soluble fraction resulted in inhibition of ATPase activity in a dose-dependent manner. The inhibitory effect of insulin was regulated by a cytoplasmic factor in a dose-dependent manner. Similar variations to those obtained with a crude synaptosomal fraction were obtained by using a partially purified ATPase. These results indicated the importance of soluble factors in the modulation of ATPase by insulin and add more evidence in support for a role of insulin as a neuromodulator.

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