There is disagreement in the literature whether or not deoxyglucose accumulation, a measure of glycolytic activity, is increased in astrocytes during exposure to elevated concentrations of the potassium ion (K+). In the present work we have confirmed our previous finding that deoxyglucose accumulation in primary cultures of well-differentiated mouse astrocytes shows a robust increase when the K+ concentration in the incubation medium is raised to or above 12 mM. This response is inhibited by ouabain (with a half-maximum effect at approximately 0.1 mM), indicating that it is a metabolic manifestation of the activity of an Na(+)-K(+)-ATPase. The stimulation at this high level of K+ indicates a remarkably low K+ affinity of the Na(+)-K(+)-ATPase involved, enabling it to be activated by above-normal concentrations of K+. At a resting concentration of K+ (5.4 mM), at least one half of the deoxyglucose accumulation is also a reflection of Na(+)-K(+)-ATPase activity, as shown by its susceptibility to inhibition by ouabain. Ouabain has some effect even at a concentration of 0.1 microM, indicating participation of not only the alpha 1 isoform which has a low affinity to ouabain, but also of the alpha 2 isoform, which has a high affinity. The stimulatory effect of elevated K+ is absent in immature astrocytes and only develops after prolonged time in culture. It could not be evoked in a seemingly similar culture of rat astrocytes, which has previously been shown to lack Na(+)-K(+)-ATPase activity as well as the alpha 2 isoform of the ATPase. This isoform has unequivocally been found to be expressed by astrocytes in situ.
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Peng et al. (2007) studied this question.