Abstract
We recently reported1 that adrenaline treatment of the perfused rat heart produced a marked activation of phosphofructokinase when assayed at low substrate concentration using a new isotopic assay2. As muscle phosphofructokinase has been reported to be phosphorylated by the cyclic AMP-dependent protein kinase3, activation of phosphofructokinase might be expected to result from phosphorylation mediated by the β-receptor/adenylate cyclase/cyclic AMP-dependent protein kinase sequence. We now report that this is not so, but that activation of phosphofructokinase in the perfused rat heart occurs independently of phosphorylase activation, by a cyclic AMP-independent mechanism, and that this process seems to be mediated predominantly through the α-adrenergic receptors. We believe this represents the first example showing that not only in liver4,5, but also in a muscular tissue, occupancy of an α-adrenergic receptor changes the activity of a glycolytic enzyme. In addition, the present findings imply a coordination of muscle glycolysis with hepatic glucose output.
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