Histochemical mapping of the substrate for brain-stimulation reward with glycogen phosphorylase

Glycogen phosphorylase is the enzyme that regulates glycogenolysis and it appears that there is a relationship between central levels of glycogen and neuronal activity, which is influenced by a variety of neurotransmitters. In the present study, glycogen phosphorylase histochemistry was used to correlate changes in metabolic activity in response to rewarding lateral hypothalamic stimulation. Rats were allowed to self-stimulate for 1 h per day for ten consecutive days following which postmortem phosphorylase a activity was examined. Significant differences in optical density between the stimulated and contralateral hemispheres were found in three of the eight analyzed structures, two of which, the diagonal band of Broca and the caudate nucleus, showed a greater density of glycogen phosphorylase a on the stimulated side and the third, the habenula, had greater contralateral activity. In conclusion, our data suggest that glycogen phosphorylase activity is a viable but not weighty marker of energy alterations induced by chronic exposure to intracranial self-stimulation, and that it is generally consistent with the patterns revealed by other metabolic indices such as cytochrome oxidase and 2-deoxyglucose autoradiography.