Localization of the thiorphan-sensitive endopeptidase, termed enkephalinase A, on glial cells.

Degradation of tritiated Leu-enkephalin was studied in cultures of primary astrocytes from rat brain. The incubation experiments with a cell suspension revealed Tyr as the main tritiated metabolite; however, Tyr-Gly-Gly and Tyr-Gly were detectable as well. Using a crude membrane preparation of the astrocytes, we found about equal amounts of Tyr and Tyr-Gly-Gly but only trace quantities of Tyr-Gly. The production of Tyr was completely inhibited by bestatin, an inhibitor of aminopeptidases, that of Tyr-Gly-Gly by thiorphan, a specific inhibitor of enkephalinase A. The results prove the ability of glial cells to degrade enkephalin by aminopeptidase and a membrane-bound enkephalinase A.