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  • Title: Localization of the thiorphan-sensitive endopeptidase, termed enkephalinase A, on glial cells.
    Author: Lentzen H, Palenker J.
    Journal: FEBS Lett; 1983 Mar 07; 153(1):93-7. PubMed ID: 6337881.
    Abstract:
    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.
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