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  • Title: Enkephalin degradation by enkephalinergic neuroblastoma cells. Involvement of angiotensin-converting-enzyme.
    Author: Palenker J, Lentzen H, Brandt U.
    Journal: Naunyn Schmiedebergs Arch Pharmacol; 1984 Mar; 325(3):214-7. PubMed ID: 6328331.
    Abstract:
    Degradation of tritiated [Leu5]enkephalin was studied in cultures of neuroblastoma cells (clone N1E-115). Incubation of cells in suspension revealed Tyr as the main tritiated metabolite; however, Tyr-Gly-Gly and Tyr-Gly were detectable as well. In a crude membrane preparation of the neuroblastoma cells the level of Tyr is reduced to 13% and that of Tyr-Gly to 10% of the initial value, whereas Tyr-Gly-Gly is increased to about 5 times the initial value. Of the degraded enkephalin, 66% was accounted for by the formation of Tyr, 30% by the formation of Tyr-Gly-Gly and 4% by the formation of Tyr-Gly. The production of Tyr was inhibited by bestatin, an inhibitor of aminopeptidases, and that of Tyr-Gly-Gly by captopril, an inhibitor of angiotensin-converting-enzyme. The results prove the ability of neuroblastoma cells (N1E-115) to degrade enkephalin by aminopeptidase and the membrane-bound angiotensin-converting-enzyme.
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