Summary
Among the various cerebral enzyme activities able to hydrolyse the enkephalins into inactive fragments only two seem responsible for the metabolism of the endogenous opioid peptides: a dipeptidylcarboxypeptidase (“enkephalinase”), and a bestatin-sensitive aminopeptidase. Their inhibition by thiorphan and bestatin results in an antinociceptive effect observed in tests in which the nociceptive stimulation is probably accompanied by a concomittent release of enkephalins.
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References
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Schwartz, J.C., de la Baume, S., Yi, C.C., Chaillet, P., Marcais-Collado, H., Costentin, J. (1983). Peptidases Involved in the Inactivation of Exogenous and Endogenous Enkephalins. In: Goldstein, M., Jellinger, K., Riederer, P. (eds) Basic Aspects of Receptor Biochemistry. Journal of Neural Transmission, vol 18. Springer, Vienna. https://doi.org/10.1007/978-3-7091-4408-4_22
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DOI: https://doi.org/10.1007/978-3-7091-4408-4_22
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