title: Peptidases involved in the inactivation of exogenous and endogenous enkephalins.
abstract: 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.
mesh_terms: D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D010450:Endopeptidases / Q000378:metabolism*; D004745:Enkephalins / Q000378:metabolism*; D007930:Leucine / Q000031:analogs & derivatives / Q000494:pharmacology; D051379:Mice; D015260:Neprilysin; D009619:Nociceptors / Q000378:metabolism; D051381:Rats; D015244:Thiorphan; D008625:Tiopronin / Q000031:analogs & derivatives / Q000494:pharmacology
chemical_list: D004745:Enkephalins; D015244:Thiorphan; D008625:Tiopronin; D010450:Endopeptidases; D000626:Aminopeptidases; D015260:Neprilysin; D007930:Leucine; C012211:ubenimex