Enkephalin metabolism in brain and its inhibition.
Various cerebral peptidases are able to hydrolyse the enkephalins into inactive fragments. Among these enzymes enkephalin-dipeptidylcarboxypeptidase ("enkephalinase") inhibited by thiorphan and a bestatin-sensitive aminopeptidase activity seem to play a key-role as "inactivating neuropeptidases". Their inhibition, in vitro as well as in vivo, leads to a protection of endogenous enkephalins and to antinociceptive effects.
D000626:Aminopeptidases / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000187:drug effects / Q000201:enzymology*; D010450:Endopeptidases / Q000378:metabolism; D004745:Enkephalins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D015260:Neprilysin; D009619:Nociceptors / Q000187:drug effects; D010447:Peptide Hydrolases / Q000378:metabolism*; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism; D011480:Protease Inhibitors / Q000494:pharmacology*; D051381:Rats
D004745:Enkephalins; D011480:Protease Inhibitors; D010450:Endopeptidases; D010447:Peptide Hydrolases; D000626:Aminopeptidases; D007703:Peptidyl-Dipeptidase A; D015260:Neprilysin