Enkephalin-degrading enzymes and angiotensin-converting enzyme in human and rat meninges.
The neutral endopeptidase NEP 24.11 (enkephalinase) has been visualized in human spinal cord by in vitro autoradiography using [3H]HACBO-Gly as a radiolabelled probe. The specific binding was present in the substantia gelatinosa and particularly dense in meninges surrounding the spinal cord. Enzymatic studies using [3H][D-Ala2, Leu]enkephalin as substrate confirmed the presence of NEP in dura and pia mater of human tissue. In addition, the human meninges were shown to contain high concentrations of angiotensin-converting enzyme (ACE) and aminopeptidases. The three enzymes have also been detected in rat tissues but their distribution pattern differs from that of human tissue. In dura mater, 45% of the [Leu]enkephalin hydrolysis was due to enkephalinase and 38% to bestatin-sensitive aminopeptidases. In contrast in pia mater aminopeptidases were more efficient in hydrolyzing enkephalin. The possible role of these enzymes in the meninges could be to maintain the homeostatic concentration of neuropeptides in the central nervous system.
D000110:Acetylcholinesterase / Q000378:metabolism; D000626:Aminopeptidases / Q000378:metabolism; D000818:Animals; D010450:Endopeptidases / Q000378:metabolism*; D004743:Enkephalin, Leucine / Q000378:metabolism; D006801:Humans; D008578:Meninges / Q000201:enzymology*; D015260:Neprilysin; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D051381:Rats; D013116:Spinal Cord / Q000201:enzymology
D004743:Enkephalin, Leucine; D000110:Acetylcholinesterase; D010450:Endopeptidases; D000626:Aminopeptidases; D007703:Peptidyl-Dipeptidase A; D015260:Neprilysin