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Enkephalin‐degrading enzymes and angiotensin‐converting enzyme in human and rat meninges
Author(s) -
Zajac Jean-Marie,
Charnay Yves,
Soleilhac Jean-Marc,
Sales Nicole,
Roques Benard P.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80768-8
Subject(s) - enkephalinase , meninges , enzyme , neprilysin , endopeptidase , spinal cord , pia mater , central nervous system , chemistry , enkephalin , human brain , dura mater , neuropeptide , biochemistry , aminopeptidase , biology , endocrinology , anatomy , receptor , neuroscience , amino acid , opioid , leucine
The neutral endopeptidase NEP 24.11 (enkephalinase) has been visualized in human spinal cord by in vitro autoradiography using [ 3 H]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 [ 3 H][D‐Ala 2 , 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.