Enkephalin‐degrading enzymes and angiotensin‐converting enzyme in human and rat meninges

FEBS Letters

Zajac, Jean-Marie¹  Sales, Nicole³  Roques, Benard P.¹  Charnay, Yves²  Soleilhac, Jean-Marc¹ 

[1] Département de Chimie Organique, U266 INSERM, UA 498 CNRS, UER des Sciences Pharmaceutiques et Biologiques, 4 avenue de l'Observatoire, 75006 Paris France;Laboratoire d'Histologie et Embryologie, UA 559 CNRS, Faculté de Médecine Lyon Sud, 69600 Oullins France;Laboratoire de Physiologie, UER des Sciences Pharmaceutiques et Biologiques, 4 avenue de l'Observatoire, 75006 Paris, France

关键词: Enkephalin;    Enkephalinase;    Angiotensin-converting enzyme;    Meninges;    Autoradiography;    (Human tissue);    NEP;    neutral endopeptidase;    ACE;    angiotensin-converting enzyme;    HACBO-Gly;    [(2RS)-3-hydroxyaminocarbonyl-2-benzyl-1-oxopropyl]glycine;   

DOI  :  10.1016/0014-5793(87)80768-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown