Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 5 June 1981:
Vol. 212. no. 4499, pp. 1153 - 1155
DOI: 10.1126/science.7015510
Prev | Table of Contents | Next

Articles

Science, Vol 212, Issue 4499, 1153-1155
Copyright © 1981 by American Association for the Advancement of Science

articles

Selective protection of methionine enkephalin released from brain slices by enkephalinase inhibition

G Patey, S De La Baume, JC Schwartz, C Gros, B Roques, MC Fournie-Zaluski, and E Soroca-Lucas

Methionine enkephalin release was evoked by depolarization of slices from rat striatum with potassium. In the presence of 0.1 microM thiorphan [(N(R,S)-3-mercapto-2-benzylpropionyl)glycine], a potent inhibitor of enkephalin dipeptidyl carboxypeptidase (enkephalinase), the recovery of the pentapeptide in the incubation medium was increased by about 100 percent. A similar effect was observed with the dipeptide phenylalanylalanine, a selective although less potent enkephalinase inhibitor. Inhibition of other known enkephalin-hydrolyzing enzymes--aminopeptidase by 0.1 mM puromycin or angiotensin-converting enzyme by 1 microM captopril--did not significantly enhance the recovery of released methionine enkephalin. These data indicate that enkephalinase is critically involved in the inactivation of the endogenous opioid peptide released from striatal neurons.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The Kell Protein of the Common K2 Phenotype Is a Catalytically Active Metalloprotease, whereas the Rare Kell K1 Antigen Is Inactive: IDENTIFICATION OF NOVEL SUBSTRATES FOR THE KELL PROTEIN.
A. Claperon, C. Rose, P. Gane, E. Collec, O. Bertrand, and T. Ouimet (2005)
J. Biol. Chem. 280, 21272-21283
   Abstract »    Full Text »    PDF »
CD10-positive Stromal Cells in Gastric Carcinoma: Correlation with Invasion and Metastasis.
W.-B. Huang, X.-J. Zhou, J.-Y. Chen, L.-H. Zhang, K. Meng, H.-H. Ma, and Z.-F. Lu (2005)
Jpn. J. Clin. Oncol. 35, 245-250
   Abstract »    Full Text »    PDF »
A Three-dimensional Model of the Neprilysin 2 Active Site Based on the X-ray Structure of Neprilysin: IDENTIFICATION OF RESIDUES INVOLVED IN SUBSTRATE HYDROLYSIS AND INHIBITOR BINDING OF NEPRILYSIN 2.
S. Voisin, D. Rognan, C. Gros, and T. Ouimet (2004)
J. Biol. Chem. 279, 46172-46181
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)