Neuropeptides and their peptidases: Functional considerations |
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| Institution: | 1. Department of Analytical Chemistry, Faculty of Chemistry, Universitat de València, Dr Moliner 50, 46100, Burjassot, Valencia, Spain;2. Institute of Material Science (ICMUV), Universitat de València, Catedrático José Beltrán 2, 46980 Paterna, Valencia, Spain;1. Center for Material Cycles and Waste Management Research, National Institute for Environmental Studies (NIES), 16-2 Onogawa, Tsukuba 305-8506, Japan;2. Graduate School of Frontier Sciences, The University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa 277-8563, Japan;3. Faculty of Applied Life Sciences, Niigata University of Pharmacy and Applied Life Sciences, 265-1, Higashijima, Akiha-ku, Niigata 956-8603, Japan;1. Université de Rennes 1, Ecole Nationale Supérieure de Chimie de Rennes, CNRS, UMR 6226, 11 allée de Beaulieu, CS 50837, 35708 Rennes Cedex 7, France;2. Ecole Nationale Supérieure de Chimie de Rennes, CNRS, UMR 6226, 11 allée de Beaulieu, CS 50837, 35708 Rennes Cedex 7, France;3. Unité de recherche de Catalyse d''Electrochimie de Nanomatériaux et leurs applications et de didactique CENAD, Institut National des Sciences Appliquées et de Technologie (INSAT), B.P.N°676, 1080 Tunis Cedex, Tunisie;4. Université Européenne de Bretagne, 5 boulevard Laënnec, 35000, France |
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| Abstract: | The properties of the various brain membrane peptidases capable of hydrolysing released neuropeptides are reviewed, with particular emphasis on endopeptidase-24.11 and angiotensin converting enzyme. The substrate specificities of both enzymes are defined and their relative contribution to the degradation of tachykinins in vitro are considered. One approach to assessing the physiological roles of identified peptidases involves examining the protective effect of selective peptidase inhibitors on the degradation of peptides released from brain slices. This procedure has been applied to study the release of substance P-like immunoreactivity from slices of rat substantia nigra. Inhibition of endopeptidase-24.11, but not of angiotensin converting enzyme, produces a significant increase in recovery of substance P. The specificity and distribution of endopeptidase-24.11 would therefore not be inconsistent with a role in the physiological inactivation of tachykinins, as well as enkephalins. At peripheral sites, LHRH and atrial natriuretic peptide may be important substrates of the enzyme. The endogenous neuropeptide substrate(s) for striatal angiotensin converting enzyme remain unclear. |
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