Inactivation of Neurotensin by Rat Brain Synaptic Membranes Partly Occurs Through Cleavage at the Arg8‐Arg9 Peptide Bond by a Metalloendopeptidase

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Abstract
One of the primary inactivating cleavages of neurotensin (NT) by rat brain synaptic membranes occurs at the Arg8‐Arg9 peptide bond, leading to the formation of NT1‐8 and NT9‐13. The involvement at this site of a recently purified metalloendopeptidase was demonstrated by the use of its specific inhibitor, N‐[1(R,S)‐carboxy‐2‐phenylethyl]‐alanylalanylphenylalanine‐p‐aminobenzoate, which exerts an inhibition on NT1‐8 formation with an IC50 (0.6 μM) close to its Ki for the purified metalloendopeptidase (1.94 μM). Furthermore, we established the role of a postproline dipeptidyl‐aminopeptidase in the secondary processing of NT9‐13 formation.