Inactivation of neurotensin by rat brain synaptic membranes partly occurs through cleavage at the Arg8-Arg9 peptide bond by a metalloendopeptidase.
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-amino -benzoate, which exerts an inhibition on NT1-8 formation with an IC50 (0.6 microM) close to its Ki for the purified metalloendopeptidase (1.94 microM). Furthermore, we established the role of a postproline dipeptidyl-aminopeptidase in the secondary processing of NT9-13 formation.
D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine; D001921:Brain / Q000201:enzymology*; D010450:Endopeptidases / Q000378:metabolism*; D007700:Kinetics; D008666:Metalloendopeptidases; D009496:Neurotensin / Q000037:antagonists & inhibitors / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity; D013570:Synaptic Membranes / Q000201:enzymology*
D009496:Neurotensin; D001120:Arginine; D010450:Endopeptidases; D008666:Metalloendopeptidases