These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Inactivation of neurotensin and neuromedin N by Zn metallopeptidases. Author: Kitabgi P. Journal: Peptides; 2006 Oct; 27(10):2515-22. PubMed ID: 16904239. Abstract: The two related peptides neurotensin (NT) and neuromedin N (NN) are efficiently inactivated by peptidases in vitro. Whereas NT is primarily degraded by a combination of three Zn metallo-endopeptidases, namely endopeptidases 24.11, 24.15 and 24.16, in all systems examined, NN is essentially inactivated by the Zn metallo-exopeptidase aminopeptidase M. In this paper we review the work that has led to the identification of the NT- and NN-degrading enzymes and to the purification and cloning of EP 24.16, a previously unidentified peptidase. We provide a brief description of the three NT-inactivating endopeptidases and of their specific and mixed inhibitors, some of them developed in the course of studying NT degradation. Finally, we review in vivo data obtained with these inhibitors that strongly support a physiological role for EP 24.11, 24.15 and 24.16 in the termination of NT-generated signals and for aminopeptidase in terminating NN action. Knowledge of the NT and NN inactivation mechanisms offers the perspective to develop metabolically stable analogs of these peptides with potential therapeutic value.[Abstract] [Full Text] [Related] [New Search]