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Neurolysin: From Initial Detection to Latest Advances

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Abstract

The mechanisms by which peptidergic signals are terminated have been the center of multiple studies leading to the discoveries of novel proteolytic activities. When studying the catabolic fate of neurotensin (NT) in brain and gastrointestinal tract, we detected a novel activity belonging to the metallopeptidases class and apparently distinct from previously known enzymes. Purification and cloning confirmed that this NT-degrading neutral metalloendopeptidase activity was indeed original. It was named endopeptidase 3.4.24.16 according to the IUBMB nomenclature and later, referred to as neurolysin. This review tells the history of neurolysin from its initial detection to its purification, cloning, design of specific inhibitors as well as in vitro and in vivo pharmacological studies aimed at delineating its role in the control of NT function. Finally, we discuss very recent advances suggesting a potential role of neurolysin in pathologies.

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Authors and Affiliations

  1. Université Côte d’Azur, INSERM, CNRS, IPMC, UMR7275, Team Labeled «Laboratory of Excellence (Labex) DISTALZ», 660 Route des Lucioles, 06560, Sophia-Antipolis, Valbonne, France

    Frédéric Checler

  2. Department of Pharmacology, Biomedical Science Institute, University of São Paulo, Av. Prof. Lineu Prestes 1524, Sala 317, São Paulo, SP, 05508-000, Brazil

    Emer S. Ferro

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  1. Frédéric Checler
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Correspondence to Frédéric Checler.

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Checler, F., Ferro, E.S. Neurolysin: From Initial Detection to Latest Advances. Neurochem Res 43, 2017–2024 (2018). https://doi.org/10.1007/s11064-018-2624-6

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