Recombinant neutral endopeptidase-24.11 expressed in mouse neuroblastoma cells is associated with neurite membranes

Author:

Lemay G1,Zollinger M1,Waksman G123,Roques B P1,Crine P13,Boileau G1

Affiliation:

1. Département de Biochimie, Faculté de Médecine, Université de Montréal, Montréal, Québec, H3C 3J7, Canada.

2. Département de Chimie Organique, U. 266 Institut de la Santé et de la Recherche Médicale, U.A. 498 and Centre National de la Recherche Scientifique, Faculté de Pharmacie, 75006 Paris, France.

3. Groupe de Recherche en Transport Membranaire, Université de Montréal, Montréal, Québec H3C 3J7, Canada.

Abstract

Neutral endopeptidase-24.11 (EC 3.4.24.11) (NEP) is a transmembrane metallo-endopeptidase that has been shown to be involved in the degradation of several mammalian neuropeptides, including enkephalins. The enzyme has recently been found to be specifically associated with the axonal and synaptic membranes of neurons in the globus pallidus of the pig brain. This result suggests that neurons must possess mechanisms for targeting NEP to particular membrane domains. Study of these mechanisms would greatly benefit from the existence of an established neuron-like cell line capable of expressing and targeting NEP to specific membrane domains. For this reason we have used a retroviral vector containing the cDNA for rabbit kidney NEP to express this enzyme in a mouse neuroblastoma cell line (Neuro2A). Labelling of the cell surface with an antibody coupled to colloidal gold particles and examination of the cells by electron microscopy revealed a non-uniform distribution of NEP at the surface of the cells, the protein being preferentially associated with the membrane of neurites compared with the cell body. This observation suggests that Neuro2A cells possess a mechanism for targeting NEP to specific domains of the plasma membrane. This cell line could thus constitute a good model for studying the mechanisms responsible for targeting this enzyme to specialized regions of the plasma membrane.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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