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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Nardilysin, A Basic Residues Specific Metallopeptidase That Mediates Cell Migration and Proliferation

Author(s): Veronique Hospital and Annik Prat

Volume 11, Issue 5, 2004

Page: [501 - 508] Pages: 8

DOI: 10.2174/0929866043406508

Price: $65

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Abstract

Nardilysin (NRDc), a metallopeptidase of the M16 family, presents, in vitro, cleavage specificity for basic residues. Depending on the cell type, it is cytoplasmic, exported or cell surface associated. As a new receptor for heparin-binding EGF-like growth factor (HB-EGF), NRDc was recently shown to be involved in cellular migration and proliferation. Since for those processes its enzymatic activity is not required, it is now evident that nardilysin fulfills at least two distinct functions, i.e. an HB-EGF modulator and a peptidase.

Keywords: nardilysin, acidic domain, hb-egf binding, soluble metallopeptidase, multiple subcellular, localization


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