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
Protein & Peptide Letters
Title: Nardilysin, A Basic Residues Specific Metallopeptidase That Mediates Cell Migration and Proliferation
Volume: 11 Issue: 5
Author(s): Veronique Hospital and Annik Prat
Affiliation:
Keywords: nardilysin, acidic domain, hb-egf binding, soluble metallopeptidase, multiple subcellular, localization
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.
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Cite this article as:
Hospital Veronique and Prat Annik, Nardilysin, A Basic Residues Specific Metallopeptidase That Mediates Cell Migration and Proliferation, Protein & Peptide Letters 2004; 11 (5) . https://dx.doi.org/10.2174/0929866043406508
DOI https://dx.doi.org/10.2174/0929866043406508 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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