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

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

Document Type: Review Article

Affiliations: Unite de Chimie Organique, Institut Pasteur,25, rue du Docteur Roux, 75724 Paris Cedex 15.

Publication date: 2004-10-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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