Protein & Peptide Letters

Prof. Ben M. Dunn  
Department of Biochemistry and Molecular Biology
University of Florida
College of Medicine
P.O. Box 100245
Gainesville, FL
USA
Email: bdunn@ufl.edu

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

Author(s): Veronique Hospital, Annik Prat.

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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Article Details

VOLUME: 11
ISSUE: 5
Year: 2004
Page: [501 - 508]
Pages: 8
DOI: 10.2174/0929866043406508
Price: $58