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First published online October 30, 2009
Journal of Experimental Biology 212, 3673-3683 (2009)
Published by The Company of Biologists 2009
doi: 10.1242/jeb.034272

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Neprilysin 4, a novel endopeptidase from Drosophila melanogaster, displays distinct substrate specificities and exceptional solubility states

Heiko Meyer¹, Mareike Panz¹, Monika Zmojdzian², Krzysztof Jagla² and Achim Paululat^1,*

¹ Department of Zoology/Developmental Biology, University of Osnabrück, Barbarastraße 11, 49069 Osnabrück, Germany
² Unité Mixte de Recherche, CNRS 6247-GreD, Clermont-Ferrand University, INSERM Clermont-Ferrand, 28 Place Henri Dunant, F-63000 Clermont-Ferrand, France

^* Author for correspondence (paululat{at}biologie.uni-osnabrueck.de)

Accepted 10 August 2009

Proteins belonging to the family of neprilysins are typically membrane bound M13 endopeptidases responsible for the inactivation and/or activation of peptide signaling events on cell surfaces. Mammalian neprilysins are known to be involved in the metabolism of various regulatory peptides especially in the nervous, immune, cardiovascular and inflammatory systems. Although there is still much to learn about their participation in various diseases, they are potential therapeutic targets. Here we report on the identification and first characterization of neprilysin 4 (NEP4) from Drosophila melanogaster. Reporter lines as well as in situ hybridization combined with immunolocalization demonstrated NEP4 expression during embryogenesis in pericardial cells, muscle founder cells, glia cells and male gonads. Western blot analysis confirmed the prediction of one membrane bound and one soluble isoform, a finding quite unusual among neprilysins with presumably strong physiological relevance. At least one NEP4 isoform was found in every developmental stage indicating protein activities required throughout the whole life cycle of Drosophila. Heterologously expressed NEP4 exhibited substrate preferences comparable to human neprilysin 2 with distinct cleavage of substance P and angiotensin I.

Key words: metalloendopeptidase, glia cells, muscle founders, peptide metabolism, pericardial cells

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