Human NRD convertase: A highly conserved metalloendopeptidase expressed at specific sites during development and in adult tissues

P. Fumagalli, M. Accarino, A. Egeo, P. Scartezzini, G. Rappazzo, A. Pizzuti, V. Avvantaggiato, A. Simeone, G. Arrigo, O. Zuffardi, S. Ottolenghi, R. Taramelli

Research output: Contribution to journalArticlepeer-review

Abstract

We report the cloning of the human homologue of the rat metalloprotease N-arginine dibasic convertase (NRD convertase). This endopeptidase is responsible for the processing, at the Arg-Lys dibasic site on the N-terminal side of the arginine residue, of propeptides and proproteins. Comparisons of the human and rat full-length cDNAs show similarity and identity of 94 and 91%, respectively. In humans NRD convertase is predominantly expressed in heart, skeletal muscle, and testis. We have also studied the expression of this gene in mouse at various developmental stages and found that the neural tissue is the almost exclusive site of expression in early development (between E 10.5 and E 16.5). To gain information about the possibility that defects in this gene are linked to inherited neuromuscular disorders, we determined the chromosomal location of the human NRD convertase gene by FISH analysis, showing that the gene resides at 1p32.2.

Original languageEnglish
Pages (from-to)238-245
Number of pages8
JournalGenomics
Volume47
Issue number2
DOIs
Publication statusPublished - Jan 15 1998

ASJC Scopus subject areas

  • Genetics

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