Structural characterization of a Lymnaea putative endoprotease related to human furin

August B. Smit, Sabine Spijker, Gregg T. Nagle, Susan L. Knock, Alexander Kurosky, Wijnand P M Geraerts

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    18 Scopus citations


    A number of peptides have been identified in the central nervous system of the freshwater snail, Lymnaea stagnalis, that function as hormones and neurotransmitters/neuromodulators. These peptides are typically proteolytically processed from larger prohormones mostly at sites composed of single or multiple basic amino acid residues. Previously we demonstrated a diversity of putative prohormone convertases that may be involved in prohormone processing in the Lymnaea brain. In the present report, we have characterized a cDNA clone encoding a putative endoprotease of 837 amino acids. The primary structure of the endoprotease (Lfur2) was comparable to that of human furin and contained a putative catalytic domain, a Cys-rich domain, and a transmembrane region. The catalytic domain of Lfur2 demonstrated about 70% residue identity when compared with human furin, PACE4 and Drosophila Dfur1 and dKLIP-1. The Lfur2 gene was expressed in the central nervous system as well as various peripheral tissues of Lymnaea.

    Original languageEnglish (US)
    Pages (from-to)27-31
    Number of pages5
    JournalFEBS Letters
    Issue number1
    StatePublished - Apr 18 1994



    • cDNA cloning
    • Central nervous system
    • Furin-related endoprotease
    • Lymnaeastagnalis
    • Mollusc
    • Polymerase chain reaction

    ASJC Scopus subject areas

    • Biochemistry
    • Biophysics
    • Molecular Biology

    Cite this

    Smit, A. B., Spijker, S., Nagle, G. T., Knock, S. L., Kurosky, A., & Geraerts, W. P. M. (1994). Structural characterization of a Lymnaea putative endoprotease related to human furin. FEBS Letters, 343(1), 27-31.