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

Research output: Contribution to journalArticlepeer-review

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
Externally publishedYes


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

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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