Abstract
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 language | English (US) |
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Pages (from-to) | 27-31 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 343 |
Issue number | 1 |
DOIs | |
State | Published - Apr 18 1994 |
Externally published | Yes |
Keywords
- 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