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) |
|---|---|
| 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 |
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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
Cite this
Structural characterization of a Lymnaea putative endoprotease related to human furin. / Smit, August B.; Spijker, Sabine; Nagle, Gregg T.; Knock, Susan L.; Kurosky, Alexander; Geraerts, Wijnand P.M.
In: FEBS Letters, Vol. 343, No. 1, 18.04.1994, p. 27-31.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structural characterization of a Lymnaea putative endoprotease related to human furin
AU - Smit, August B.
AU - Spijker, Sabine
AU - Nagle, Gregg T.
AU - Knock, Susan L.
AU - Kurosky, Alexander
AU - Geraerts, Wijnand P.M.
PY - 1994/4/18
Y1 - 1994/4/18
N2 - 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.
AB - 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.
KW - Central nervous system
KW - Furin-related endoprotease
KW - Lymnaeastagnalis
KW - Mollusc
KW - Polymerase chain reaction
KW - cDNA cloning
UR - http://www.scopus.com/inward/record.url?scp=0028349610&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028349610&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(94)80600-4
DO - 10.1016/0014-5793(94)80600-4
M3 - Article
C2 - 8163012
AN - SCOPUS:0028349610
VL - 343
SP - 27
EP - 31
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1
ER -