Premium
Molluscan putative prohormore convertases: Structural diversity in the central nervous system of Lymnaea stagnalis
Author(s) -
Smit August B.,
Spijker Sabine,
Geraerts Wijnand P.M.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80938-d
Subject(s) - lymnaea stagnalis , lymnaea , furin , biology , complementary dna , snail , microbiology and biotechnology , peptide sequence , signal peptide , gene , genetics , biochemistry , enzyme , ecology
In the cerebral ganglia of the central nervous system of the freshwater snail Lymnaea stagnalis many neuropeptides are proteolytically processed from larger prohormones at sites marked by both single and multiple basic amino acids. In the present study we identified cloned cDNA and PCR products corresponding to three putative endoproteases that may be involved in prohormone processing. The cDNA encodes a protein of 653 residues with an overall sequence identity of 60%, 41%, 35%, 40%, and 27% with the recently characterized endoproteases PC2, PC1/3, PC4, furin and Kex2, respectively. The Lymnaea preproconvertase has ∼80% homology with the catalytic domain, and ∼40% and 5̃0 with the N‐and C‐terminal part, respectively, of the vertebrate PC2. Two cloned PCR products, L fur 1 and L fur 2, show highest sequence identity to furin. Expression of the LPC2 gene is exclusively in the central nervous system, where two LPC2 transcripts of 3.0 and 4.8 kb were detected.