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 journalArticle

    18 Citations (Scopus)

    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 languageEnglish (US)
    Pages (from-to)27-31
    Number of pages5
    JournalFEBS Letters
    Volume343
    Issue number1
    DOIs
    StatePublished - Apr 18 1994

    Fingerprint

    Furin
    Lymnaea
    Neurology
    Neurotransmitter Agents
    Catalytic Domain
    Central Nervous System
    Proprotein Convertases
    Basic Amino Acids
    Peptides
    Snails
    Fresh Water
    Drosophila
    Brain
    Complementary DNA
    Clone Cells
    Genes
    Hormones
    Tissue
    Amino Acids
    Processing

    Keywords

    • 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. https://doi.org/10.1016/0014-5793(94)80600-4

    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 journalArticle

    Smit, AB, Spijker, S, Nagle, GT, Knock, SL, Kurosky, A & Geraerts, WPM 1994, 'Structural characterization of a Lymnaea putative endoprotease related to human furin', FEBS Letters, vol. 343, no. 1, pp. 27-31. https://doi.org/10.1016/0014-5793(94)80600-4
    Smit AB, Spijker S, Nagle GT, Knock SL, Kurosky A, Geraerts WPM. Structural characterization of a Lymnaea putative endoprotease related to human furin. FEBS Letters. 1994 Apr 18;343(1):27-31. https://doi.org/10.1016/0014-5793(94)80600-4
    Smit, August B. ; Spijker, Sabine ; Nagle, Gregg T. ; Knock, Susan L. ; Kurosky, Alexander ; Geraerts, Wijnand P M. / Structural characterization of a Lymnaea putative endoprotease related to human furin. In: FEBS Letters. 1994 ; Vol. 343, No. 1. pp. 27-31.
    @article{eb0a6fa2572945e0869d5dfd20fcc690,
    title = "Structural characterization of a Lymnaea putative endoprotease related to human furin",
    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.",
    keywords = "cDNA cloning, Central nervous system, Furin-related endoprotease, Lymnaeastagnalis, Mollusc, Polymerase chain reaction",
    author = "Smit, {August B.} and Sabine Spijker and Nagle, {Gregg T.} and Knock, {Susan L.} and Alexander Kurosky and Geraerts, {Wijnand P M}",
    year = "1994",
    month = "4",
    day = "18",
    doi = "10.1016/0014-5793(94)80600-4",
    language = "English (US)",
    volume = "343",
    pages = "27--31",
    journal = "FEBS Letters",
    issn = "0014-5793",
    publisher = "Elsevier",
    number = "1",

    }

    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 - cDNA cloning

    KW - Central nervous system

    KW - Furin-related endoprotease

    KW - Lymnaeastagnalis

    KW - Mollusc

    KW - Polymerase chain reaction

    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 -