Long-sarafotoxins: Characterization of a new family of endothelin-like peptides

Mirian A.F. Hayashi, Caroline Ligny-Lemaire, Zvi Wollberg, Michaël Wery, Andrzej Galat, Tomohisa Ogawa, Bruno H. Muller, Hung Lamthanh, Yvon Doljansky, Avner Bdolah, Reto Stöcklin, Frédéric Ducancel

    Research output: Contribution to journalArticlepeer-review

    33 Citations (Scopus)

    Abstract

    Sarafotoxins (SRTXs) constitute a family of vasoactive peptides that were initially isolated from the venom of Atractaspis engaddensis, and that are structurally and functionally related to endothelins (ETs). Analysis of the venom of Atractaspis microlepidota microlepidota revealed several new SRTX molecules manifesting some new structural and functional characteristics. These novel SRTXs are longer by three amino acids than the previously described SRTXs, and are designated here "long-SRTXs". Six isoforms, derived from new poly-cistronic precursors, have been identified so far in the venom of this snake. One of these isoforms, designated SRTX-m, was chemically synthesized and its biological properties were studied. Our results show that SRTX-m induces toxicity in mice, mostly due to vasoconstriction, and also that it has a lower toxicity and potency than the more potent SRTX described up to now: sarafotoxin-b (SRTX-b) from A. engaddensis.

    Original languageEnglish
    Pages (from-to)1243-1251
    Number of pages9
    JournalPeptides
    Volume25
    Issue number8
    DOIs
    Publication statusPublished - 2004 Aug

    Keywords

    • ET
    • HPLC
    • SDS-PAGE
    • SRTX
    • cDNA
    • complementary deoxyribonucleic acid
    • endothelin
    • l-SRTX
    • long-sarafotoxin
    • messenger ribonucleic acid
    • poly (A) RNA or mRNA
    • sarafotoxin
    • sodium dodecyl sulfate-polyacrylamide gel electrophoresis

    ASJC Scopus subject areas

    • Biochemistry
    • Physiology
    • Endocrinology
    • Cellular and Molecular Neuroscience

    Fingerprint

    Dive into the research topics of 'Long-sarafotoxins: Characterization of a new family of endothelin-like peptides'. Together they form a unique fingerprint.

    Cite this