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

Peptides. 2004 Aug;25(8):1243-51. doi: 10.1016/j.peptides.2004.05.010.

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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Dose-Response Relationship, Drug
  • Endothelins / chemistry*
  • Endothelins / toxicity
  • Heart Rate / drug effects
  • Mice
  • Molecular Sequence Data
  • Muscle Contraction / drug effects
  • Peptides / chemistry*
  • Peptides / genetics
  • Peptides / toxicity
  • Protein Isoforms / chemistry
  • Protein Isoforms / genetics
  • Protein Isoforms / toxicity
  • Rabbits
  • Snakes
  • Vasoconstrictor Agents / chemistry
  • Vasoconstrictor Agents / toxicity
  • Viper Venoms / chemistry*
  • Viper Venoms / genetics
  • Viper Venoms / toxicity

Substances

  • Endothelins
  • Peptides
  • Protein Isoforms
  • Vasoconstrictor Agents
  • Viper Venoms
  • sarafotoxins s6

Associated data

  • GENBANK/AY485934