Characterization of a potassium channel toxin from the Caribbean Sea anemone Stichodactyla helianthus

  • Toxicon. 1995 May;33(5):603-13. doi: 10.1016/0041-0101(95)00013-c.
O Castañeda  1 ,  V Sotolongo ,  A M Amor ,  R Stöcklin ,  A J Anderson ,  A L Harvey ,  A Engström ,  C Wernstedt ,  E Karlsson
Affiliations
  • 1. Facultad de Biología, Universidad de La Habana, Cuba.
PMID: 7660365 DOI: 10.1016/0041-0101(95)00013-c
Abstract

A peptide toxin, ShK, that blocks voltage-dependent potassium channels was isolated from the whole body extract of the Caribbean sea anemone Stichodactyla helianthus. It competes with dendrotoxin I and alpha-dendrotoxin for binding to synaptosomal membranes of rat brain, facilities acetylcholine release at an avian neuromuscular junction and suppresses K+ currents in rat dorsal root ganglion neurones in culture. Its amino acid sequence is R1SCIDTIPKS10RCTAFQCKHS20MKYRLSFCRK30TCGTC35. There is no homology with Other K+ channel-blocking peptides, except for BgK from the sea anemone Bunodosoma granulifera. ShK and BgK appear to be in a different structural class from Other toxins affecting K+ channels.

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