Characterization of a potassium channel toxin from the Caribbean Sea anemone Stichodactyla helianthus
| Autor: | Evert Karlsson, Alan L. Harvey, Ana Maria Amor, Christer Wernstedt, Åke Engström, Olga Castañeda, A.J. Anderson, Vivian Sotolongo, Reto Stöcklin |
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| Rok vydání: | 1995 |
| Předmět: |
Potassium Channels
Molecular Sequence Data Sea anemone Toxicology medicine.disease_cause Neuromuscular junction Cnidarian Venoms Botany medicine Potassium Channel Blockers Animals Amino Acid Sequence Amino Acids Peptide sequence biology Stichodactyla helianthus Toxin Potassium channel blocker biology.organism_classification Potassium channel Rats medicine.anatomical_structure Sea Anemones Biochemistry Acetylcholine medicine.drug Synaptosomes |
| Zdroj: | Toxicon : official journal of the International Society on Toxinology. 33(5) |
| ISSN: | 0041-0101 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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