Inhibition of voltage-activated K+ currents in cultured sensory neurons by the polyamine spider toxin argiotoxin-636 may involve a polyamine transporter and an intracellular site of action.
Department of Biomedical Science, Institute of Medical Science, Aberdeen University, Foresterhill, Scotland, U.K.
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D000200:Action Potentials / Q000187:drug effects; D000818:Animals; D015317:Biogenic Polyamines / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D002478:Cells, Cultured; D007210:Indoleacetic Acids; D015640:Ion Channel Gating; D008935:Mitoguazone / Q000494:pharmacology; D009475:Neurons, Afferent / Q000187:drug effects* / Q000502:physiology; D010648:Phenylacetates / Q000494:pharmacology*; D011073:Polyamines / Q000494:pharmacology*; D015221:Potassium Channels / Q000187:drug effects* / Q000502:physiology; D051381:Rats; D017208:Rats, Wistar; D013111:Spider Venoms / Q000737:chemistry*
D015317:Biogenic Polyamines; D002352:Carrier Proteins; D007210:Indoleacetic Acids; D010648:Phenylacetates; D011073:Polyamines; D015221:Potassium Channels; D013111:Spider Venoms; C558368:argiotoxin-636; D008935:Mitoguazone