Scorpion toxins: tools for studying K+ channels

Toxicon. 1998 Nov;36(11):1641-50. doi: 10.1016/s0041-0101(98)00157-3.

Abstract

Over the last period of time, a large number of scorpion toxins have been characterized. These peptidyl inhibitors of K+ channels have been very useful as probes for determining the molecular architecture of these channels, for purifying channels from native tissue and determining their subunit composition, for developing the pharmacology of K+ channels, and for determining the physiologic role that K+ channels play in target tissues. The large knowledge that we have developed regarding K+ channel function would not have been possible without the discovery of these peptidyl inhibitors. It is expected that as more novel peptides are discovered, our understanding of K+ channel structure and function will be further enhanced.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aorta
  • Carbohydrate Sequence
  • Cattle
  • Charybdotoxin / pharmacology
  • Humans
  • Kv1.3 Potassium Channel
  • Large-Conductance Calcium-Activated Potassium Channels
  • Molecular Sequence Data
  • Muscle, Smooth, Vascular / drug effects
  • Muscle, Smooth, Vascular / metabolism
  • Potassium Channel Blockers
  • Potassium Channels / agonists
  • Potassium Channels / metabolism*
  • Potassium Channels, Calcium-Activated*
  • Potassium Channels, Voltage-Gated*
  • Scorpion Venoms* / pharmacology
  • Scorpions
  • Sequence Homology, Amino Acid
  • T-Lymphocytes / drug effects
  • T-Lymphocytes / metabolism

Substances

  • KCNA3 protein, human
  • Kv1.3 Potassium Channel
  • Large-Conductance Calcium-Activated Potassium Channels
  • Potassium Channel Blockers
  • Potassium Channels
  • Potassium Channels, Calcium-Activated
  • Potassium Channels, Voltage-Gated
  • Scorpion Venoms
  • Charybdotoxin
  • agitoxin 1