Identification of a Peptide Toxin from Grammostola spatulata Spider Venom That Blocks Cation-Selective Stretch-Activated Channels

@article{Suchyna2000IdentificationOA,
  title={Identification of a Peptide Toxin from Grammostola spatulata Spider Venom That Blocks Cation-Selective Stretch-Activated Channels},
  author={T. Suchyna and J. H. Johnson and K. Hamer and J. Leykam and D. Gage and H. Clemo and C. Baumgarten and F. Sachs},
  journal={The Journal of General Physiology},
  year={2000},
  volume={115},
  pages={583 - 598}
}
  • T. Suchyna, J. H. Johnson, +5 authors F. Sachs
  • Published 2000
  • Chemistry, Medicine
  • The Journal of General Physiology
  • We have identified a 35 amino acid peptide toxin of the inhibitor cysteine knot family that blocks cationic stretch-activated ion channels. The toxin, denoted GsMTx-4, was isolated from the venom of the spider Grammostola spatulata and has <50% homology to other neuroactive peptides. It was isolated by fractionating whole venom using reverse phase HPLC, and then assaying fractions on stretch-activated channels (SACs) in outside-out patches from adult rat astrocytes. Although the channel gating… CONTINUE READING
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