Calcicludine Explained

Calcicludine (CaC) is a protein toxin from the venom of the green mamba that inhibits high-voltage-activated calcium channels, especially L-type calcium channels.

Sources

Calcicludine is a toxin in the venom of the green mamba (Dendroaspis angusticeps).

Chemistry

Calcicludine is a 60-amino acid polypeptide with six cysteines forming three disulfide bridges. Calcicludine structurally resembles dendrotoxin, but works differently, since even at high concentrations, calcicludine has no effect on dendrotoxin-sensitive potassium channels in chicken and rat neurons.

Target

Calcicludine is a blocker of high-voltage-activated calcium channels (L-, N- and P-type channels). It has highest affinity to the L-type calcium channel (IC50 = 88nM[2]). However, sensitivity of the drug on the channel depends on the species and the tissue. For example, the IC50 for block of L-type calcium channels on a cerebellar granule cell is 0.2 nM, but the IC50 of the block of rat peripheral DRG neuronal L-type channels is around 60-80 nM.[1]

Mode of Action

Calcicludine has a unique mode of action, which is still incompletely understood. It has been suggested to act by a partial pore block or an effect on channel gating.[2]

Toxicity

Calcicludine has been shown to work on rat cardiac cells and rat cerebellum granule cells.[1]

Notes and References

  1. Schweitz H, Heurteaux C, Bois P, Moinier D, Romey G, Lazdunski M . Calcicludine, a venom peptide of the Kunitz-type protease inhibitor family, is a potent blocker of high-threshold Ca2+ channels with a high affinity for L-type channels in cerebellar granule neurons . Proc Natl Acad Sci USA . 91 . 3 . 878–82 . February 1994 . 8302860 . 521415 . 10.1073/pnas.91.3.878. 1994PNAS...91..878S . free .
  2. Stotz SC, Spaetgens RL, Zamponi GW . Block of voltage-dependent calcium channel by the green mamba toxin calcicludine . J. Membr. Biol. . 174 . 2 . 157–65 . March 2000 . 10742459 . 10.1007/s002320001040 . 20776129 . 2009-02-06 . https://web.archive.org/web/20000915111057/http://link.springer-ny.com/link/service/journals/00232/bibs/0174002/01740157.html . 2000-09-15 . dead .