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J Biol Chem, Vol. 273, Issue 35, 22792-22799, August 28, 1998

Cloning and Functional Expression of a Voltage-gated Calcium Channel ₁ Subunit from Jellyfish

From the Whitney Laboratory and the ^§ Departments of Physiology and Neuroscience, University of Florida, St. Augustine, Florida 32086

Voltage-gated Ca²⁺ channels in vertebrates comprise at least seven molecular subtypes, each of which produces a current with distinct kinetics and pharmacology. Although several invertebrate Ca²⁺ channel ₁ subunits have also been cloned, their functional characteristics remain unclear, as heterologous expression of a full-length invertebrate channel has not previously been reported. We have cloned a cDNA encoding the ₁ subunit of a voltage-gated Ca²⁺ channel from the scyphozoan jellyfish Cyanea capillata, one of the earliest existing organisms to possess neural and muscle tissue. The deduced amino acid sequence of this subunit, named CyCa₁, is more similar to vertebrate L-type channels (_1S, _1C, and _1D) than to non-L-type channels (_1A, _1B, and _1E) or low voltage-activated channels (_1G). Expression of CyCa₁ in Xenopus oocytes produces a high voltage-activated Ca²⁺ current that, unlike vertebrate L-type currents, is only weakly sensitive to 1,4-dihydropyridine or phenylalkylamine Ca²⁺ channel blockers and is not potentiated by the agonist S()-BayK 8644. In addition, the channel is less permeable to Ba²⁺ than to Ca²⁺ and is more permeable to Sr²⁺. CyCa₁ thus represents an ancestral L-type ₁ subunit with significant functional differences from mammalian L-type channels.

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