Sphingolipid-gated Ca2+ release from intracellular stores of endothelial cells is mediated by a novel Ca2+-permeable channel

Stella Kim, Vipul Lakhani, Debra J. Costa, Ala I. Sharara, J. Gregory Fitz, Li Wen Huang, Kevin G. Peters, L. Allen Kindman

Research output: Contribution to journalArticlepeer-review

43 Scopus citations


Sphingolipid-gated Ca2+ signaling is mediated through Ca2+-permeable channels. In this report, we characterize the properties of the channel in a human endothelial cell line (EA.hy926). Ca2+ release from intracellular stores is not antagonized by nifedipine, ω conotoxin G-VIa, or heparin. To further characterize the molecular properties of the channel, we developed a novel assay to directly measure efflux of Ca2+ from intracellular stores of permeabilized Xenopus oocytes. Following size fractionation by sucrose gradient, poly(A)+ RNA from EA.hy926 cells is microinjected into oocytes of Xenopus laevis. We find that the mRNA encoding Ca2+ release activity is ∼1.5-2.0 kilobases in length. The sphingolipid-gated Ca2+-permeable channel is thus likely to be a novel Ca2+-permeable channel distinct from other characterized intracellular Ca2+ channels such as the ryanodyne receptor and the inositol 1,4,5-trisphosphate receptor. The method described here provides a new approach to further characterizing this channel and other intracellular Ca2+ channels.

Original languageEnglish (US)
Pages (from-to)5266-5269
Number of pages4
JournalJournal of Biological Chemistry
Issue number10
StatePublished - Mar 10 1995

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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