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Am J Physiol Cell Physiol 277: C665-C672, 1999;
0363-6143/99 $5.00
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Vol. 277, Issue 4, C665-C672, October 1999

Ceramide triggers intracellular calcium release via the IP3 receptor in Xenopus laevis oocytes

Evgeny Kobrinsky1, Andrew I. Spielman2, Sophia Rosenzweig2, and Andrew R. Marks1

1 Molecular Cardiology Program, Divisions of Cardiology and Circulatory Physiology, Departments of Medicine and Pharmacology, Columbia University College of Physicians and Surgeons, New York 10032; and 2 New York University College of Dentistry, Basic Science Division, New York, New York 10010

Ceramide, a product of sphingomyelin turnover, is a lipid second messenger that mediates diverse signaling pathways, including those leading to cell cycle arrest and differentiation. The mechanism(s) by which ceramide signals downstream events have not been fully elucidated. Here we show that, in Xenopus laevis oocytes, ceramide-induced maturation is associated with the release of intracellular calcium stores. Ceramide caused a dose-dependent elevation in the second messenger inositol 1,4,5-trisphosphate (IP3) via activation of Gq/11alpha and phospholipase C-beta X. Elevation of IP3, in turn, activated the IP3 receptor calcium release channel on the endoplasmic reticulum, resulting in a rise in cytoplasmic calcium. Thus our study demonstrates that cross talk between the ceramide and phosphoinositide signaling pathways modulates intracellular calcium homeostasis.

meiotic maturation; calcium signaling; phospholipase C





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