Modulation of skeletal muscle Ca2(+)-release channel activity by sphingosine

The American Journal of Physiology
D H NeedlemanS L Hamilton

Abstract

The effect of D-erythro-C18-sphingosine (sphingosine) and related compounds on the Ca(2+)-release channel (ryanodine binding protein) was examined on rabbit skeletal muscle membranes, on the purified ryanodine binding protein, and on the channel reconstituted into planar lipid bilayers. Sphingosine inhibited [3H]ryanodine binding to sarcoplasmic reticulum (SR) membranes in a dose-dependent manner similar to published results (R. A. Sabbadini, R. Betto, A. Teresi, G. Fachechi-Cassano, and G. Salviati. J. Biol. Chem. 267: 15475-15484, 1992). The sphingolipid also inhibited [3H]ryanodine binding to the purified ryanodine binding protein. Our results demonstrate that the inhibition of [3H]ryanodine binding by sphingosine is due to an increased rate of dissociation of bound [3H]ryanodine from SR membranes and a decreased rate of association of [3H]ryanodine to the high-affinity site. Unlike other modulators of the Ca(2+)-release channel, sphingosine can remove bound [3H]ryanodine from the high-affinity site within minutes. Sphingosine increased the rate of dissociation of [3H]ryanodine bound to a solubilized proteolytic fragment derived from the carboxy terminus of the ryanodine binding protein (cleavage at Arg4475). Sphingosine als...Continue Reading

References

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Citations

Mar 16, 2018·Mediators of Inflammation·Sabine GröschElisabetta Albi
Jan 22, 2005·American Journal of Physiology. Cell Physiology·Daniela Danieli-BettoRomeo Betto
Nov 20, 2004·Molecular Pharmacology·Christian GrimmChristian Harteneck
Apr 2, 2011·Antioxidants & Redox Signaling·Mariana N Nikolova-Karakashian, Michael B Reid

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