Sphingolipid metabolites selectively elicit increases in nuclear calcium concentration in cell suspension cultures and in isolated nuclei of tobacco

Abstract Sphingolipids are known to interfere with calcium-based signalling pathways. Here we report that these compounds modulate nuclear calcium signalling in tobacco BY-2 cells. Nuclear protein kinase activity phosphorylated endogenous sphingoid long-chain bases (LCBs), suggesting that LCBs are a...

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Published in	Cell calcium (Edinburgh) Vol. 43; no. 1; pp. 29 - 37
Main Authors	Xiong, Tou Cheu, Coursol, Sylvie, Grat, Sabine, Ranjeva, Raoul, Mazars, Christian
Format	Journal Article
Language	English
Published	Netherlands Elsevier India Pvt Ltd 01.01.2008 Elsevier
Subjects	Advanced Basic Science Aequorin Calcium - metabolism Calcium Signaling Calcium signalling Cell Fractionation Cell Nucleus - enzymology Cell Nucleus - metabolism Cells, Cultured Cellular Biology Life Sciences Nicotiana - cytology Nicotiana - enzymology Nicotiana - metabolism Phosphotransferases (Alcohol Group Acceptor) - metabolism Plant cell nucleus Sphingoid long-chain base Sphingoid long-chain base kinase Sphingolipids Sphingolipids - chemistry Sphingolipids - metabolism Sphingolipids - pharmacology Sphingosine - analogs & derivatives Sphingosine - chemistry Sphingosine - pharmacology Tobacco BY-2 cells Transient Receptor Potential Channels - antagonists & inhibitors Calcium signalling Tobacco BY-2 cells Sphingolipids Sphingoid long-chain base kinase Aequorin Sphingoid long-chain base Plant cell nucleus TRANSPORT DE CALCIUM PLANT CELL NUCLEUS TOBACCO BY-2 CELLS TENEUR EN CALCIUM SPHINGOID LONG-CHAIN BASE AEQUORIN CALCIUM SIGNALLING SPHINGOLIPIDS SPHINGOID LONG-CHAIN BASE KINASE
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Abstract	Abstract Sphingolipids are known to interfere with calcium-based signalling pathways. Here we report that these compounds modulate nuclear calcium signalling in tobacco BY-2 cells. Nuclear protein kinase activity phosphorylated endogenous sphingoid long-chain bases (LCBs), suggesting that LCBs are actively metabolized in the nucleus of tobacco BY-2 cells. The Δ4-unsaturated LCB d - erythro -sphingosine and the saturated LCB d - ribo -phytosphingosine elicited increases in free calcium in the nucleus in a dose-dependent and structure-related manner. However, neither sphingosine-1-phosphate nor C2-ceramide was able to stimulate nuclear calcium changes. N- , N -Dimethyl- d - erythro -sphingosine, a structural analogue of d - erythro -sphingosine, was the most efficient LCB so far tested in eliciting nuclear calcium changes both in intact tobacco BY-2 cells and in isolated nuclei. TRP channel inhibitors prevent the effect of DMS, suggesting that LCBs may activate TRP-like channels located on the inner nuclear membrane Collectively, the obtained data show that nuclei respond to LCBs on their own independently of the cytosolic compartment.
AbstractList	Sphingolipids are known to interfere with calcium-based signalling pathways. Here we report that these compounds modulate nuclear calcium signalling in tobacco BY-2 cells. Nuclear protein kinase activity phosphorylated endogenous sphingoid long-chain bases (LCBs), suggesting that LCBs are actively metabolized in the nucleus of tobacco BY-2 cells. The Delta 4-unsaturated LCB d-erythro-sphingosine and the saturated LCB d-ribo-phytosphingosine elicited increases in free calcium in the nucleus in a dose-dependent and structure-related manner. However, neither sphingosine-1-phosphate nor C2-ceramide was able to stimulate nuclear calcium changes. N-,N-Dimethyl-d-erythro-sphingosine, a structural analogue of d-erythro-sphingosine, was the most efficient LCB so far tested in eliciting nuclear calcium changes both in intact tobacco BY-2 cells and in isolated nuclei. TRP channel inhibitors prevent the effect of DMS, suggesting that LCBs may activate TRP-like channels located on the inner nuclear membrane Collectively, the obtained data show that nuclei respond to LCBs on their own independently of the cytosolic compartment. Sphingolipids are known to interfere with calcium-based signalling pathways. Here we report that these compounds modulate nuclear calcium signalling in tobacco BY-2 cells. Nuclear protein kinase activity phosphorylated endogenous sphingoid long-chain bases (LCBs), suggesting that LCBs are actively metabolized in the nucleus of tobacco BY-2 cells. The Delta4-unsaturated LCB D-erythro-sphingosine and the saturated LCB D-ribo-phytosphingosine elicited increases in free calcium in the nucleus in a dose-dependent and structure-related manner. However, neither sphingosine-1-phosphate nor C2-ceramide was able to stimulate nuclear calcium changes. N-,N-Dimethyl-D-erythro-sphingosine, a structural analogue of D-erythro-sphingosine, was the most efficient LCB so far tested in eliciting nuclear calcium changes both in intact tobacco BY-2 cells and in isolated nuclei. TRP channel inhibitors prevent the effect of DMS, suggesting that LCBs may activate TRP-like channels located on the inner nuclear membrane Collectively, the obtained data show that nuclei respond to LCBs on their own independently of the cytosolic compartment. Abstract Sphingolipids are known to interfere with calcium-based signalling pathways. Here we report that these compounds modulate nuclear calcium signalling in tobacco BY-2 cells. Nuclear protein kinase activity phosphorylated endogenous sphingoid long-chain bases (LCBs), suggesting that LCBs are actively metabolized in the nucleus of tobacco BY-2 cells. The Δ4-unsaturated LCB d - erythro -sphingosine and the saturated LCB d - ribo -phytosphingosine elicited increases in free calcium in the nucleus in a dose-dependent and structure-related manner. However, neither sphingosine-1-phosphate nor C2-ceramide was able to stimulate nuclear calcium changes. N- , N -Dimethyl- d - erythro -sphingosine, a structural analogue of d - erythro -sphingosine, was the most efficient LCB so far tested in eliciting nuclear calcium changes both in intact tobacco BY-2 cells and in isolated nuclei. TRP channel inhibitors prevent the effect of DMS, suggesting that LCBs may activate TRP-like channels located on the inner nuclear membrane Collectively, the obtained data show that nuclei respond to LCBs on their own independently of the cytosolic compartment. Sphingolipids are known to interfere with calcium-based signalling pathways. Here we report that these compounds modulate nuclear calcium signalling in tobacco BY-2 cells. Nuclear protein kinase activity phosphorylated endogenous sphingoid long-chain bases (LCBs), suggesting that LCBs are actively metabolized in the nucleus of tobacco BY-2 cells. The Δ4-unsaturated LCB d- erythro-sphingosine and the saturated LCB d- ribo-phytosphingosine elicited increases in free calcium in the nucleus in a dose-dependent and structure-related manner. However, neither sphingosine-1-phosphate nor C2-ceramide was able to stimulate nuclear calcium changes. N-, N-Dimethyl- d- erythro-sphingosine, a structural analogue of d- erythro-sphingosine, was the most efficient LCB so far tested in eliciting nuclear calcium changes both in intact tobacco BY-2 cells and in isolated nuclei. TRP channel inhibitors prevent the effect of DMS, suggesting that LCBs may activate TRP-like channels located on the inner nuclear membrane Collectively, the obtained data show that nuclei respond to LCBs on their own independently of the cytosolic compartment. Sphingolipids are known to interfere with calcium-based signalling pathways. Here we report that these compounds modulate nuclear calcium signalling in tobacco BY-2 cells. Nuclear protein kinase activity phosphorylated endogenous sphingoid long-chain bases (LCBs), suggesting that LCBs are actively metabolized in the nucleus of tobacco BY-2 cells. The _4-unsaturated LCB d-erythro-sphingosine and the saturatedLCBd-ribo-phytosphingosine elicited increases in free calcium in the nucleus in a dose-dependent and structure-related manner.However, neither sphingosine-1-phosphate nor C2-ceramidewas able to stimulate nuclear calcium changes. N-,N-Dimethyl-d-erythro-sphingosine, a structural analogue of d-erythro-sphingosine, was the most efficient LCB so far tested in eliciting nuclear calcium changes both in intact tobacco BY-2 cells and in isolated nuclei. TRP channel inhibitors prevent the effect of DMS, suggesting that LCBs may activate TRP-like channels located on the inner nuclear membrane Collectively, the obtained data show that nuclei respond to LCBs on their own independently of the cytosolic compartment.
Author	Ranjeva, Raoul Mazars, Christian Grat, Sabine Xiong, Tou Cheu Coursol, Sylvie
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Keywords	Calcium signalling Tobacco BY-2 cells Sphingolipids Sphingoid long-chain base kinase Aequorin Sphingoid long-chain base Plant cell nucleus TRANSPORT DE CALCIUM PLANT CELL NUCLEUS TOBACCO BY-2 CELLS TENEUR EN CALCIUM SPHINGOID LONG-CHAIN BASE AEQUORIN CALCIUM SIGNALLING SPHINGOLIPIDS SPHINGOID LONG-CHAIN BASE KINASE
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Snippet	Abstract Sphingolipids are known to interfere with calcium-based signalling pathways. Here we report that these compounds modulate nuclear calcium signalling... Sphingolipids are known to interfere with calcium-based signalling pathways. Here we report that these compounds modulate nuclear calcium signalling in tobacco...
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SubjectTerms	Advanced Basic Science Aequorin Calcium - metabolism Calcium Signaling Calcium signalling Cell Fractionation Cell Nucleus - enzymology Cell Nucleus - metabolism Cells, Cultured Cellular Biology Life Sciences Nicotiana - cytology Nicotiana - enzymology Nicotiana - metabolism Phosphotransferases (Alcohol Group Acceptor) - metabolism Plant cell nucleus Sphingoid long-chain base Sphingoid long-chain base kinase Sphingolipids Sphingolipids - chemistry Sphingolipids - metabolism Sphingolipids - pharmacology Sphingosine - analogs & derivatives Sphingosine - chemistry Sphingosine - pharmacology Tobacco BY-2 cells Transient Receptor Potential Channels - antagonists & inhibitors
Title	Sphingolipid metabolites selectively elicit increases in nuclear calcium concentration in cell suspension cultures and in isolated nuclei of tobacco
URI	https://www.clinicalkey.es/playcontent/1-s2.0-S0143416007000425 https://dx.doi.org/10.1016/j.ceca.2007.02.005 https://www.ncbi.nlm.nih.gov/pubmed/17570488 https://search.proquest.com/docview/20564254 https://search.proquest.com/docview/70203732 https://hal.inrae.fr/hal-02665730
Volume	43
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