Sphingosine-1-phosphate, a putative second messenger, mobilizes calcium from internal stores via an inositol trisphosphate-independent pathway.

Mattie, M. E.; Brooker, Gary; Spiegel, Sarah

doi:10.1016/s0021-9258(17)41846-1

Cited by 261 publications

(22 citation statements)

References 45 publications

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“…In several studies SPP was reported to act as an intracellular mediator, able to mobilize Ca# + from internal Ca# + pools insensitive to Ins(1,4,5)P $ , independent of binding to specific GPCRs [4,5]. In contrast, the present results show that in C # C "# myoblasts, as also demonstrated in other cell types [1][2][3], SPPinduced Ca# + increase was a receptor-coupled process.…”

Section: Discussionsupporting

confidence: 50%

“…Even though these possibilities are not necessarily mutually exclusive, it is, however, important to define specific biological responses regulated by SPP as an extracellular mediator and those regulated by its intracellular action. In earlier studies, SPP was reported to act directly on the internal Ca# + pool, inducing Ca# + mobilization in permeabilized cells or in the purified endoplasmic reticulum [4,5]. Since then, a role for the bioactive lipid as a second messenger responsible for Ca# + mobilization induced by epidermal growth factor [6], antigen FcεRI receptor [7] and some G-protein-coupled receptors (GPCRs) [8] has been proposed.…”

Section: Introductionmentioning

confidence: 99%

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Sphingosine 1-phosphate evokes calcium signals in C2C12 myoblasts via Edg3 and Edg5 receptors

et al. 2002

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Sphingosine 1-phosphate (SPP) is a bioactive lipid that exerts multiple biological effects in a large variety of cell types, acting as either an intracellular messenger or an extracellular ligand coupled to Edg-family receptors (where Edg stands for endothelial differentiation gene). Here we report that in C(2)C(12) myoblasts SPP elicited significant Ca(2+) mobilization. Analysis of the process using a confocal laser-scanning microscope showed that the Ca(2+) response occurred in a high percentage of cells, despite variations in amplitude and kinetics. Quantitative analysis of SPP-induced Ca(2+) transients performed with a spectrophotofluorimeter showed that the rise in Ca(2+) was strictly dependent on availability of extracellular Ca(2+). Cell treatment with pertussis toxin partially prevented the Ca(2+) response induced by SPP, indicating that G(i)-coupled-receptors were involved. Indeed, SPP action was shown to be mediated by agonist-specific Edg receptors. In particular, suramin, an antagonist of the SPP-specific receptor Edg3, as well as down-regulation of Edg3 by cell transfection with antisense oligodeoxyribonucleotides (ODN), significantly reduced agonist-mediated Ca(2+) mobilization. Moreover, an antisense ODN designed to inhibit Edg5 expression also decreased the SPP-induced rise in Ca(2+), although to a lesser extent than that observed by inhibiting Edg3. On the contrary, the SPP response was unaffected in myoblasts loaded with antisense ODN specific for Edg1. Remarkably, the concomitant inhibition of Edg3 and Edg5 receptors abolished the SPP-induced Ca(2+) increase, supporting the notion that Ca(2+) mobilization in C(2)C(12) cells induced by SPP is a receptor-mediated process that involves Edg3 and Edg5, but not Edg1.

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Section: Discussionsupporting

confidence: 50%

Section: Introductionmentioning

confidence: 99%

Sphingosine 1-phosphate evokes calcium signals in C2C12 myoblasts via Edg3 and Edg5 receptors

et al. 2002

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“…As no InsP 3 accumulation could be detected in IFN-γtreated cells following aggregation of FcγRI, alternative routes for calcium release were investigated. As a sphingoid base has previously been implicated in mobilisation of intracellular calcium stores [29][30][31], the differentiationdependent coupling of FcγRI to sphingosine kinase was investigated in these cells. A prompt twofold increase in sphingosine kinase activity was observed 30 seconds after receptor aggregation in these cells whereas it was not activated in dbcAMP-differentiated cells.…”

Section: The Fcγri-mediated Calcium Response In Ifn-γ-treated Cells Is Dependent On Pld and Sphingosine Kinasementioning

confidence: 99%

A molecular switch changes the signalling pathway used by the FcγRI antibody receptor to mobilise calcium

et al. 1998

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The switch in Fc gamma RI signalling pathways upon monocyte differentiation is mediated by a switch in the accessory molecule recruited by Fc gamma RI, which lacks its own intrinsic signal transduction motif. As many immune receptors have separate polypeptide chains for ligand binding and signal transduction (allowing a similar switch in signalling pathways), the mechanism described here is likely to be widely used.

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“…Extracellular S1P binds to the cell surface receptors S1PR 1‐5 and regulates immune cell trafficking (Spiegel & Milstien, 2003, 2011; Rosen & Goetzl, 2005; Maceyka & Spiegel, 2014). S1P also functions as an intracellular signaling molecule and interferes with histone acetylation (Hait et al, 2009), calcium mobilization from the ER (Ghosh et al, 1990, 1994; Mattie et al, 1994), and TNFα‐induced NF‐κB activation (Alvarez et al, 2010), which indicates pleiotropic targets of S1P within the cell.…”

Section: Introductionmentioning

confidence: 99%

Cellular stress promotes NOD1/2‐dependent inflammation via the endogenous metabolite sphingosine‐1‐phosphate

Pei

Żyła

et al. 2021

The EMBO Journal

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Cellular stress has been associated with inflammation, yet precise underlying mechanisms remain elusive. In this study, various unrelated stress inducers were employed to screen for sensors linking altered cellular homeostasis and inflammation. We identified the intracellular pattern recognition receptors NOD1/2, which sense bacterial peptidoglycans, as general stress sensors detecting perturbations of cellular homeostasis. NOD1/2 activation upon such perturbations required generation of the endogenous metabolite sphingosine‐1‐phosphate (S1P). Unlike peptidoglycan sensing via the leucine‐rich repeats domain, cytosolic S1P directly bound to the nucleotide binding domains of NOD1/2, triggering NF‐κB activation and inflammatory responses. In sum, we unveiled a hitherto unknown role of NOD1/2 in surveillance of cellular homeostasis through sensing of the cytosolic metabolite S1P. We propose S1P, an endogenous metabolite, as a novel NOD1/2 activator and NOD1/2 as molecular hubs integrating bacterial and metabolic cues.

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Sphingosine-1-phosphate, a putative second messenger, mobilizes calcium from internal stores via an inositol trisphosphate-independent pathway.

Cited by 261 publications

References 45 publications

Sphingosine 1-phosphate evokes calcium signals in C2C12 myoblasts via Edg3 and Edg5 receptors

Sphingosine 1-phosphate evokes calcium signals in C2C12 myoblasts via Edg3 and Edg5 receptors

A molecular switch changes the signalling pathway used by the FcγRI antibody receptor to mobilise calcium

Cellular stress promotes NOD1/2‐dependent inflammation via the endogenous metabolite sphingosine‐1‐phosphate

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