Generation and metabolism of bioactive sphingosine‐1‐phosphate

Stunff, Hervé Le; Milstien, Sheldon; Spiegel, Sarah

doi:10.1002/jcb.20097

Cited by 185 publications

(164 citation statements)

References 104 publications

(125 reference statements)

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“…Although PAM is highly expressed in the ovary, it remains to be determined in future studies whether this mechanism also takes place in steroidogenic cells. Although we could not determine the effect of LPA on the amounts of either sphingosine or N-acylated sphingosine, the possible contribution of other pathways to the intracellular S1P production should also be considered (52). Future studies should clarify whether sphingosine kinase activity is in fact regulated by LPA stimulation and whether this activity is correlated with the activation of PAM.…”

Section: Discussionmentioning

confidence: 92%

Differential effects of lysolipids on steroid synthesis in cells expressing endogenous LPA2 receptor

Budnik

Brunswig-Spickenheier

2005

Journal of Lipid Research

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Section: Discussionmentioning

confidence: 92%

Differential effects of lysolipids on steroid synthesis in cells expressing endogenous LPA2 receptor

Budnik

Brunswig-Spickenheier

2005

Journal of Lipid Research

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“…In mammals, the predominant LCB is sphingosine (Sph), whereas LCBs in plants are predominantly isomers of 4,8-sphingadienine and 4-hydroxy-8-sphingenine, such as phytosphingosine (Phyto-Sph) and dihydrosphingosine (DHS) [14]. In eukaryotes, phosphorylated LCBs (LCBPs) are synthesized from LCBs by long-chain base kinases (LCBKs) [5,6], whereas LCBs themselves are produced via the combinatorial activities of three LCB modification enzymes, such as LCB C-4 hydroxylase, LCB ∆8-desaturase, and LCB ∆4-desaturase [7,8].…”

mentioning

confidence: 99%

Sphingosine-1-phosphate (S1P) mediates darkness-induced stomatal closure through raising cytosol pH and hydrogen peroxide (H2O2) levels in guard cells in Vicia faba

She

Yang

2012

Sci. China Life Sci.

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The role and signaling of sphingosine-1-phosphate (S1P) during darkness-induced stomatal closure were examined in Vicia faba. Darkness substantially raised S1P and hydrogen peroxide (H 2 O 2 ) levels and closed stomata. These darkness effects were significantly suppressed by DL-threo-dihydrosphingosine (DL-threo-DHS) and N,N-dimethylsphingosine (DMS), two inhibitors of long-chain base kinases. Exogenous S1P led to stomatal closure and H 2 O 2 production, and the effects of S1P were largely prevented by the H 2 O 2 modulators ascorbic acid, catalase, and diphenyleneiodonium. These results indicated that S1P mediated darkness-induced stomatal closure by triggering H 2 O 2 production. In addition, DL-threo-DHS and DMS significantly suppressed both darkness-induced cytosolic alkalization in guard cells and stomatal closure. Exogenous S1P caused cytosolic alkalization and stomatal closure, which could be largely abolished by butyric acid. These results demonstrated that S1P synthesis was necessary for cytosolic alkalization during stomatal closure caused by darkness. Furthermore, together with the data described above, inhibition of darkness-induced H 2 O 2 production by butyric acid revealed that S1P synthesis-induced cytosolic alkalization was a prerequisite for H 2 O 2 production during stomatal closure caused by darkness, a conclusion supported by the facts that the pH increase caused by exogenous S1P had a shorter lag and peaked faster than H 2 O 2 levels and that butyric acid prevented exogenous S1P-induced H 2 O 2 production. Altogether, our data suggested that darkness induced S1P synthesis, causing cytosolic alkalization and subsequent H 2 O 2 production, finally leading to stomatal closure.sphingosine-1-phosphate, cytosol pH, hydrogen peroxide, darkness, stomatal closure Citation:Ma Y L, She X P, Yang S S. Sphingosine-1-phosphate (S1P) mediates darkness-induced stomatal closure through raising cytosol pH and hydrogen peroxide (H 2 O 2 ) levels in guard cells in Vicia faba. Sci China Life Sci, 2012, 55: 974 -983,

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“…Degradation of S1P is mediated either by irreversible cleavage to ethanolamine phosphate and hexadecenal by a pyridoxaldependent S1P lyase or by reversible dephosphorylation to sphingosine by specific S1P phosphohydrolases (SPPs) (8). Two isoforms of mammalian S1P phosphohydrolases, designated SPP-1 (9 -11) and SPP-2 (12), have been identified.…”

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confidence: 99%

Recycling of Sphingosine Is Regulated by the Concerted Actions of Sphingosine-1-phosphate Phosphohydrolase 1 and Sphingosine Kinase 2

Stunff

Giussani

Maceyka

et al. 2007

Journal of Biological Chemistry

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106

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In yeast, the long-chain sphingoid base phosphate phosphohydrolase Lcb3p is required for efficient ceramide synthesis from exogenous sphingoid bases. Similarly, in this study, we found that incorporation of exogenous sphingosine into ceramide in mammalian cells was regulated by the homologue of Lcb3p, sphingosine-1-phosphate phosphohydrolase 1 (SPP-1), an endoplasmic reticulum resident protein. Sphingosine incorporation into endogenous long-chain ceramides was increased by SPP-1 overexpression, whereas recycling of C 6 -ceramide into long-chain ceramides was not altered. The increase in ceramide was inhibited by fumonisin B 1 , an inhibitor of ceramide synthase, but not by ISP-1, an inhibitor of serine palmitoyltransferase, the rate-limiting step in the de novo biosynthesis of ceramide. Mass spectrometry analysis revealed that SPP-1 expression increased the incorporation of sphingosine into all ceramide acyl chain species, particularly enhancing C16:0, C18:0, and C20:0 long-chain ceramides. The increased recycling of sphingosine into ceramide was accompanied by increased hexosylceramides and, to a lesser extent, sphingomyelins. Sphingosine kinase 2, but not sphingosine kinase 1, acted in concert with SPP-1 to regulate recycling of sphingosine into ceramide. Collectively, our results suggest that an evolutionarily conserved cycle of phosphorylation-dephosphorylation regulates recycling and salvage of sphingosine to ceramide and more complex sphingolipids.Sphingolipids are a structurally diverse family of membrane lipids. Several lines of evidence have implicated metabolites of sphingolipids such as ceramide, sphingosine, and sphingosine 1-phosphate (S1P) 5 in diverse cellular processes (1, 2). Ceramide and sphingosine have been implicated in pathways involving stress responses, cell differentiation, apoptosis, and cell cycle arrest (1). Unlike ceramide and sphingosine, S1P promotes cell growth and survival and inhibits apoptosis (2, 3). Because of their inter-convertibility and opposing effects, the dynamic balance between S1P and ceramide/sphingosine has been proposed to be an important factor that determines cell fate (2). Accumulating evidence suggests that the S1P/ceramide balance is ultimately regulated by the relative activities of enzymes controlling the turnover of these sphingolipid metabolites. However, the molecular mechanisms involved in the regulation of intracellular levels of these sphingolipids are not yet fully understood. Cellular levels of S1P are kept low by tight spatio-temporal regulation of its synthesis and degradation. Sphingosine kinases (SphKs) catalyze the synthesis of S1P by phosphorylation of sphingosine. Two distinct SphK isoforms, SphK1 and SphK2, have been cloned and characterized in mammals (2). Diverse external stimuli, particularly growth and survival factors, stimulate SphK1, generating S1P that has been implicated in their mitogenic and anti-apoptotic effects (4, 5). In contrast to SphK1, rather than promoting growth and survival, overexpression of SphK2 suppressed growth and...

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Generation and metabolism of bioactive sphingosine‐1‐phosphate

Cited by 185 publications

References 104 publications

Differential effects of lysolipids on steroid synthesis in cells expressing endogenous LPA2 receptor

Differential effects of lysolipids on steroid synthesis in cells expressing endogenous LPA2 receptor

Sphingosine-1-phosphate (S1P) mediates darkness-induced stomatal closure through raising cytosol pH and hydrogen peroxide (H2O2) levels in guard cells in Vicia faba

Recycling of Sphingosine Is Regulated by the Concerted Actions of Sphingosine-1-phosphate Phosphohydrolase 1 and Sphingosine Kinase 2

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