Sphingolipid-to-glycerophospholipid conversion in SPL-null cells implies the existence of an alternative isozyme

Ikeda, Mika; Kihara, Akio; Kariya, Yuki; Lee, Young Moo; Igarashi, Yasuyuki

doi:10.1016/j.bbrc.2005.02.014

Cited by 11 publications

(8 citation statements)

References 23 publications

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“…F9‐7 ( SPL −/– ), F9‐8 ( SPL −/– / HA‐SPL ) and F9‐9 ( SPL +/+ / HA‐SPHK1a ) cells have been previously described (Kihara et al . 2003; Ikeda et al . 2004, 2005).…”

Section: Methodsmentioning

confidence: 99%

Products by the sphingosine kinase/sphingosine 1‐phosphate (S1P) lyase pathway but not S1P stimulate mitogenesis

Kariya¹,

Kihara²,

Ikeda³

et al. 2005

Genes to Cells

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Sphingosine 1-phosphate (S1P) functions as a ligand for the S1P/EDG family receptors. For years, intracellular signaling roles for S1P have also been suggested, especially in cell proliferation. Now, we have generated several mouse F9 embryonic carcinoma cell lines varying in expression of the S1P-degrading enzyme, S1P lyase (SPL) and/or sphingosine kinase (SPHK1). All these cell lines accumulated S1P compared to the wild-type F9 cells, but the amounts varied. We investigated the ability of these cells to proliferate under low serum conditions, as measured by a thymidine uptake assay. Although F9 cells over-expressing SPHK1 did exhibit enhanced DNA synthesis, other S1P-accumulating cells ( SPL -null cells and SPL -null cells over-expressing SPHK1) did not. The overproduction of both SPL and SPHK1 resulted in the most striking mitogenic effect. Moreover, nM concentrations of sphingosine (or dihydrosphingosine) stimulated DNA synthesis in an SPL -dependent manner. These results indicate that products by the SPL pathway, not S1P itself, function in mitogenesis.

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“…F9‐7 ( SPL −/– ), F9‐8 ( SPL −/– / HA‐SPL ) and F9‐9 ( SPL +/+ / HA‐SPHK1a ) cells have been previously described (Kihara et al . 2003; Ikeda et al . 2004, 2005).…”

Section: Methodsmentioning

confidence: 99%

Products by the sphingosine kinase/sphingosine 1‐phosphate (S1P) lyase pathway but not S1P stimulate mitogenesis

Kariya¹,

Kihara²,

Ikeda³

et al. 2005

Genes to Cells

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“…Harvested cells were subjected to lipid extraction by chloroform/methanol/HCl (100:200:1, v/v/v) and vortexing, followed by addition of chloroform and 1 % KCl. After phase separation, extracted lipids were further separated by TLC on Silica Gel 60 high performance TLC plates (Merck) with 1-butanol/acetic acid/H 2 O (3:1:1, v/v/v) and visualized by autoradiography [26].…”

Section: Methodsmentioning

confidence: 99%

“…Rfs were estimated from the previous report [26] and the data from our in house experiments. GlcCer glucosylceramide, PS phosphatidylserine, PI phosphatidylinositol, PC phosphatidylcholine supply of coenzyme PLP, which includes uptake of VB6 and conversion to PLP.…”

Section: Tlc Analysis Of [ 3 H]-labeled Sphingolipids Reveals Spl Inhmentioning

confidence: 99%

“…Then lipids were extracted, separated, and visualized as described in ''Materials and methods'' section. Rfs was estimated from the previous report[26] and the data from our in house experiments Effects of test compounds on cell viabilities (a) and Sgpl1 expression (b) under VB6(-) conditions. a Cells were treated with test compounds under VB6(-) condition, followed by cell viability tests using Cell Count Reagent SF (Nacalai tesque).…”

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confidence: 99%

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Sphingosine 1-phosphate lyase inhibition by 2-acetyl-4-(tetrahydroxybutyl)imidazole (THI) under conditions of vitamin B6 deficiency

et al. 2014

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Caramel food colorant 2-acetyl-4-(tetrahydroxybutyl)imidazole (THI) causes lymphopenia in animals through sphingosine 1-phosphate lyase (SPL) inhibition. However, this mechanism of action is partly still controversial because THI did not inhibit SPL in vitro either in cell-free or in cell-based systems. It is thought that the in vitro experimental conditions which have been used so far were not suitable for the evaluation of SPL inhibition, especially in case of cell-based experiments. We speculated that the key factor might be the coenzyme pyridoxal 5'-phosphate (PLP), an active form of vitamin B6 (VB6), because media used in cell-based assays usually contain an excess amount of VB6 which leads to the activation of SPL. By the use of VB6-deficient culture medium, we could regulate apo- (without PLP) and holo- (with PLP) SPL enzyme in cultured cells, resulting in the successful detection of SPL inhibition by THI. Although the observed inhibitory effect was not as strong as that of 4-deoxypyridoxine (a VB6 analog SPL inhibitor), these findings may be useful for further understanding the mechanism of action of THI.

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“…S1P lyase, a key enzyme of sphingolipid metabolism, is thought to be the only known enzyme that catalyzes irreversible degradation of sphingoid base-1-phosphates to phosphoethanolamine and the corresponding fatty aldehydes [16,17]. However, Ikeda et al [16] presented evidence of an alternative S1P-degrading enzyme in S1P lyase-null F9 cells which were able to degrade dihydrosphingosine. Both phosphoethanolamine and aldehyde are involved in glycerophospholipid synthesis.…”

Section: Fig 2 Production and Catabolism Of Sphingosine-1-phosphatementioning

confidence: 99%

Sphingosine-1-phosphate: distribution, metabolism and role in the regulation of cellular functions

Морозов

Сакута²,

Kalinski³

2013

Ukr.Biochem.J.

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Sphingolipid-to-glycerophospholipid conversion in SPL-null cells implies the existence of an alternative isozyme

Cited by 11 publications

References 23 publications

Products by the sphingosine kinase/sphingosine 1‐phosphate (S1P) lyase pathway but not S1P stimulate mitogenesis

Products by the sphingosine kinase/sphingosine 1‐phosphate (S1P) lyase pathway but not S1P stimulate mitogenesis

Sphingosine 1-phosphate lyase inhibition by 2-acetyl-4-(tetrahydroxybutyl)imidazole (THI) under conditions of vitamin B6 deficiency

Sphingosine-1-phosphate: distribution, metabolism and role in the regulation of cellular functions

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