New aspects of sphingosine 1-phosphate signaling in mammalian cells

Nigel J. Pyne, Jaclyn S. Long, Sue Chin Lee, Carolyn Loveridge, Laura Gillies, Susan Pyne

Research output: Contribution to journalLiterature review

15 Citations (Scopus)

Abstract

Sphingosine 1-phosphate (S1P) is a bioactive lipid that is formed by the phosphorylation of sphingosine by the enzyme, sphingosine kinase. S1P regulates cell function via a family of five closely related G-protein-coupled receptors (GPCR) termed S1P1-5 which bind S1P with high affinity (Chun et al., 2002). The S1P receptors relay the effects of S1P through signaling networks that regulate cell proliferation, survival, migration etc. A number of growth factors also activate sphingosine kinase to produce intracellular S1P which binds to putative intracellular proteins to produce cellular responses. There are two isoforms of sphingosine kinase termed SK1 and SK2. Sphingosine kinase 1 (SK1) was purified as a 49 kDa protein from rat kidney (Olivera et al., 1998) and subsequently two variants termed SK1a and SK1b were cloned from mouse (Kohama et al., 1998). The identification of SK2 was by BLAST searches of EST data using the mouse SK1 sequence. SK2 has regions of high homology with SK1, but contains an additional 240 amino acids located at the N-terminus and in the centre of the protein (Liu et al., 2000). Multiple spliced variant forms of SK1 and SK2 have subsequently been cloned (reviewed by Alemany et al., 2007). SK1 and SK2 are partially redundant since SK1−/− or SK2−/− mice are normal whereas elimination of both genes is embryonic lethal ([Allende et al., 2004] and [Mizugishi et al., 2005]). However, these enzymes may also have different sub-cellular localisations and antagonistic roles. For instance, SK1 enhances growth and survival whereas SK2 has been shown to be involved in the regulation of apoptosis (Spiegel and Milstien, 2003)
LanguageEnglish
Pages214-221
Number of pages7
JournalAdvances in Enzyme Regulation
Volume49
Issue number1
DOIs
Publication statusPublished - 2009

Fingerprint

sphingosine kinase
sphingosine 1-phosphate
Lysosphingolipid Receptors
Proteins
Sphingosine
Expressed Sequence Tags
Enzymes
G-Protein-Coupled Receptors
Cell Survival
Intercellular Signaling Peptides and Proteins
Protein Isoforms
Phosphorylation
Cell Proliferation
Apoptosis
Kidney
Lipids
Amino Acids
Growth
Genes

Keywords

  • sphingosine 1-phosphate
  • mammalian cells
  • cell biology
  • cancer

Cite this

Pyne, Nigel J. ; Long, Jaclyn S. ; Lee, Sue Chin ; Loveridge, Carolyn ; Gillies, Laura ; Pyne, Susan. / New aspects of sphingosine 1-phosphate signaling in mammalian cells. In: Advances in Enzyme Regulation. 2009 ; Vol. 49, No. 1. pp. 214-221.
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New aspects of sphingosine 1-phosphate signaling in mammalian cells. / Pyne, Nigel J.; Long, Jaclyn S.; Lee, Sue Chin; Loveridge, Carolyn; Gillies, Laura; Pyne, Susan.

In: Advances in Enzyme Regulation, Vol. 49, No. 1, 2009, p. 214-221.

Research output: Contribution to journalLiterature review

TY - JOUR

T1 - New aspects of sphingosine 1-phosphate signaling in mammalian cells

AU - Pyne, Nigel J.

AU - Long, Jaclyn S.

AU - Lee, Sue Chin

AU - Loveridge, Carolyn

AU - Gillies, Laura

AU - Pyne, Susan

PY - 2009

Y1 - 2009

N2 - Sphingosine 1-phosphate (S1P) is a bioactive lipid that is formed by the phosphorylation of sphingosine by the enzyme, sphingosine kinase. S1P regulates cell function via a family of five closely related G-protein-coupled receptors (GPCR) termed S1P1-5 which bind S1P with high affinity (Chun et al., 2002). The S1P receptors relay the effects of S1P through signaling networks that regulate cell proliferation, survival, migration etc. A number of growth factors also activate sphingosine kinase to produce intracellular S1P which binds to putative intracellular proteins to produce cellular responses. There are two isoforms of sphingosine kinase termed SK1 and SK2. Sphingosine kinase 1 (SK1) was purified as a 49 kDa protein from rat kidney (Olivera et al., 1998) and subsequently two variants termed SK1a and SK1b were cloned from mouse (Kohama et al., 1998). The identification of SK2 was by BLAST searches of EST data using the mouse SK1 sequence. SK2 has regions of high homology with SK1, but contains an additional 240 amino acids located at the N-terminus and in the centre of the protein (Liu et al., 2000). Multiple spliced variant forms of SK1 and SK2 have subsequently been cloned (reviewed by Alemany et al., 2007). SK1 and SK2 are partially redundant since SK1−/− or SK2−/− mice are normal whereas elimination of both genes is embryonic lethal ([Allende et al., 2004] and [Mizugishi et al., 2005]). However, these enzymes may also have different sub-cellular localisations and antagonistic roles. For instance, SK1 enhances growth and survival whereas SK2 has been shown to be involved in the regulation of apoptosis (Spiegel and Milstien, 2003)

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KW - sphingosine 1-phosphate

KW - mammalian cells

KW - cell biology

KW - cancer

UR - http://www.journals.elsevier.com/advances-in-enzyme-regulation

U2 - 10.1016/j.advenzreg.2009.01.011

DO - 10.1016/j.advenzreg.2009.01.011

M3 - Literature review

VL - 49

SP - 214

EP - 221

JO - Advances in Enzyme Regulation

T2 - Advances in Enzyme Regulation

JF - Advances in Enzyme Regulation

SN - 0065-2571

IS - 1

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