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From the Department of Biochemistry, Medical College of Virginia
Campus, Virginia Commonwealth University, Richmond, Virginia 23298-0614 and the § Laboratory of Cellular and Molecular Regulation,
National Institute of Mental Health, Bethesda, Maryland 20892
The bioactive sphingolipid metabolite
sphingosine 1-phosphate
(S1P),1 formed by
phosphorylation of sphingosine catalyzed by sphingosine kinase (Fig.
1), is an important lipid mediator that
has been implicated in many biological processes. S1P has been detected in organisms as diverse as plants, yeast, worms, flies, and mammals. More than a decade has elapsed since it was first suggested that S1P
can regulate cell growth (1). Because it has multiple actions and
regulates many processes, only relatively recently have we begun
to make major progress in unraveling its pleiotropic actions following
the cloning of the enzymes that regulate its levels and identification
of its specific cell surface receptors. Much still remains to be
uncovered, and its name, derived from the riddle of the mysterious
sphinx, remains appropriate for this enigmatic lipid.
It is now well established that S1P is the natural ligand for
specific G protein-coupled receptors (GPCRs), hereafter referred to as
S1PRs. To date, five members, EDG-1/S1P1,
EDG-5/S1P2, EDG-3/S1P3, EDG-6/S1P4,
and EDG-8/S1P5 have been identified (2-5). These receptors
are highly specific and only bind S1P and dihydro-S1P, which lacks the
trans double bond of the sphingoid base. Although earlier studies
suggested that S1P1 might also bind the structurally related serum-borne phospholipid, lysophosphatidic acid (6), it is now
clear that this lipid is not a ligand for any of the S1PRs and has its
own closely related family of GPCRs (7). The S1PRs are ubiquitously
expressed and are coupled to a variety of G proteins. Whereas
S1P1 and S1P5 are coupled mainly to
Gi, S1P2 can be coupled to all G proteins,
S1P3 is coupled to Gi, Gq, and
G12/13, and S1P4 activates Gi and
G12 but not Gs or Gq/11 in
response to S1P. As a consequence, S1P influences distinct biological
processes depending on the relative expression of S1PRs as well as G
proteins. Members of the S1PRs also differentially regulate the small
GTPases of the Rho family, particularly Rho and Rac (8), which are
downstream of the heterotrimeric G proteins and are important for
cytoskeletal rearrangements and cell movement (9). Activation of
S1P1 stimulates Rac-coupled cortical actin formation and
enhances motility (8, 10-13) whereas S1P2 elicits Rho-coupled stress fiber assembly and suppresses Rac activation (14),
thereby inhibiting cell migration. Interestingly, only higher
eukaryotes express S1PRs, whereas lower organisms, including plants and
yeast, though responsive to S1P, seem not to have them.
Understanding the biological functions of the S1PRs is still in its
infancy although some major advances have emerged from recent gene
disruption studies. The phenotype of s1p1 null
mice revealed the important function of S1P1 in vascular
maturation (11). The embryos died in utero between E12.5 and
E14.5 because of incomplete vascular maturation (11) resulting from a
failure of vascular smooth muscle cells and pericytes to migrate around arteries and capillaries and properly reinforce them. Disruption of the
PDGF-BB or PDGFR- The importance of S1P2 in cardiac development was revealed
in the zebrafish mutant miles apart (mil), the
S1P2 orthologue, by the formation of a bilateral heart on
the either side of the midline (22). Remarkably, the S1P2
gene is not expressed in the migrating heart precursors; rather, it is
expressed in the midline region of zebrafish embryos (22). In contrast
to what might be expected, S1P2 deletion in mice did not
produce a similar cardiovascular or any other physiological defect
(23).
S1P3-deleted mice also developed normally suggesting that
it is likewise nonessential for development (24). However,
S1P-dependent activation of PLC and not Rho was defective
in fibroblasts from these mice (24). These results suggest that
S1P3 is the predominant receptor coupling Gi to
PLC activation and inositol 1,4,5-trisphosphate formation. Even
less is known of S1P4, which is mainly expressed in
lymphoid and hematopoietic tissues and activates ERK1/2 (25) and PLC
via pertussis toxin-sensitive G proteins (26). Of all of these GPCRs,
S1P5, which is expressed predominantly by oligodendrocytes and/or fibrous astrocytes in the rat brain (27), is the only one that
mediates anti-proliferative effects, and it has the most unusual
signaling properties. Surprisingly, ligand-activated S1P5 inhibited serum-induced activation of ERK1/2, most probably because of
activation of a tyrosine phosphatase (28).
Does S1P exert its action solely through GPCRs? In analogy with
some other lipid mediators, such as eicosanoids, which might bind to
and activate nuclear receptors (29), it is tempting to speculate that
S1P may also have intracellular targets. Indeed, there is abundant
evidence that S1P can also function as a second messenger important for
regulation of calcium homeostasis (30-32) and suppression of apoptosis
(33-36). Although intracellular targets of S1P have not yet been
identified (making this a controversial area) several lines of evidence
strongly support a role for intracellular actions of S1P. (i)
Sphinganine 1-phosphate (dihydro-S1P), which is identical to S1P and
only lacks the 4,5-trans double bond, binds to all of the
S1PRs and activates them, yet does not mimic all of the effects of S1P,
especially those related to cell survival (17, 34, 37, 38). (ii)
Microinjection of S1P, as well as caged S1P, which elevate
intracellular S1P, have been shown to mobilize calcium (32) and enhance
proliferation and survival (34, 37). (iii) Yeast do not possess GPCRs,
yet levels of phosphorylated long chain sphingoid bases regulate
environmental stress responses and survival (39-42) in a manner
reminiscent of the function of S1P in mammalian cells. (iv) Finally,
recent evidence implicates S1P in calcium signaling and mobilization in
yeast (43) and in higher plants (44).
Ceramide (N-acylsphingosine) and sphingosine, the
precursor of S1P (Fig. 1), are associated with cell growth arrest and
are important regulatory components of stress responses and apoptosis (see accompanying minireview by Hannun and Obeid (72)). In contrast, S1P has been implicated in cellular proliferation and survival (33, 45). Whereas stresses increase de novo
ceramide synthesis or activate sphingomyelinases and ceramidase and
elevate levels of ceramide and sphingosine leading to apoptosis, many
other stimuli, particularly growth and survival factors, activate SPHK,
resulting in accumulation of S1P and consequent suppression of
ceramide-mediated apoptosis (33). Thus, it has been suggested that the
dynamic balance between intracellular S1P versus sphingosine
and ceramide and the consequent regulation of opposing signaling
pathways are important factors that determine whether cells survive or
die (33).
This sphingolipid rheostat concept has important clinical
implications. For example, increased S1P or decreased ceramide can prevent radiation-induced oocyte loss in adult wild-type female mice,
the event that drives premature ovarian failure and infertility in
female cancer patients (34, 46). This effect was not mimicked by
dihydro-S1P nor was it blocked by pertussis toxin, indicating (in
agreement with previous studies (33, 35, 38, 47-50)) that the
cytoprotective effects of S1P are likely S1PR-independent. The balance
between sphingosine and S1P also has been suggested to determine the
allergic responsiveness of mast cells (51). Moreover, the protective
action of high density lipoprotein against the development of
atherosclerosis and associated coronary heart disease has also been
correlated with resetting of the sphingolipid rheostat (52).
The sphingolipid rheostat is evolutionarily conserved, as it also plays
a role in regulation of stress responses of yeast cells (40-42). In
these lower eukaryotic cells, the sphingolipid metabolites ceramide and
sphingosine have been implicated in heat stress responses as decreased
phosphorylated long chain sphingoid bases dramatically enhanced
survival upon severe heat shock (40, 41). Recently, it was
reported that sphingosine is required for endocytosis in
Saccharomyces cerevisiae and for proper actin organization
(53, 54). Whether sphingosine plays such a role in mammalian cells is
an open question.
A prerequisite to understanding how cells regulate intracellular
levels of an important signaling molecule such as S1P is a complete
description and characterization of enzymes responsible for its
production and degradation. Recently, two different isotypes of
sphingosine kinase, the most important enzyme regulating S1P levels in
eukaryotic cells, have been cloned and characterized (55, 56). Although
highly similar in amino acid composition and sequence and possessing
five conserved domains, sphingosine kinase type 1 is much smaller than
type 2 and expressed mainly in the cytosol (Fig.
3). In contrast, SPHK2 additionally has
several predicted transmembrane regions and a proline-rich SH3-binding domain, suggesting a different subcellular location. Importantly, these
two ubiquitously expressed isoenzymes have different kinetic properties
and also differ in the temporal patterns of their appearance during
development (55, 56), implying that they perform distinct cellular
functions and may be regulated differently. To date, sphingosine
kinases have also been characterized in yeast S. cerevisiae (57) and plant Arabidopsis thaliana (58),
and homologues have been identified in Drosophila
melanogaster and Caenorhabditis elegans by data base
searches, suggesting that sphingosine kinases are a unique family of
lipid kinases and further supporting the notion of evolutionarily
conserved roles for S1P.
MINIREVIEW
Sphingosine 1-Phosphate, a Key Cell Signaling
Molecule*
and
INTRODUCTION
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Fig. 1.
Signaling functions of the substrate and
product of the sphingosine kinase reaction. SPHKs, using ATP as
the phosphate donor, catalyze the phosphorylation of
D-erythro-sphingosine to produce S1P. Several
downstream targets and potential functions of both sphingosine and S1P
are indicated. PKC, protein kinase C; ICRAC,
calcium release-activated calcium current.
Extracellular Functions of Sphingosine 1-Phosphate
genes in mice also resulted in defective ensheathment of nascent blood vessels (15, 16). Dysfunctional migration
of S1P1 null embryonic fibroblasts toward a gradient of
PDGF (13) links these two phenotypes at the final steps of vascular
development, underscoring the importance of S1P1 and endothelial cell-pericyte communication in vascular maturation and
angiogenesis. This study also revealed novel cross-talk between a
receptor tyrosine kinase, PDGFR, and a GPCR, S1P1. Hence,
binding of PDGF to its receptor activates and recruits sphingosine
kinase to the leading edge of the cell (17). This localized formation of S1P spatially and temporally stimulates S1P1 (13),
resulting in activation and integration of downstream signals essential for cell locomotion, such as FAK and Src, necessary for turnover of
focal complexes, and the small guanosine triphosphatase Rac, important
for protrusion of lamellipodia and forward movement (13, 17) (Fig.
2A). These results shed light
on the proposed vital role of S1P1 in vascular maturation
(11) and angiogenesis (8, 10, 18, 19). Further support for such
receptor cross-communication recently emerged from the demonstration
that PDGFR is tethered to S1P1 providing a platform for
integrative signaling by these two types of receptors (20). In
contrast, it was recently proposed that tyrosine kinase receptors, such
as the insulin-like growth factor-1 receptor, transactivate
S1P1 through Akt-dependent phosphorylation that
does not require the sphingosine kinase pathway (21). Thus, in this
scheme, insulin-like growth factor-1-activated Akt binds S1P1 and phosphorylates its third intracellular loop at
Thr-236, which is required for Rac activation and chemotaxis (21).
Further studies are necessary to validate the generality of this
concept of S1P-independent activation of S1PRs.
View larger version (30K):
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Fig. 2.
Receptor tyrosine kinase transactivates S1P
receptors. This scheme depicts cross-communication between
a tyrosine kinase growth factor receptor, PDGFR, and S1P receptors.
Binding of PDGF to PDGFR results in activation and translocation of
SPHK to the plasma membrane and restricted generation of S1P. S1P in
turn activates its receptors leading to recruitment and/or activation
of downstream signaling molecules, including Src, FAK, and Rac,
important for cell migration (A) or other downstream
signaling, such as phospholipase C that regulates calcium levels
(B). S1P can mobilize calcium from internal sources either
via an unidentified inositol 1,4,5-trisphosphate
(IP3)-independent receptor on the endoplasmic
reticulum (ER) or by activation of S1PRs that
stimulate phospholipase C. Stimulation of SPHK also results in
decreased sphingosine levels that normally block the store-operated
calcium release-activated calcium current leading to refilling of the
stores (modified from Ref. 13). DAG, diacylglycerol.
Sphingosine 1-Phosphate: an Intracellular Mediator?
The Sphingolipid Rheostat: a Conserved Stress Regulator
Metabolism of Sphingosine 1-Phosphate
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Fig. 3.
Structural organization of the sphingosine
kinase family. All SPHKs have five conserved domains, labeled
SC1 to SC5 for convenience. All SPHK catalytic
domains contain the conserved ATP binding sequence,
GDGXXXEXXNG. Human SPHK2 contains a proline-rich
region, which is known to bind to SH3 domains, and four transmembrane
regions (TM). It is also noteworthy that
Drosophila SPHK2 has a SEC14 domain and a
phosphatidylinositol-binding domain at the COOH terminus. SEC14 is a
lipid-binding domain that is present in a homologue of an S. cerevisiae phosphatidylinositol transfer protein and in RhoGAPs,
RhoGEFs, RasGEF, and neurofibromin. Although type 1 SPHK from A. thaliana is a bona fide sphingosine kinase (58), a data
base search revealed an unusual putative type 2 SPHK with a duplicated
catalytic domain.
TOP
INTRODUCTION
Extracellular Functions of...Sphingosine kinase is activated by numerous external stimuli including
PDGF (45), nerve growth factor (59), muscarinic acetylcholine
agonists (31), cytokines such as tumor necrosis factor-
(38)
and interleukin-1 (60), vitamin D3 (61), and cross-linking of
the immunoglobulin receptors Fc
RI (62) and Fc
RI (63) and GPCRs,
including S1PRs themselves (64). Overexpression of SPHK1 in NIH 3T3
fibroblasts resulted in enhanced proliferation (48), growth in soft
agar, and tumor formation in NOD/SCID mice (65). An elegant study used
a sphingosine kinase inhibitor and a dominant negative mutant of this
enzyme to demonstrate that sphingosine kinase contributes to cell
transformation mediated by oncogenic H-Ras (65). Overexpression of
SPHK1 also protected against apoptosis, particularly death induced
by ceramide elevation (35, 48). The cytoprotective effect was
attributed to inhibition of activation of caspase-2, -3, and -7 and of
the stress-activated protein kinase, JNK (c-Jun
NH2-terminal kinase) (35).
Specific sphingoid base phosphate phosphohydrolases were first identified in yeast and shown to be important regulators of heat stress response (40, 66). Deletions of these S1P phosphatases led to increased thermotolerance, whereas overexpression reduced it (40, 41), substantiating a role for phosphorylated sphingoid bases in heat stress responses. Based on homology with the yeast gene, a mammalian S1P phosphatase has been cloned that only degrades phosphorylated sphingoid bases (67). Overexpression of this unique S1P phosphatase altered the dynamic balance between S1P and sphingosine/ceramide in mammalian cells and, consequently, markedly enhanced apoptosis (67). Although several other mammalian lipid phosphate phosphohydrolases that can degrade S1P have been identified (68) it seems unlikely that they would play an important role in S1P metabolism (due to their lack of specificity), although further studies are necessary to confirm this.
S1P can also be degraded by S1P lyase, a pyridoxal-dependent enzyme, to ethanolamine phosphate and hexadecanal. S1P lyase, like S1P phosphatase, appears to be localized to the endoplasmic reticulum. Yeast lyase deletion mutants exhibited cell cycle arrest (39). Interestingly, disruption of the S1P lyase gene in the slime mold Dictyostelium discoideum resulted in aberrant morphogenesis as well as enhanced viability during stationary phase and provided resistance to the anti-cancer drug cisplatin, thus suggesting a role for S1P in survival and development of even this primitive multicellular organism (69).
An important question, to which there are only fragmentary answers, is
how is S1P transported inside and outside cells? Recent studies in
S. cerevisiae implicated the yeast oligomycin resistance gene (YOR1), a member of the ABC family of proteins,
in the transport of S1P. Interestingly, the cystic fibrosis
transmembrane regulator (CFTR), a unique member of this family with
high homology to YOR1, was recently shown to regulate uptake of S1P
(70). It will be important in the future to determine whether other
members of the ABC family that translocate lipids across the plasma
membrane are also S1P translocators (see accompanying minireview by van Meer and Lisman (73)).
| |
Universal Intracellular Roles of Sphingosine 1-Phosphate: from Plants to Higher Eukaryotes |
|---|
Recent studies indicate that S1P, known to be important for
calcium regulation in animal cells, is also involved in
calcium-dependent signaling of calcineurin in yeast (43)
and in the plant A. thaliana (44). It was initially
suggested that, in mammalian cells, S1P mobilizes calcium from internal
sources in an inositol 1,4,5-trisphosphate-independent manner (30).
Although many studies appear to support this concept (31, 32, 62), the
direct receptor on the endoplasmic reticulum has yet to be identified.
In mast cells, FcRI cross-linking leads to activation of SPHK and
conversion of sphingosine to S1P. Not only can S1P mobilize calcium
(62), but perhaps more importantly, sphingosine blocks the
store-operated calcium release-activated calcium current
(ICRAC) activated by agonists. Hence, upon
depletion of internal calcium stores, metabolism of sphingosine by
conversion to S1P catalyzed by SPHK lowers sphingosine levels and leads
to the disinhibition of ICRAC (71) and a net
increase of cytosolic calcium (Fig. 2B).
Recently, an intriguing study showed that S1P is a new
calcium-mobilizing molecule in plants (44). The plant hormone abscisic acid produced in roots during desiccation stress is transported to the
leaves, where it decreases stomatal opening by direct activation of
plasma membrane calcium channels. When plants were grown in drought
conditions, the levels of endogenous S1P increased. Exogenously applied
S1P, but not dihydro-S1P, stimulated calcium oscillations and stomata
closure, just as drought conditions do. Moreover, the effect of
abscisic acid was blocked by treatment with a SPHK inhibitor. Together,
these data suggest that S1P might act as a second messenger in plants
and that S1P regulates plant guard cell aperture.
| |
Perspectives and Future Directions |
|---|
The results of the many studies carried out only within the last
few years that are described in this review provide strong support for
the notion that S1P functions as both a first messenger and a second
messenger. In summary of its most well established functions to date,
S1P acts extracellularly by binding to members of the S1PR family of
GPCRs, thereby regulating cell movement, and it acts intracellularly to
regulate survival and Ca2+ homeostasis. Future challenges
include further characterization of the specific physiological roles of
the various S1PRs, identification of the intracellular targets of S1P,
the sources of S1P, and elucidation of its transport into and out of
cells. The number of genes known to be involved in S1P metabolism has
increased rapidly during the last years, yet it is likely that other
isoforms will be identified and much more needs to be learned.
Structure-function analysis of these gene products, as well as
characterization of their topology, localization, and mechanisms of
activation will enhance understanding of the cellular functions of S1P.
The development of antagonists or agonists of S1PRs and of inhibitors
or activators of enzymes that affect the intracellular concentration of
S1P may provide the basis for the development of novel therapeutics.
| |
ACKNOWLEDGEMENTS |
|---|
We apologize to those authors whose work could not be cited because of space limitations and we thank the members our laboratories for their contributions to the studies that were quoted in this review and especially Drs. Hong Liu and Hans Rosenfeldt for help with the artwork.
| |
FOOTNOTES |
|---|
* This minireview will be reprinted in the 2002 Minireview Compendium, which will be available in December, 2002. Pertinent findings were supported by National Institutes of Health Grants GM43880 and CA61774 and Department of the Army Grant DAMD17-02-1-0060 (to S. S.). This is the third article of five in the "Sphingolipid Metabolism and Signaling Minireview Series."
To whom correspondence should be addressed. Tel.: 804-828-9762;
Fax: 804-828-1473; E-mail: sspiegel@mail1.vcu.edu.
Published, JBC Papers in Press, May 13, 2002, DOI 10.1074/jbc.R200007200
| |
ABBREVIATIONS |
|---|
The abbreviations used are: S1P, sphingosine 1-phosphate; GPCR, G protein-coupled receptor; S1PR, S1P receptor; PDGF, platelet-derived growth factor; PDGFR, PDGF receptor; PLC, phospholipase C; SPHK, sphingosine kinase.
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 T. Ozbay, A. Rowan, A. Leon, P. Patel, and M. B. Sewer Cyclic Adenosine 5'-Monophosphate-Dependent Sphingosine-1-Phosphate Biosynthesis Induces Human CYP17 Gene Transcription by Activating Cleavage of Sterol Regulatory Element Binding Protein 1 Endocrinology, March 1, 2006; 147(3): 1427 - 1437. [Abstract] [Full Text] [PDF]
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H. Van Overloop, S. Gijsbers,, and P. P. Van Veldhoven Further characterization of mammalian ceramide kinase: substrate delivery and (stereo)specificity, tissue distribution, and subcellular localization studies J. Lipid Res., February 1, 2006; 47(2): 268 - 283. [Abstract] [Full Text] [PDF]
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 L. J. Heung, C. Luberto, and M. Del Poeta Role of Sphingolipids in Microbial Pathogenesis Infect. Immun., January 1, 2006; 74(1): 28 - 39. [Full Text] [PDF]
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 E. Le Scolan, D. Pchejetski, Y. Banno, N. Denis, P. Mayeux, W. Vainchenker, T. Levade, and F. Moreau-Gachelin Overexpression of sphingosine kinase 1 is an oncogenic event in erythroleukemic progression Blood, September 1, 2005; 106(5): 1808 - 1816. [Abstract] [Full Text] [PDF]
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 A. Piva, G. Casadei, G. Pagliuca, E. Cabassi, F. Galvano, M. Solfrizzo, R. T. Riley, and D. E. Diaz Activated carbon does not prevent the toxicity of culture material containing fumonisin B1 when fed to weanling piglets J Anim Sci, August 1, 2005; 83(8): 1939 - 1947. [Abstract] [Full Text] [PDF]
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Y. Kariya, A. Kihara, M. Ikeda, F. Kikuchi, S. Nakamura, S. Hashimoto, C.-H. Choi, Y.-M. Lee, and Y. Igarashi Products by the sphingosine kinase/sphingosine 1-phosphate (S1P) lyase pathway but not S1P stimulate mitogenesis Genes Cells, June 1, 2005; 10(6): 605 - 615. [Abstract] [Full Text] [PDF]
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J. Min, P. P. Van Veldhoven, L. Zhang, M. H. Hanigan, H. Alexander, and S. Alexander Sphingosine-1-Phosphate Lyase Regulates Sensitivity of Human Cells to Select Chemotherapy Drugs in a p38-Dependent Manner Mol. Cancer Res., May 1, 2005; 3(5): 287 - 296. [Abstract] [Full Text] [PDF]
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 L. D. Mastrandrea, S. M. Sessanna, and S. G. Laychock Sphingosine Kinase Activity and Sphingosine-1 Phosphate Production in Rat Pancreatic Islets and INS-1 Cells: Response to Cytokines Diabetes, May 1, 2005; 54(5): 1429 - 1436. [Abstract] [Full Text] [PDF]
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V. Limaye, X. Li, C. Hahn, P. Xia, M. C. Berndt, M. A. Vadas, and J. R. Gamble Sphingosine kinase-1 enhances endothelial cell survival through a PECAM-1-dependent activation of PI-3K/Akt and regulation of Bcl-2 family members Blood, April 15, 2005; 105(8): 3169 - 3177. [Abstract] [Full Text] [PDF]
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S. Vaena de Avalos, X. Su, M. Zhang, Y. Okamoto, W. Dowhan, and Y. A. Hannun The Phosphatidylglycerol/Cardiolipin Biosynthetic Pathway Is Required for the Activation of Inositol Phosphosphingolipid Phospholipase C, Isc1p, during Growth of Saccharomyces cerevisiae J. Biol. Chem., February 25, 2005; 280(8): 7170 - 7177. [Abstract] [Full Text] [PDF]
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 Z Roth and P J Hansen Disruption of nuclear maturation and rearrangement of cytoskeletal elements in bovine oocytes exposed to heat shock during maturation Reproduction, February 1, 2005; 129(2): 235 - 244. [Abstract] [Full Text] [PDF]
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K. Itagaki, K. B. Kannan, and C. J. Hauser Lysophosphatidic acid triggers calcium entry through a non-store-operated pathway in human neutrophils J. Leukoc. Biol., February 1, 2005; 77(2): 181 - 189. [Abstract] [Full Text] [PDF]
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S. M. Pitson, P. Xia, T. M. Leclercq, P. A.B. Moretti, J. R. Zebol, H. E. Lynn, B. W. Wattenberg, and M. A. Vadas Phosphorylation-dependent translocation of sphingosine kinase to the plasma membrane drives its oncogenic signalling J. Exp. Med., January 3, 2005; 201(1): 49 - 54. [Abstract] [Full Text] [PDF]
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J. Min, D. Traynor, A. L. Stegner, L. Zhang, M. H. Hanigan, H. Alexander, and S. Alexander Sphingosine Kinase Regulates the Sensitivity of Dictyostelium discoideum Cells to the Anticancer Drug Cisplatin Eukaryot. Cell, January 1, 2005; 4(1): 178 - 189. [Abstract] [Full Text] [PDF]
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C. Delon, M. Manifava, E. Wood, D. Thompson, S. Krugmann, S. Pyne, and N. T. Ktistakis Sphingosine Kinase 1 Is an Intracellular Effector of Phosphatidic Acid J. Biol. Chem., October 22, 2004; 279(43): 44763 - 44774. [Abstract] [Full Text] [PDF]
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 Z.-Q. Jin, E. J. Goetzl, and J. S. Karliner Sphingosine Kinase Activation Mediates Ischemic Preconditioning in Murine Heart Circulation, October 5, 2004; 110(14): 1980 - 1989. [Abstract] [Full Text] [PDF]
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X.-L. Chen, J. Y. Grey, S. Thomas, F.-H. Qiu, R. M. Medford, M. A. Wasserman, and C. Kunsch Sphingosine kinase-1 mediates TNF-{alpha}-induced MCP-1 gene expression in endothelial cells: upregulation by oscillatory flow Am J Physiol Heart Circ Physiol, October 1, 2004; 287(4): H1452 - H1458. [Abstract] [Full Text] [PDF]
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C. A. Welsch, L. W. A. Roth, J. F. Goetschy, and N. R. Movva Genetic, Biochemical, and Transcriptional Responses of Saccharomyces cerevisiae to the Novel Immunomodulator FTY720 Largely Mimic Those of the Natural Sphingolipid Phytosphingosine J. Biol. Chem., August 27, 2004; 279(35): 36720 - 36731. [Abstract] [Full Text] [PDF]
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 R. E. Toman, S. G. Payne, K. R. Watterson, M. Maceyka, N. H. Lee, S. Milstien, J. W. Bigbee, and S. Spiegel Differential transactivation of sphingosine-1-phosphate receptors modulates NGF-induced neurite extension J. Cell Biol., August 2, 2004; 166(3): 381 - 392. [Abstract] [Full Text] [PDF]
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M. M. Monick, R. K. Mallampalli, M. Bradford, D. McCoy, T. J. Gross, D. M. Flaherty, L. S. Powers, K. Cameron, S. Kelly, A. H. Merrill Jr., et al. Cooperative Prosurvival Activity by ERK and Akt in Human Alveolar Macrophages is Dependent on High Levels of Acid Ceramidase Activity J. Immunol., July 1, 2004; 173(1): 123 - 135. [Abstract] [Full Text] [PDF]
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J. Min, A. L. Stegner, H. Alexander, and S. Alexander Overexpression of Sphingosine-1-Phosphate Lyase or Inhibition of Sphingosine Kinase in Dictyostelium discoideum Results in a Selective Increase in Sensitivity to Platinum-Based Chemotherapy Drugs Eukaryot. Cell, June 1, 2004; 3(3): 795 - 805. [Abstract] [Full Text] [PDF]
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 E. Yokoo, Y. Yatomi, T. Takafuta, M. Osada, Y. Okamoto, and Y. Ozaki Sphingosine 1-Phosphate Inhibits Migration of RBL-2H3 Cells via S1P2: Cross-Talk between Platelets and Mast Cells J. Biochem., June 1, 2004; 135(6): 673 - 681. [Abstract] [Full Text] [PDF]
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M. M. Monick, K. Cameron, L. S. Powers, N. S. Butler, D. McCoy, R. K. Mallampalli, and G. W. Hunninghake Sphingosine Kinase Mediates Activation of Extracellular Signal-Related Kinase and Akt by Respiratory Syncytial Virus Am. J. Respir. Cell Mol. Biol., June 1, 2004; 30(6): 844 - 852. [Abstract] [Full Text] [PDF]
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 H. Zhou and K. S. Murthy Distinctive G protein-dependent signaling in smooth muscle by sphingosine 1-phosphate receptors S1P1 and S1P2 Am J Physiol Cell Physiol, May 1, 2004; 286(5): C1130 - C1138. [Abstract] [Full Text] [PDF]
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J. D. Saba and T. Hla Point-Counterpoint of Sphingosine 1-Phosphate Metabolism Circ. Res., April 2, 2004; 94(6): 724 - 734. [Abstract] [Full Text] [PDF]
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S. V. de Avalos, Y. Okamoto, and Y. A. Hannun Activation and Localization of Inositol Phosphosphingolipid Phospholipase C, Isc1p, to the Mitochondria during Growth of Saccharomyces cerevisiae J. Biol. Chem., March 19, 2004; 279(12): 11537 - 11545. [Abstract] [Full Text] [PDF]
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G. Boguslawski, P. W. McGlynn, K. A. Harvey, and A. T. Kovala SU1498, an Inhibitor of Vascular Endothelial Growth Factor Receptor 2, Causes Accumulation of Phosphorylated ERK Kinases and Inhibits Their Activity in Vivo and in Vitro J. Biol. Chem., February 13, 2004; 279(7): 5716 - 5724. [Abstract] [Full Text] [PDF]
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A. Gomez-Munoz, J. Y. Kong, B. Salh, and U. P. Steinbrecher Ceramide-1-phosphate blocks apoptosis through inhibition of acid sphingomyelinase in macrophages J. Lipid Res., January 1, 2004; 45(1): 99 - 105. [Abstract] [Full Text] [PDF]
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 D. Deretic, V. Traverso, N. Parkins, F. Jackson, E. B. R. de Turco, and N. Ransom Phosphoinositides, Ezrin/Moesin, and rac1 Regulate Fusion of Rhodopsin Transport Carriers in Retinal Photoreceptors Mol. Biol. Cell, January 1, 2004; 15(1): 359 - 370. [Abstract] [Full Text] [PDF]
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A. Olivera, H. M. Rosenfeldt, M. Bektas, F. Wang, I. Ishii, J. Chun, S. Milstien, and S. Spiegel Sphingosine Kinase Type 1 Induces G12/13-mediated Stress Fiber Formation, yet Promotes Growth and Survival Independent of G Protein-coupled Receptors J. Biol. Chem., November 21, 2003; 278(47): 46452 - 46460. [Abstract] [Full Text] [PDF]
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H. Liu, R. E. Toman, S. K. Goparaju, M. Maceyka, V. E. Nava, H. Sankala, S. G. Payne, M. Bektas, I. Ishii, J. Chun, et al. Sphingosine Kinase Type 2 Is a Putative BH3-only Protein That Induces Apoptosis J. Biol. Chem., October 10, 2003; 278(41): 40330 - 40336. [Abstract] [Full Text] [PDF]
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H. M. ROSENFELDT, Y. AMRANI, K. R. WATTERSON, K. S. MURTHY, R. A. PANETTIERI JR, and S. SPIEGEL Sphingosine-1-phosphate stimulates contraction of human airway smooth muscle cells FASEB J, October 1, 2003; 17(13): 1789 - 1799. [Abstract] [Full Text] [PDF]
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 O. A. Sukocheva, L. Wang, N. Albanese, S. M. Pitson, M. A. Vadas, and P. Xia Sphingosine Kinase Transmits Estrogen Signaling in Human Breast Cancer Cells Mol. Endocrinol., October 1, 2003; 17(10): 2002 - 2012. [Abstract] [Full Text] [PDF]
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K. R. Johnson, K. Y. Johnson, K. P. Becker, J. Bielawski, C. Mao, and L. M. Obeid Role of Human Sphingosine-1-phosphate Phosphatase 1 in the Regulation of Intra- and Extracellular Sphingosine-1-phosphate Levels and Cell Viability J. Biol. Chem., September 5, 2003; 278(36): 34541 - 34547. [Abstract] [Full Text] [PDF]
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M. Dragusin, C. Gurgui, G. Schwarzmann, J. Hoernschemeyer, and G. van Echten-Deckert Metabolism of the unnatural anticancer lipid safingol, L-threo-dihydrosphingosine, in cultured cells J. Lipid Res., September 1, 2003; 44(9): 1772 - 1779. [Abstract] [Full Text] [PDF]
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K. Arikawa, N. Takuwa, H. Yamaguchi, N. Sugimoto, J. Kitayama, H. Nagawa, K. Takehara, and Y. Takuwa Ligand-dependent Inhibition of B16 Melanoma Cell Migration and Invasion via Endogenous S1P2 G Protein-coupled Receptor: REQUIREMENT OF INHIBITION OF CELLULAR RAC ACTIVITY J. Biol. Chem., August 29, 2003; 278(35): 32841 - 32851. [Abstract] [Full Text] [PDF]
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C. Mao, R. Xu, Z. M. Szulc, J. Bielawski, K. P. Becker, A. Bielawska, S. H. Galadari, W. Hu, and L. M. Obeid Cloning and Characterization of a Mouse Endoplasmic Reticulum Alkaline Ceramidase: AN ENZYME THAT PREFERENTIALLY REGULATES METABOLISM OF VERY LONG CHAIN CERAMIDES J. Biol. Chem., August 15, 2003; 278(33): 31184 - 31191. [Abstract] [Full Text] [PDF]
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T. Yoshimoto, M. Furuhata, S. Kamiya, M. Hisada, H. Miyaji, Y. Magami, K. Yamamoto, H. Fujiwara, and J. Mizuguchi Positive Modulation of IL-12 Signaling by Sphingosine Kinase 2 Associating with the IL-12 Receptor {beta}1 Cytoplasmic Region J. Immunol., August 1, 2003; 171(3): 1352 - 1359. [Abstract] [Full Text] [PDF]
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K. Itagaki and C. J. Hauser Sphingosine 1-Phosphate, a Diffusible Calcium Influx Factor Mediating Store-operated Calcium Entry J. Biol. Chem., July 18, 2003; 278(30): 27540 - 27547. [Abstract] [Full Text] [PDF]
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A. A. Maghazachi G protein-coupled receptors in natural killer cells J. Leukoc. Biol., July 1, 2003; 74(1): 16 - 24. [Abstract] [Full Text] [PDF]
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E. Lloyd-Evans, D. Pelled, C. Riebeling, J. Bodennec, A. de-Morgan, H. Waller, R. Schiffmann, and A. H. Futerman Glucosylceramide and Glucosylsphingosine Modulate Calcium Mobilization from Brain Microsomes via Different Mechanisms J. Biol. Chem., June 20, 2003; 278(26): 23594 - 23599. [Abstract] [Full Text] [PDF]
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Y. Jin, E. Knudsen, L. Wang, Y. Bryceson, B. Damaj, S. Gessani, and A. A. Maghazachi Sphingosine 1-phosphate is a novel inhibitor of T-cell proliferation Blood, June 15, 2003; 101(12): 4909 - 4915. [Abstract] [Full Text] [PDF]
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T. Ohmori, Y. Yatomi, M. Osada, F. Kazama, T. Takafuta, H. Ikeda, and Y. Ozaki Sphingosine 1-phosphate induces contraction of coronary artery smooth muscle cells via S1P2 Cardiovasc Res, April 1, 2003; 58(1): 170 - 177. [Abstract] [Full Text] [PDF]
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Z. A. Malik, C. R. Thompson, S. Hashimi, B. Porter, S. S. Iyer, and D. J. Kusner Cutting Edge: Mycobacterium tuberculosis Blocks Ca2+ Signaling and Phagosome Maturation in Human Macrophages Via Specific Inhibition of Sphingosine Kinase J. Immunol., March 15, 2003; 170(6): 2811 - 2815. [Abstract] [Full Text] [PDF]
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K. Funato, R. Lombardi, B. Vallee, and H. Riezman Lcb4p Is a Key Regulator of Ceramide Synthesis from Exogenous Long Chain Sphingoid Base in Saccharomyces cerevisiae J. Biol. Chem., February 21, 2003; 278(9): 7325 - 7334. [Abstract] [Full Text] [PDF]
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H. Le Stunff, I. Galve-Roperh, C. Peterson, S. Milstien, and S. Spiegel Sphingosine-1-phosphate phosphohydrolase in regulation of sphingolipid metabolism and apoptosis J. Cell Biol., September 16, 2002; 158(6): 1039 - 1049. [Abstract] [Full Text] [PDF]
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Y. A. Hannun and L. M. Obeid The Ceramide-centric Universe of Lipid-mediated Cell Regulation: Stress Encounters of the Lipid Kind J. Biol. Chem., July 12, 2002; 277(29): 25847 - 25850. [Full Text] [PDF]
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G. van Meer and Q. Lisman Sphingolipid Transport: Rafts and Translocators J. Biol. Chem., July 12, 2002; 277(29): 25855 - 25858. [Full Text] [PDF]
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