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J. Biol. Chem., Vol. 277, Issue 29, 25847-25850, July 19, 2002
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From the Department of Biochemistry and Molecular Biology and the
§ Ralph H. Johnson Veterans Affairs Medical Center and
Department of Medicine, Medical University of South Carolina,
Charleston, South Carolina 29425
Whereas regulated turnover of glycerolipids has
been observed and studied for more than six decades, dogma has held
sphingolipids to be mostly structural molecules with inert metabolism.
If anything, investigation over the past 15 years or so has taught us
that sphingolipid metabolism comprises a set of highly regulated
pathways that serve to control the levels of individual molecules,
their interconversions, and their function. Most notable of these
bioactive molecules are the sphingoid bases, ceramide, and sphingosine
1-phosphate (S1P)1; other
emerging bioactive sphingolipids include sphingosylphosphorylcholine, psychosine, lactosylceramide, and cerebroside (1).
Much attention in the last decade has focused on ceramide metabolism
and function because of the increased appreciation of the involvement
of pathways involving this lipid in regulating key biologic responses
such as stress responses, cell senescence, and apoptosis. Indeed, there
have been more than 5000 publications on the biochemistry and cellular
activities of ceramide during this period.
The excitement and anticipation of rapid progress in elucidating the
molecular/biochemical mechanisms of these pathways and their specific
contributions to emerging fields of cell biology have been tempered by
the serious lag in studies on sphingolipids when compared with other
fields of biochemical study. Most of the key enzymes regulating
ceramide metabolism have been poorly studied, and there has been a
paucity of molecular and pharmacologic tools to probe these pathways
and their functions.
Luckily, there has been an advancing crescendo of studies that have
begun to shed significant light on our understanding of ceramide
metabolism and function. This minireview will highlight these major
advances, elucidate organizing principles, and advance key questions
for future research.
By necessity, this minireview adopts a ceramide-centric view of
sphingolipid metabolism and function. Borrowing from physics, it is
easier to organize information and reconstruct pathways for a fixed
observer with a fixed frame of reference. This does not change the
validity of conclusions, only their relative perspective.
Ceramide is at the hub of sphingolipid metabolism, and it serves
as the first point of significant accumulation of sphingolipids in the
de novo pathway (see minireview by Merrill (55)).
Ceramide then serves as the precursor for all major sphingolipids in
eukaryotes (such as sphingomyelin (SM) or glucosylceramide) (Fig.
1 and see minireview by Kolter et
al. (56)). The breakdown of complex sphingolipids results in the
formation of ceramide through the action of either sphingomyelinases
(SMases) or glycosidases. The breakdown of ceramide proceeds through
the action of ceramidases (CDases), and the resulting sphingoid bases
serve as substrates for sphingosine kinases to form S1P or are recycled
into ceramide and complex sphingolipids through the action of ceramide
synthases (for reviews see Refs. 1 and 2).
Functionally, ceramide has been proposed as a "coordinator" of
eukaryotic stress responses (3). This paradigm is supported by the
repeated findings that many inducers of stress response (not limited to
those inducing apoptosis) result in ceramide accumulation, usually as a
result of activation of either SMases (4) or the de
novo pathway (5) but sometimes as a result of inhibition of
ceramide clearance (through SM synthase or CDases). These inducers include cytokines (TNF, Fas, nerve growth factor), "environmental" stresses (heat, UV radiation, hypoxia/reperfusion), chemotherapeutic agents (Ara-C, doxorubicin, etoposide, and many others), and other miscellaneous agents (dexamethasone, lipopolysaccharide, sitosterol, and B-cell receptor stimulation). Several lines of investigation (see
next section) now support roles for endogenous ceramide in mediating/regulating many key and specific cellular responses.
Yeast and Molecular Identification of Enzymes of Sphingolipid
Metabolism--
A major biochemical breakthrough in the past few years
centered on the identification of the genes for all known enzymes of sphingolipid metabolism in the yeast Saccharomyces
cerevisiae (1, 6). Importantly, most of these enzymes have either
homologues or orthologues in mammalian species (1), and this is already paying dividends in the identification of mammalian counterparts (7).
Improved Methods for Quantitation of Ceramide--
The
diacylglycerol kinase assay for ceramide quantitation has emerged
as the workhorse for quantitative analysis of this lipid, and some
shortfalls in its application (especially poor attention to
quantitative conversion of ceramide) have recently been identified and
clarified (8). Also quite promising are various newly developed mass
spectroscopy-based assays for qualitative and semi-quantitative analysis of ceramide and its molecular species that may allow dissection of specific pathways of ceramide metabolism and/or function
(9, 10).
Probing for Functions of Endogenous Ceramide--
The first decade
of investigation on ceramide biology relied heavily on the use of short
chain soluble ceramides such as C2- and
C6-ceramide. Although this approach suffers the usual
limitations that arise from the use of lipid reagents (11), its utility has been reinforced by the determination of the specificity of action
of these molecules (especially the lack of activity of dihydroceramide,
the metabolic precursor of ceramide) (12). Results using these reagents
have led to the generation of several hypotheses on the roles of
ceramide in mediating specific effects in apoptosis and stress
responses (1).
The availability of specific pharmacologic inhibitors of some enzymes
of ceramide metabolism (e.g. glucosylceramide synthase (GCS)
and CDases) and the ongoing molecular cloning of some of the key
enzymes of ceramide formation (SMases and serine palmitoyltransferase (SPT)) have allowed the examination of the cellular consequences of
inducing levels of endogenous ceramide, and the results, for the most
part, have agreed with those obtained with exogenous ceramides. For
example, inhibitors of GCS and of CDases have been shown to induce
increases in ceramide levels and cause apoptosis and/or cell cycle
arrest, especially of cancer cells, and overexpression of bacterial
SMase has been shown to induce apoptosis and cell cycle arrest (1).
Determination of Necessary Roles for Ceramide in Key Cellular
Events--
The cloning of enzymes that clear ceramide such as GCS and
CDases (1, 2), the generation of knock-out mice in acid SMase (13), and
the development/discovery of specific inhibitors of enzymes of ceramide
generation (myriocin/ISP1 for SPT and fumonisin B1 for ceramide
synthase) (2) have begun to provide substantial evidence on the roles
of ceramide in mediating key cellular activities. For example,
fumonisin B1 has been shown to inhibit various aspects of apoptosis in
response to many agents (e.g. angiotensin II (14), anti-IgM
(10), and some cancer chemotherapy agents (5)). The overexpression of
GCS (15) or CDase (16) has been shown to attenuate the induced levels
of ceramide in response to TNF and other agents and to ameliorate the
apoptotic response, thus providing substantial evidence for the role of
endogenous ceramide in regulating apoptosis.
Mechanisms of Action of Ceramide: Phosphatases, Proteases, and
Kinases--
Recent studies have begun to identify key direct targets
for ceramide action. These include the ceramide-activated protein phosphatases PP1 and PP2A, which are activated by ceramide in vitro. Increasing evidence points to roles for these phosphatases in mediating many of the actions of ceramide in cells. For example, phosphatase inhibitors have been shown to inhibit the ability of
ceramide (and agents that induce ceramide formation) to cause dephosphorylation of several cellular proteins including PKC
Cathepsin D was discovered as a ceramide-binding protein, and evidence
has been provided that ceramide activates this lysosomal protease in
cells (18).
Kinase suppressor of Ras has been advanced as a mediator of the effects
of ceramide on Ras, Raf, and ERKs (extracellular signal-regulated kinases) (19). Similarly, it has been shown that ceramide activates PKC Oxidation and Neutral SMases--
Numerous studies point to a role
for changes in intracellular redox in regulation of neutral SMase (4).
For example, it has been shown that the action of TNF in inducing
apoptosis is closely related to intracellular oxidation and a drop in
the levels of GSH. In turn, this has been demonstrated as a necessary
condition for activation of SMase in response to TNF. Similarly, GSH
may regulate activation of SMase in response to hypoxia,
xenobiotics, and chemotherapeutic agents (4).
The Mitochondrion: a Novel Compartment for Ceramide Metabolism and
Action--
A novel CDase has been localized to mitochondria,
demonstrating unequivocally the existence of a mitochondrial pathway of ceramide metabolism (22). Ceramide levels have been detected in
mitochondria (23), and TNF was shown to induce accumulation of ceramide
in the heavy membrane compartment (10,000 × g pellet) (24). The addition of exogenous ceramide to purified mitochondria results in inhibition of the respiratory chain, the generation of
reactive oxygen species, and the release of cytochrome c
(24-27). The expression of bacterial SMase in mitochondria, but not
other subcellular compartments, resulted in induction of apoptosis
(28), suggesting a role for endogenous mitochondrial ceramide in
regulating apoptosis.
Diseases Related to Disturbances in Ceramide Metabolism:
Neuropathies, Diabetes, Cancer, and Aging--
One of the most
exciting areas of development in sphingolipid biology has been the
increasing evidence pointing to roles for these pathways in disease
pathogenesis. For example, the primary mutation responsible for
hereditary neuropathy has been mapped to the LCB1 subunit of SPT, and
it was suggested to induce apoptosis of susceptible sensory neurons
(29, 30). Ceramide levels have been shown to be elevated in a number of
neurodegenerative disorders such as Batten's disease, and two of the
genes responsible for subtypes of this disorder, CLN3 and protein
palmitoyl thioesterase, have been shown to attenuate ceramide levels in
response to apoptotic stimuli, suggesting a role for the ceramide
pathway in mediating cell dysfunction and death in these disorders (31,
32).
A flurry of recent studies have begun to implicate ceramide and
sphingolipid metabolism in the pathogenesis of diabetes and its
complications. Ceramide has been shown to induce dephosphorylation and
inactivation of the Akt/PKB protein kinases which play key roles in
insulin action (33). Unger and co-workers (34) have proposed that
conditions of free fatty acid overload (especially palmitate), as would
occur in obesity or diabetes, drive the de novo
pathway of ceramide synthesis leading to induction of ceramide-mediated responses (e.g. dysfunction and death of islet cells).
The emerging intimate role for ceramide in regulating stress responses
and apoptosis has led to implicating this lipid in mediating the
apoptotic and cytotoxic actions of various chemotherapeutic agents
(35). Moreover, it has been shown that drug resistance often involves
up-regulation of GCS and the failure to sustain an accumulation of
ceramide in response to chemotherapy agents (15, 36). Deficiency in
acid SMase has also been shown to diminish the response of endothelial
and neuronal cells to radiation-induced apoptosis (37).
The results demonstrating causative roles for oxidative stress in
activating SMases begin to point to important coupling of oxidative
stress to ceramide signaling. This is of particular importance to aging
biology as the aging of many tissues as well as animal models has been
closely related to accumulative oxidant stress (38). In addition, a
strong case has been provided for an important role for ceramide in
regulating the senescence of fibroblasts, endothelial cells, and
neuronal cells, tissue culture models that recapitulate several aspects
of in vivo aging (39). For example, ceramide was found to
inhibit mitogenic signaling by inhibiting PKC activation of
phospholipase D and subsequent AP1-mediated transcription.
Ceramide also causes dephosphorylation of the retinoblastoma gene
product, resulting in cell cycle arrest (40), and more recently,
ceramide has been shown to inhibit telomerase, thus linking these two
regulators of cell senescence (41).
Very recently, two genes encoding for ceramide synthase (or essential
regulatory subunits) have been identified (42, 43). These genes had
been previously discovered in S. cerevisiae as longevity assurance genes (lag1 and
the homologous lac1), and deletion of these genes extended yeast life
span by 50%, thus suggesting a role for ceramide in yeast
longevity/aging.
Yeast as a Model for Investigating Sphingolipid
Action--
Studies in S. cerevisiae have provided
substantial evidence for a basic conservation of ceramide and
sphingolipid metabolism (noted above) and function. For example, heat
stress in S. cerevisiae activates SPT and induces
accumulation of sphingoid bases, their phosphates, and ceramides over a
time frame of 10-120 min (44). Evidence has been provided for a
necessary role for this pathway in inducing the transient cell cycle
arrest and the down-regulation of nutrient permeases seen in response
to heat stress (45, 46). Thus, strong parallels are emerging on the
function of bioactive sphingolipids between mammals and yeast, and this
promises significant insight generated from the combined use of
genetics and biochemistry in probing the mechanisms of these pathways
and their function.
Focusing on Specific Pathways of Ceramide Metabolism: Modules in
Signal Transduction--
A major principle in understanding ceramide
metabolism (which applies to all other bioactive lipids) stipulates
that individual enzymes function as modules in cell regulation (Fig. 1)
that transduce an input (the activating mechanism) to an output (the
response to the changes in the product). It has thus become obvious
that "the study of ceramide" should be attempted at the level of
individual pathways and modules.
Compartmentalization and Topology of Ceramide
Metabolism--
Indeed, enzymes of ceramide metabolism show distinct
subcellular localization and perhaps topology (see minireview by van Meer and Lisman (57)). (Fig. 2). (i) The
plasma membrane harbors a fraction of acid SMase and possibly a
caveolar-associated neutral SMase (4), and generation of ceramide at
the plasma membrane exerts distinct and specific functions, such as
inhibition of PKC translocation, inhibition of NF- Key Enzymes of Ceramide Metabolism as Switches in Cell
Regulation--
Because of the intimate interconnections of lipid
metabolism, many of the enzymes that regulate bioactive lipids also
function as switches by regulating the levels of bioactive substrates
and products. For example, ceramidases can regulate the levels of ceramide (substrate) and/or sphingosine and S1P (products), with S1P
often exerting anti-apoptotic effects that antagonize ceramide-mediated responses (see minireview by Spiegel and Milstien (58)). TNF has been
shown to activate CDases, and this was correlated with lack of
accumulation of ceramide and absence of an apoptotic response. Also,
the action of IL-1 was shown to induce activation of CDase especially
at low concentrations of the cytokine, thus leading to
sphingosine-mediated responses. At higher concentrations of IL-1,
ceramide accumulates and mediates effects of IL-1 on expression of
Integration of Ceramide Metabolism and Function: Concept of
Lipidomics--
Although these switching functions may be confusing
for the casual study of bioactive lipids, they do provide the cell with a very rich matrix for fine-tuning cell responses. As such, this interconnected network of bioactive lipids allows the titration of the
levels of many lipids simultaneously whenever the existing steady state
is perturbed at any of its enzymatic nodes (Fig. 1). For example,
activation of SMase results in the accumulation of ceramide. However,
the coupling of ceramide metabolism to that of sphingosine, DAG, S1P,
and glucosylceramide (and other lipids) provides for an infinite number
of permutations in the overall profiles of bioactive lipids. As each of
these metabolites is recognized to exert its own direct actions, one
could then appreciate the richness of responses mediated by the
integration of these distinct pathways (Fig. 1).
As all bioactive lipids exert allosteric (read: non-genomic) effects on
their direct targets, the consequences of changes in levels of
bioactive lipids cannot be determined directly from genomic or
proteomic profiles. Therefore, we propose that a more complete
description of any given cell's configuration requires an assessment
of the levels of its endogenous bioactive lipids (hence, the
designation "lipidomics").
Identifying the Few Missing Key Enzymes of Ceramide
Metabolism--
There is a clear need for the molecular identification
of sphingomyelinases, sphingomyelin synthases, and ceramide kinase, the
remaining known enzymes of ceramide metabolism. Studies have reported
on the cloning of two candidate neutral sphingomyelinases (nSMase 1 and
nSMase 2) (50) although evidence was provided that nSMase 1, which
localizes to the endoplasmic reticulum, probably functions as
a lyso-PAF phospholipase C (51). nSMase 2 localizes to the
Golgi, and its physiologic substrates have not been determined. Enzymatic and subfractionation studies suggest the presence of at least
a plasma membrane and possibly mitochondrial SMases. Similarly, little
is known concerning SM synthase, one of the most recalcitrant enzymes
that has resisted efforts at purification and cloning.
Development of Pharmacologic Tools--
The study of ceramide and
sphingolipid function has benefited significantly from the availability
of myriocin/ISP1 and fumonisin B1 as specific inhibitors of SPT
and ceramide synthase, respectively. These reagents have helped in
establishing key roles for the de novo pathway of
ceramide formation in apoptosis and agonist action (see above). Thus,
there are important needs to define better inhibitors, especially for
sphingomyelinases, SM synthase, and CDases.
Determination of Biochemical/Molecular Mechanisms of Regulation of
Enzymes of Ceramide Metabolism--
The identification of these
mechanisms (e.g. analogous to activation of phospholipase
C Determination of Molecular Mechanisms of Action of
Ceramide--
Similarly, defining the mechanisms of action of ceramide
and related lipids should provide direct insight into the biochemical outputs of these specific pathways. Further studies are required to
define which targets of ceramide are directly activated in cells and
what specific functions they mediate.
Probing the Next Level of Cell Biology--
It is anticipated that
specific and compartmentalized pathways of ceramide formation and
clearance exert specific functions (such as the regulation of SR
proteins in response to de novo generated
ceramide, discussed above). Thus, the development of molecular and
pharmacologic tools and the identification of direct cellular targets
for ceramide (and related sphingolipids) should accelerate the
delineation of specific functions for ceramide in response to
individual agonists.
Exploring Other Layers of Sphingolipid Metabolism--
It is quite
likely that the currently identified pathways of sphingolipid
metabolism represent one layer with other layers to be determined. For
example, recent studies have shown the presence of receptors for
lyso-SM and psychosine, although little is known as to what enzymes
regulate the metabolism of these molecules. It is conceivable that
other "minor" pathways may exist that lead to novel metabolites.
Forging into Translational Research--
Ceramide analogs and
inhibitors of ceramide metabolism are increasingly finding their way
into translational research. Catheter balloon tips, coated with
C6-ceramide, exert significant anti-proliferative effects
on endothelium and prevent coronary restenosis (52). Exogenous
ceramides were shown to reduce infarct size in spontaneously hypertensive rats (53). B13, a ceramidase inhibitor, prevents metastasis of colon cancer to liver in a nude mouse model (54).
Sphingolipid metabolism and function is not only an exciting and
now rapidly developing field but is one of the few remaining "frontiers" in basic biochemistry, and delineation of its
biochemical mechanisms and physiologic functions promises important
rewards. It is our conjecture that one cannot understand key areas of
cell biology (including apoptosis, senescence, vesicle sorting and trafficking, membrane organization, and stress responses) and disease
pathobiology (cancer, diabetes, aging, and inflammation) without
understanding sphingolipid metabolism.
We thank Jeffrey Jones for providing Fig. 1.
We apologize for not referring to the many outstanding studies that
have propelled this field. These can be found cited in the several
comprehensive reviews cited in this minireview.
*
This minireview will be reprinted
in the 2002 Minireview Compendium, which
will be available in December, 2002. This work was supported in part by National
Institutes of Health Grants GM43285 and CA 87584 (to Y. A. H.) and AG
16583 and GM62887 (to L. M. O.). This is the second article of five
in the "Sphingolipid Metabolism and Signaling Minireview Series."
¶
Recipient of a Department of Veterans Affairs merit award.
Published, JBC Papers in Press, May 13, 2002, DOI 10.1074/jbc.R200008200
The abbreviations used are:
S1P, sphingosine
1-phosphate;
SM, sphingomyelin;
SMase, sphingomyelinase;
CDase, ceramidase;
TNF, tumor necrosis factor;
GCS, glucosylceramide
synthase;
SPT, serine palmitoyltransferase;
PKC, protein kinase C;
IL-1, interleukin-1;
DAG, diacylglycerol;
nSMase, neutral
sphingomyelinase.
MINIREVIEW
The Ceramide-centric Universe of Lipid-mediated Cell
Regulation: Stress Encounters of the Lipid Kind*
and§¶
INTRODUCTION
TOP
INTRODUCTION
Summary of the Ceramide-centric...
Recent Advances in the...
Organizing Principles
Future Directions/Goals
Conclusions
REFERENCES
Summary of the Ceramide-centric View of Universe
TOP
INTRODUCTION
Summary of the Ceramide-centric...
Recent Advances in the...
Organizing Principles
Future Directions/Goals
Conclusions
REFERENCES
View larger version (26K):
[in a new window]
Fig. 1.
Basic pathways of ceramide metabolism and
interrelationship of regulatory pathways mediated by bioactive
lipids. Ceramide can be formed de novo or
from hydrolysis of SM or complex glycolipids (horizontal plane in
diagram). In turn, ceramide may be converted to sphingosine
(Sph) or serve as a substrate for SM synthesis (generating
DAG) or glycolipids. Each of the major bioactive lipids is then capable
of interacting with specific targets leading to specific responses
(vertical plane). PalCoA, palmitoyl-CoA;
DHS, dihydrosphingosine; DHCer, dihydroceramide;
SK, sphingosine kinase; PC, phosphatidylcholine;
PA, phosphatidic acid; SMS, SM synthase;
DGK, DAG kinase; SL, sphingolipid.
Recent Advances in the Study of Ceramide Metabolism and
Function
TOP
INTRODUCTION
Summary of the Ceramide-centric...
Recent Advances in the...
Organizing Principles
Future Directions/Goals
Conclusions
REFERENCES
, Akt/PKB, c-Jun, and Bcl-2 (17).
and that this may couple the action of ceramide to activation of
the transcription factor NF-
B and the activation of the
stress-activated kinases (20, 21).
Organizing Principles
TOP
INTRODUCTION
Summary of the Ceramide-centric...
Recent Advances in the...
Organizing Principles
Future Directions/Goals
Conclusions
REFERENCES
B, and aggregation
of the Fas receptor (1, 47) but not other effects mediated by
endogenous ceramide (apoptosis, cell cycle arrest) (1). (ii)
Lysosomal acid SMase may activate cathepsin D as a direct target for
lysosomal ceramide (18). (iii) The endoplasmic reticulum (and
possibly the Golgi, mitochondrial-associated membranes, and the
nuclear membrane) is the primary site of de novo
synthesis of ceramide, and several lines of evidence point to roles for
this ceramide (inhibitable by fumonisin B) in mediating apoptosis. In a
recent study, it was shown that de novo ceramide
specifically induces dephosphorylation of nuclear SR proteins
through activation of PP1 (17). (iv) As discussed above, recent
evidence points to mitochondria as a major site for specific roles of
ceramide in apoptosis. (v) The nucleus has also been implicated as a
site of ceramide generation with possible roles in hepatocyte
regeneration and apoptosis (48).
View larger version (49K):
[in a new window]
Fig. 2.
Compartmentalization of ceramide metabolism
and function. Shown are several distinct compartments of ceramide
metabolism and function (refer to text for discussion). Cer,
ceramide; DHS, dihydrosphingosine; Cath D,
cathepsin D; Sph, sphingosine; Sph-K, sphingosine
kinase; Alk, alkaline; PalCoA, palmitoyl-CoA;
SR, sarcoplasmic reticulum; dhCer,
dihydroceramide; CerS, ceramide synthase; deSat,
desaturase; PC, phosphatidylcholine; SMS, SM
synthase.
1-acid glycoprotein (2). SM synthase (or inositol
phosphoceramide synthase in yeast) regulates the levels of
ceramide and DAG in a reciprocal manner. Indeed, evidence has been
provided that active SM synthase can switch a signaling response from
one mediated by ceramide (inhibition of NF-B) to one mediated by DAG
(activation of NF-B) (49). Thus, many of the enzymes of sphingolipid
metabolism are emerging as regulated switches controlling the relative
levels of more than one bioactive lipid.
Future Directions/Goals
TOP
INTRODUCTION
Summary of the Ceramide-centric...
Recent Advances in the...
Organizing Principles
Future Directions/Goals
Conclusions
REFERENCES
by direct tyrosine phosphorylation) should define the specific
biochemical inputs that are responsible for activation of each of these
enzymes. As a rule in cell biology, these proximal mechanisms tend to
be invariant and as such allow an advanced level of understanding of
these pathways and the prediction of when they are to be activated.
Conclusions
TOP
INTRODUCTION
Summary of the Ceramide-centric...
Recent Advances in the...
Organizing Principles
Future Directions/Goals
Conclusions
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ACKNOWLEDGEMENTS
FOOTNOTES
To whom correspondence may be addressed. E-mail: hannun@musc.edu
or obeidl{at}musc.edu.
ABBREVIATIONS
REFERENCES
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INTRODUCTION
Summary of the Ceramide-centric...
Recent Advances in the...
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Conclusions
REFERENCES
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Y. Pewzner-Jung, S. Ben-Dor, and A. H. Futerman When Do Lasses (Longevity Assurance Genes) Become CerS (Ceramide Synthases)?: INSIGHTS INTO THE REGULATION OF CERAMIDE SYNTHESIS J. Biol. Chem., September 1, 2006; 281(35): 25001 - 25005. [Full Text] [PDF]
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Y. Nagata, T. A. Partridge, R. Matsuda, and P. S. Zammit Entry of muscle satellite cells into the cell cycle requires sphingolipid signaling J. Cell Biol., July 17, 2006; 174(2): 245 - 253. [Abstract] [Full Text] [PDF]
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I. Condo, N. Ventura, F. Malisan, B. Tomassini, and R. Testi A Pool of Extramitochondrial Frataxin That Promotes Cell Survival J. Biol. Chem., June 16, 2006; 281(24): 16750 - 16756. [Abstract] [Full Text] [PDF]
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E. Houben, W. M. Holleran, T. Yaginuma, C. Mao, L. M. Obeid, V. Rogiers, Y. Takagi, P. M. Elias, and Y. Uchida Differentiation-associated expression of ceramidase isoforms in cultured keratinocytes and epidermis J. Lipid Res., May 1, 2006; 47(5): 1063 - 1070. [Abstract] [Full Text] [PDF]
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 O. L. German, G. E. Miranda, C. E. Abrahan, and N. P. Rotstein Ceramide is a Mediator of Apoptosis in Retina Photoreceptors. Invest. Ophthalmol. Vis. Sci., April 1, 2006; 47(4): 1658 - 1668. [Abstract] [Full Text] [PDF]
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S. L. Panwar and W. S. Moye-Rowley Long Chain Base Tolerance in Saccharomyces cerevisiae Is Induced by Retrograde Signals from the Mitochondria J. Biol. Chem., March 10, 2006; 281(10): 6376 - 6384. [Abstract] [Full Text] [PDF]
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 K. D. Meier, O. Deloche, K. Kajiwara, K. Funato, and H. Riezman Sphingoid Base Is Required for Translation Initiation during Heat Stress in Saccharomyces cerevisiae Mol. Biol. Cell, March 1, 2006; 17(3): 1164 - 1175. [Abstract] [Full Text] [PDF]
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P. I. Darroch, A. Dagan, T. Granot, X. He, S. Gatt, and E. H. Schuchman A lipid analogue that inhibits sphingomyelin hydrolysis and synthesis, increases ceramide, and leads to cell death J. Lipid Res., November 1, 2005; 46(11): 2315 - 2324. [Abstract] [Full Text] [PDF]
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S. Lahiri and A. H. Futerman LASS5 Is a Bona Fide Dihydroceramide Synthase That Selectively Utilizes Palmitoyl-CoA as Acyl Donor J. Biol. Chem., October 7, 2005; 280(40): 33735 - 33738. [Abstract] [Full Text] [PDF]
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J. Wu, Y. Cheng, B. A. G. Jonsson, A. Nilsson, and R.-D. Duan Acid sphingomyelinase is induced by butyrate but does not initiate the anticancer effect of butyrate in HT29 and HepG2 cells J. Lipid Res., September 1, 2005; 46(9): 1944 - 1952. [Abstract] [Full Text] [PDF]
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 R. Jennemann, R. Sandhoff, S. Wang, E. Kiss, N. Gretz, C. Zuliani, A. Martin-Villalba, R. Jager, H. Schorle, M. Kenzelmann, et al. Cell-specific deletion of glucosylceramide synthase in brain leads to severe neural defects after birth PNAS, August 30, 2005; 102(35): 12459 - 12464. [Abstract] [Full Text] [PDF]
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D. Danieli-Betto, E. Germinario, A. Esposito, A. Megighian, M. Midrio, B. Ravara, E. Damiani, L. D. Libera, R. A. Sabbadini, and R. Betto Sphingosine 1-phosphate protects mouse extensor digitorum longus skeletal muscle during fatigue Am J Physiol Cell Physiol, June 1, 2005; 288(6): C1367 - C1373. [Abstract] [Full Text] [PDF]
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S. A. Novgorodov, Z. M. Szulc, C. Luberto, J. A. Jones, J. Bielawski, A. Bielawska, Y. A. Hannun, and L. M. Obeid Positively Charged Ceramide Is a Potent Inducer of Mitochondrial Permeabilization J. Biol. Chem., April 22, 2005; 280(16): 16096 - 16105. [Abstract] [Full Text] [PDF]
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R. E. Martin, M. H. Elliott, R. S. Brush, and R. E. Anderson Detailed Characterization of the Lipid Composition of Detergent-Resistant Membranes from Photoreceptor Rod Outer Segment Membranes Invest. Ophthalmol. Vis. Sci., April 1, 2005; 46(4): 1147 - 1154. [Abstract] [Full Text] [PDF]
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H. Van Overloop, G. Van der Hoeven, and P. P. Van Veldhoven N-Acyl migration in ceramides J. Lipid Res., April 1, 2005; 46(4): 812 - 816. [Abstract] [Full Text] [PDF]
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S. Jenna, M.-E. Caruso, A. Emadali, D. T. Nguyen, M. Dominguez, S. Li, R. Roy, J. Reboul, M. Vidal, G. N. Tzimas, et al. Regulation of Membrane Trafficking by a Novel Cdc42-related Protein in Caenorhabditis elegans Epithelial Cells Mol. Biol. Cell, April 1, 2005; 16(4): 1629 - 1639. [Abstract] [Full Text] [PDF]
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W. Stoffel, B. Jenke, B. Block, M. Zumbansen, and J. Koebke Neutral sphingomyelinase 2 (smpd3) in the control of postnatal growth and development PNAS, March 22, 2005; 102(12): 4554 - 4559. [Abstract] [Full Text] [PDF]
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S. A. Summers and D. H. Nelson A Role for Sphingolipids in Producing the Common Features of Type 2 Diabetes, Metabolic Syndrome X, and Cushing's Syndrome Diabetes, March 1, 2005; 54(3): 591 - 602. [Abstract] [Full Text] [PDF]
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W. Hu, R. Xu, G. Zhang, J. Jin, Z. M. Szulc, J. Bielawski, Y. A. Hannun, L. M. Obeid, and C. Mao Golgi Fragmentation Is Associated with Ceramide-induced Cellular Effects Mol. Biol. Cell, March 1, 2005; 16(3): 1555 - 1567. [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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H. H. Wandall, S. Pizette, J. W. Pedersen, H. Eichert, S. B. Levery, U. Mandel, S. M. Cohen, and H. Clausen Egghead and Brainiac Are Essential for Glycosphingolipid Biosynthesis in Vivo J. Biol. Chem., February 11, 2005; 280(6): 4858 - 4863. [Abstract] [Full Text] [PDF]
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K. P. Becker, K. Kitatani, J. Idkowiak-Baldys, J. Bielawski, and Y. A. Hannun Selective Inhibition of Juxtanuclear Translocation of Protein Kinase C {beta}II by a Negative Feedback Mechanism Involving Ceramide Formed from the Salvage Pathway J. Biol. Chem., January 28, 2005; 280(4): 2606 - 2612. [Abstract] [Full Text] [PDF]
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Z. Liu, H. Lu, Z. Jiang, A. Pastuszyn, and C.-a. A. Hu Apolipoprotein L6, a Novel Proapoptotic Bcl-2 Homology 3-Only Protein, Induces Mitochondria-Mediated Apoptosis in Cancer Cells Mol. Cancer Res., January 1, 2005; 3(1): 21 - 31. [Abstract] [Full Text] [PDF]
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G. Triola, G. Fabrias, M. Dragusin, L. Niederhausen, R. Broere, A. Llebaria, and G. van Echten-Deckert Specificity of the Dihydroceramide Desaturase Inhibitor N-[(1R,2S)-2-Hydroxy-1-hydroxymethyl-2-(2-tridecyl-1-cyclopropenyl)ethyl]octanamide (GT11) in Primary Cultured Cerebellar Neurons Mol. Pharmacol., December 1, 2004; 66(6): 1671 - 1678. [Abstract] [Full Text] [PDF]
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 D. E. Modrak, T. M. Cardillo, G. A. Newsome, D. M. Goldenberg, and D. V. Gold Synergistic Interaction between Sphingomyelin and Gemcitabine Potentiates Ceramide-Mediated Apoptosis in Pancreatic Cancer Cancer Res., November 15, 2004; 64(22): 8405 - 8410. [Abstract] [Full Text] [PDF]
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C. M. Finnegan, S. S. Rawat, A. Puri, J. M. Wang, F. W. Ruscetti, and R. Blumenthal Ceramide, a target for antiretroviral therapy PNAS, October 26, 2004; 101(43): 15452 - 15457. [Abstract] [Full Text] [PDF]
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Y. Yatomi, S. Yamamura, N. Hisano, K. Nakahara, Y. Igarashi, and Y. Ozaki Sphingosine 1-Phosphate Breakdown in Platelets J. Biochem., October 1, 2004; 136(4): 495 - 502. [Abstract] [Full Text] [PDF]
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 N. Abboushi, A. El-Hed, W. El-Assaad, L. Kozhaya, M. E. El-Sabban, A. Bazarbachi, R. Badreddine, A. Bielawska, J. Usta, and G. S. Dbaibo Ceramide Inhibits IL-2 Production by Preventing Protein Kinase C-Dependent NF-{kappa}B Activation: Possible Role in Protein Kinase C{theta} Regulation J. Immunol., September 1, 2004; 173(5): 3193 - 3200. [Abstract] [Full Text] [PDF]
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S. Stratford, K. L. Hoehn, F. Liu, and S. A. Summers Regulation of Insulin Action by Ceramide: DUAL MECHANISMS LINKING CERAMIDE ACCUMULATION TO THE INHIBITION OF Akt/PROTEIN KINASE B J. Biol. Chem., August 27, 2004; 279(35): 36608 - 36615. [Abstract] [Full Text] [PDF]
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C. Blazquez, L. Gonzalez-Feria, L. Alvarez, A. Haro, M. L. Casanova, and M. Guzman Cannabinoids Inhibit the Vascular Endothelial Growth Factor Pathway in Gliomas Cancer Res., August 15, 2004; 64(16): 5617 - 5623. [Abstract] [Full Text] [PDF]
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 R. Bhatia, K. Matsushita, M. Yamakuchi, C. N. Morrell, W. Cao, and C. J. Lowenstein Ceramide Triggers Weibel-Palade Body Exocytosis Circ. Res., August 6, 2004; 95(3): 319 - 324. [Abstract] [Full Text] [PDF]
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K. Matsushita, C. N. Morrell, and C. J. Lowenstein Sphingosine 1-phosphate activates Weibel-Palade body exocytosis PNAS, August 3, 2004; 101(31): 11483 - 11487. [Abstract] [Full Text] [PDF]
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M. Kolaczkowski, A. Kolaczkowska, B. Gaigg, R. Schneiter, and W. S. Moye-Rowley Differential Regulation of Ceramide Synthase Components LAC1 and LAG1 in Saccharomyces cerevisiae Eukaryot. Cell, August 1, 2004; 3(4): 880 - 892. [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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 A. P. Struckhoff, R. Bittman, M. E. Burow, S. Clejan, S. Elliott, T. Hammond, Y. Tang, and B. S. Beckman Novel Ceramide Analogs as Potential Chemotherapeutic Agents in Breast Cancer J. Pharmacol. Exp. Ther., May 1, 2004; 309(2): 523 - 532. [Abstract] [Full Text] [PDF]
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S. Malagarie-Cazenave, B. Segui, S. Leveque, V. Garcia, S. Carpentier, M.-F. Altie, A. Brouchet, V. Gouaze, N. Andrieu-Abadie, Y. Barreira, et al. Role of FAN in Tumor Necrosis Factor-{alpha} and Lipopolysaccharide-induced Interleukin-6 Secretion and Lethality in D-Galactosamine-sensitized Mice J. Biol. Chem., April 30, 2004; 279(18): 18648 - 18655. [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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J. M. Adams II, T. Pratipanawatr, R. Berria, E. Wang, R. A. DeFronzo, M. C. Sullards, and L. J. Mandarino Ceramide Content Is Increased in Skeletal Muscle From Obese Insulin-Resistant Humans Diabetes, January 1, 2004; 53(1): 25 - 31. [Abstract] [Full Text] [PDF]
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 D. J. Powell, E. Hajduch, G. Kular, and H. S. Hundal Ceramide Disables 3-Phosphoinositide Binding to the Pleckstrin Homology Domain of Protein Kinase B (PKB)/Akt by a PKC{zeta}-Dependent Mechanism Mol. Cell. Biol., November 1, 2003; 23(21): 7794 - 7808. [Abstract] [Full Text] [PDF]
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 H. Liang, N. Yao, J. T. Song, S. Luo, H. Lu, and J. T. Greenberg Ceramides modulate programmed cell death in plants Genes & Dev., November 1, 2003; 17(21): 2636 - 2641. [Abstract] [Full Text] [PDF]
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 L. M. Obeid and Y. A. Hannun Ceramide, Stress, and a "LAG" in Aging Sci. Aging Knowl. Environ., October 1, 2003; 2003(39): pe27 - 27. [Abstract] [Full Text]
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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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A. Gidwani, H. A. Brown, D. Holowka, and B. Baird Disruption of lipid order by short-chain ceramides correlates with inhibition of phospholipase D and downstream signaling by Fc{epsilon}RI J. Cell Sci., August 1, 2003; 116(15): 3177 - 3187. [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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S. S. Chirala, H. Chang, M. Matzuk, L. Abu-Elheiga, J. Mao, K. Mahon, M. Finegold, and S. J. Wakil Fatty acid synthesis is essential in embryonic development: Fatty acid synthase null mutants and most of the heterozygotes die in utero PNAS, May 27, 2003; 100(11): 6358 - 6363. [Abstract] [Full Text] [PDF]
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B.-J. Kroesen, S. Jacobs, B. J. Pettus, H. Sietsma, J. W. Kok, Y. A. Hannun, and L. F. M. H. de Leij BcR-induced Apoptosis Involves Differential Regulation of C16 and C24-Ceramide Formation and Sphingolipid-dependent Activation of the Proteasome J. Biol. Chem., April 18, 2003; 278(17): 14723 - 14731. [Abstract] [Full Text] [PDF]
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R. Barsacchi, C. Perrotta, S. Bulotta, S. Moncada, N. Borgese, and E. Clementi Activation of Endothelial Nitric-Oxide Synthase by Tumor Necrosis Factor-alpha : A Novel Pathway Involving Sequential Activation of Neutral Sphingomyelinase, Phosphatidylinositol-3' kinase, and Akt Mol. Pharmacol., April 1, 2003; 63(4): 886 - 895. [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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D. E. Muscarella and S. E. Bloom Cross-linking of Surface IgM in the Burkitt's Lymphoma Cell Line ST486 Provides Protection against Arsenite- and Stress-induced Apoptosis That Is Mediated by ERK and Phosphoinositide 3-Kinase Signaling Pathways J. Biol. Chem., January 31, 2003; 278(6): 4358 - 4367. [Abstract] [Full Text] [PDF]
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G. Liu, L. Robillard, B. Banihashemi, and P. R. Albert Growth Hormone-induced Diacylglycerol and Ceramide Formation via Galpha i3 and Gbeta gamma in GH4 Pituitary Cells. POTENTIATION BY DOPAMINE-D2 RECEPTOR ACTIVATION J. Biol. Chem., December 6, 2002; 277(50): 48427 - 48433. [Abstract] [Full Text] [PDF]
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C. Garcia-Ruiz, A. Colell, A. Morales, M. Calvo, C. Enrich, and J. C. Fernandez-Checa Trafficking of Ganglioside GD3 to Mitochondria by Tumor Necrosis Factor-alpha J. Biol. Chem., September 20, 2002; 277(39): 36443 - 36448. [Abstract] [Full Text] [PDF]
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A. H. Merrill Jr. De Novo Sphingolipid Biosynthesis: A Necessary, but Dangerous, Pathway J. Biol. Chem., July 12, 2002; 277(29): 25843 - 25846. [Full Text] [PDF]
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S. Spiegel and S. Milstien Sphingosine 1-Phosphate, a Key Cell Signaling Molecule J. Biol. Chem., July 12, 2002; 277(29): 25851 - 25854. [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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