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Information on EC 2.3.1.297 - very-long-chain ceramide synthase and Organism(s) Homo sapiens and UniProt Accession Q96G23
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2.3.1.297 very-long-chain ceramide synthaseIUBMB Comments
This entry describes ceramide synthase enzymes that are specific for very-long-chain fatty acyl-CoA substrates. The two isoforms from yeast and the plant LOH1 and LOH3 isoforms transfer 24:0 and 26:0 acyl chains preferentially and use phytosphingosine as the preferred sphingoid base. The mammalian CERS2 isoform is specific for acyl donors of 20-26 carbons, which can be saturated or unsaturated. The mammalian CERS3 isoform catalyses this activity, but has a broader substrate range and also catalyses the activity of EC 2.3.1.298, ultra-long-chain ceramide synthase. Both mammalian enzymes can use multiple sphingoid bases, including sphinganine, sphingosine, and phytosphingosine.
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Word Map
- 2.3.1.297
- sphingolipids
- sphingomyelins
- dihydroceramide
-
cers1-6
- elovl1
- pnpla1
- cyp4f22
- alox12b
-
sdr9c7
-
nipal4
-
abca12
-
cerss
- aloxe3
- diagnostics
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
a very-long-chain fatty acyl-CoA
+
=
a very-long-chain ceramide
+
Synonyms
cers2, lass2, cers3, ceramide synthase 2, ceramide synthase 3, lass4, lass3, longevity assurance homologue 2, lag13, lag11, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ceramide synthase 2
-
CerS3
LAC1
-
-
-
-
LAG1
-
-
-
-
LASS3
-
-
-
-
LOH1
-
-
-
-
LOH3
-
-
-
-
mammalian ceramide synthase 2
-
-
-
-
sphingoid base N-very-long-chain fatty acyl-coA transferase
-
-
-
-
CerS3
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
very-long-chain fatty acyl-coA:sphingoid base N-acyltransferase
This entry describes ceramide synthase enzymes that are specific for very-long-chain fatty acyl-CoA substrates. The two isoforms from yeast and the plant LOH1 and LOH3 isoforms transfer 24:0 and 26:0 acyl chains preferentially and use phytosphingosine as the preferred sphingoid base. The mammalian CERS2 isoform is specific for acyl donors of 20-26 carbons, which can be saturated or unsaturated. The mammalian CERS3 isoform catalyses this activity, but has a broader substrate range and also catalyses the activity of EC 2.3.1.298, ultra-long-chain ceramide synthase. Both mammalian enzymes can use multiple sphingoid bases, including sphinganine, sphingosine, and phytosphingosine.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
behenoyl-CoA + dihydrosphingosine
CoA + N-behenoyldihydrosphingosine
-
-
-
?
dihydrosphingosine + palmitoyl-CoA
N-palmitoyldihydrosphingosine + CoA
low activity
-
-
?
dihydrosphingosine + stearoyl-CoA
N-stearoyldihydrosphingosine + CoA
low activity
-
-
?
sphinganine + lignoceroyl-CoA
N-lignoceroylsphinganine + CoA
-
-
-
?
sphingosine + 2-hydroxybehenoyl-CoA
N-2-hydroxybehenoylsphingosine + CoA
-
-
-
?
sphingosine + 2-hydroxylignoceroyl-CoA
N-2-hydroxylignoceroylsphingosine + CoA
-
-
-
?
a very-long-chain fatty acyl-CoA + sphinganine
a very-long-chain sphinganine + CoA
-
-
-
-
?
sphingosine + 2-hydroxybehenoyl-CoA
N-2-hydroxybehenoylsphingosine + CoA
-
-
-
?
sphingosine + 2-hydroxyeicosanoyl-CoA
N-2-hydroxyeicosanoylsphingosine + CoA
-
-
-
?
sphingosine + 2-hydroxylignoceroyl-CoA
N-2-hydroxylignoceroylsphingosine + CoA
-
-
-
?
sphingosine + eicosanoyl-CoA
N-eicosanoylsphingosine + CoA
-
-
-
?
sphingosine + lignoceroyl-CoA
N-lignoceroylsphingosine + CoA
-
-
-
?
dihydrosphingosine + lignoceroyl-CoA
N-lignoceroyldihydrosphingosine + CoA
-
-
-
?
dihydrosphingosine + lignoceroyl-CoA
N-lignoceroyldihydrosphingosine + CoA
low activity
-
-
?
dihydrosphingosine + nervonoyl-CoA
N-nervonoyldihydrosphingosine + CoA
-
-
-
?
dihydrosphingosine + nervonoyl-CoA
N-nervonoyldihydrosphingosine + CoA
highly preferred substrate
-
-
?
sphingosine + lignoceroyl-CoA
N-lignoceroylsphingosine + CoA
-
-
-
?
additional information
?
-
CERS2 preferentially transfers very long chain fatty acids (C22-C26)
-
-
?
additional information
?
-
CERS activity is assayed using LC-MS/MS for product quantification, crude extracts containing cell membranes are firstly prepared from tissues or cultured cells, reactions contain deuterated dihydrosphingosine (or sphingosine) and a fatty acid substrate linked to CoA (C16:0 to C24:0/24:1), detailed method descritpion and evaluation, overview
-
-
?
additional information
?
-
CERS2 preferentially transfers very long chain fatty acids (C22:0-C26:0) to dihydrosphingosine. Improvement of a fluorescent assay, using HPLC using C16:0, C18:0 and C24:1 fatty acids and commercially available sphinganine-NBD, i.e. 7-nitro-2-1,3-benzoxadiazole-labelled dihydrosphingosine or (2S,3R)-2-amino-18((7-nitrobenzo[c][1,2,5]oxadiazol-4-yl)amino)octadecane-1-3-diol, as substrates, very accurate and sensitive method for quantification of CERS activity, method evaluation
-
-
?
additional information
?
-
substrate specificity, overview. Long-chain preference of CerS2
-
-
?
additional information
?
-
substrate specificity, overview. Long-chain preference of CerS2
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
behenoyl-CoA + dihydrosphingosine
CoA + N-behenoyldihydrosphingosine
-
-
-
?
dihydrosphingosine + lignoceroyl-CoA
N-lignoceroyldihydrosphingosine + CoA
-
-
-
?
dihydrosphingosine + nervonoyl-CoA
N-nervonoyldihydrosphingosine + CoA
-
-
-
?
sphinganine + lignoceroyl-CoA
N-lignoceroylsphinganine + CoA
-
-
-
?
a very-long-chain fatty acyl-CoA + sphinganine
a very-long-chain sphinganine + CoA
-
-
-
-
?
sphingosine + eicosanoyl-CoA
N-eicosanoylsphingosine + CoA
-
-
-
?
sphingosine + lignoceroyl-CoA
N-lignoceroylsphingosine + CoA
-
-
-
?
additional information
?
-
CERS2 preferentially transfers very long chain fatty acids (C22-C26)
-
-
?
sphingosine + lignoceroyl-CoA
N-lignoceroylsphingosine + CoA
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FTY720
inhibits ceramide synthases and upregulates dihydrosphingosine 1-phosphate formation in human lung endothelial cells. FTY720 is a sphingosine analogue and in clinical trials as an immunomodulator. Multifaceted mode of interaction between FTY720 and CerS. FTY720 itself and not FTY720-P, is responsible for CerS2 inhibition. FTY720 inhibits ceramide synthesis using C18-CoA to a greater extent than other acyl-CoAs. Sphinganine first binds to CerS to form an E-S (CerS-sphinganine) complex, and only after formation of this complex can FTY720 bind. The binding sites of FTY720 and acyl-CoA appear to be distinct, but the interaction between sphinganine binding and FTY720 binding nevertheless impacts the rate of the reaction with respect to acyl-CoA. FTY720 inhibits ceramide synthesis at high sphinganine concentrations in vivo, but not at low concentrations, supporting a complex, possibly allosteric mode of interaction between sphinganine and FTY720 and is consistent with uncompetitive inhibitors being most effective at high substrate concentrations. Inhibition of CerS2 by FTY720 does not occur via a nonspecific mechanism
sphingosine 1-phosphate
significantly inhibits CerS2, CerS2 contains a sphingosine 1-phosphate receptor-like motif via which sphingosine 1-phosphate inhibits CerS2 activity
FTY720
-
FTY720 is an effective immunomodulatory molecule and is a competitive inhibitor of ceramide synthase 2 toward dihydrosphingosine, it shows interference with sphingolipid de novo biosynthesis, overview. The inhibition of CerS2 activity is reversible as the potency of inhibition diminishes with the dilution of the enzyme-inhibitor preparation
additional information
in contrast to the dual effects of fumonisin B1, which is only observed in cells overexpressing CerS, FTY720 elevates ceramide levels in untransfected cells. Lysophosphatidic acid does not inhibit CerS2. Dimethylsphingosine has no effect on CerS2 activity
-
fumonisin B1
inhibits the increase in total cellular ceramide induced by UV-C irradiation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
nonlinear fitting and Michaelis-Menten kinetic analyses
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
isozymes CerS2 (EC 2.3.1.297) and CerS6 (EC 2.3.1.24) mRNA is significantly elevated in breast cancer tissue compared to normal tissue, with approximately half of the individuals showing elevated CerS2 and CerS6 mRNA. A significant correlation is found between CerS2 and CerS6 isozyme expression, and between isozymes CerS4 (EC 2.3.1.24) and CerS2/CerS6 expression
epidermal, expression analysis of the CerS family members during keratinocyte differentiation, overview. Expression of CerS2 mRNA remains nearly unchanged during differentiation
CerS2 and CerS6 are the major very long-chain and long-chain CerS isoforms in MCF-7 cells, respectively
epidermal, expression analysis of the CerS family members during keratinocyte differentiation, overview. A slight increase in CerS4 mRNA is observed at the late stage of differentiation
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
profiles of non-hydroxylated and 2-hydroxy-ceramides in transgenic HeLa cells expressing different CerS isozymes and or different specific interfence RNAs, overview
physiological function
differences in the expression patterns of CerS family members may play an important role in the production of the CER/2-hydroxy ceramide (CER) compositions of different chain lengths observed in different cell types and even in the altered production that occurring during keratinocyte differentiation
additional information
chimeric mutant CerS5:TM:CerS2-HA displays slightly more activity using C16-CoA as substrate than CerS5, but remarkably, CerS2 activity measured using C22-CoA is elevated by 3fold. Isozymes CerS5 and CerS6 modulate CerS2 activity upon co-expression. This increase in CerS2 activity is abolished using a noncatalytically active form of CerS5 in the constitutive dimer (CerS5HH:TM:CerS2-HA), demonstrating that optimal CerS2 activity depends on an interaction with a catalytically active form of CerS5
malfunction
in HeLa cells overproducing the fatty acid 2-hydroxylase FA2H, knockdown of CerS2 results in a reduction in total long-chain 2-hydroxy-ceramides, confirming enzyme substrate specificity for chain length. Profiles of non-hydroxylated and 2-hydroxy-ceramides in transgenic HeLa cells expressing different CerS isozymes and or different specific interfence RNAs, overview
malfunction
inhibition of CerS is able to protect from cell death. Moreover, this protection occurs downstream or independently of mitochondrial permeabilization. Inhibition of CerS greatly inhibits plasma membrane permeabilization. Individual CerS knockdown does not significantly inhibit total ceramide accumulation. Knockdown of CerS2 in untreated cells reduces very long-chain Cer and increases long-chain Cer both in untreated and UV-C-treated cells. Inhibition of CerS but not de novo synthesis inhibits plasma membrane rupture that is not specific to UV-C irradiation or MCF-7 cells
malfunction
overexpression of CerS2 results in partial protection from IR-induced apoptosis. Knockdown studies determines that CerS2 is responsible for all observable IR-induced C24:0 CerS activity. CerS2 and CerS5 overexpression significantly alters apoptosis
metabolism
regulation of CerS isozymes, overview. The interplay among the CerS proteins takes place in a stress stimulus-, cell type-, and subcellular compartment-specific manner. CerS2 and CerS5 overexpression significantly alters apoptosis. Determination of ionizing radiation-induced mitochondrial ceramide elevations via CerS2, 5, and 6, overview. CerS2 and CerS5 overexpressions defines opposing roles in radiation-induced mitochondrial apoptosis
metabolism
regulation of sphingolipid metabolism by UV-C irradiation, overview. Ceramide species that are the least abundant (e.g. C18-Cer, C18:1-Cer, C20-Cer, C22:1-Cer, etc.) exhibit the greatest fold increases. More abundant ceramide species (e.g. C16-Cer, C24-Cer, and C24:1-Cer) show more modest fold changes, although they account for much more of the overall increase in ceramides
physiological function
ceramides are synthesized by ceramide synthases through the addition of a variable length fatty acid to the amine group of a sphingoid base. In mammalian cells, the sphingoid base used for de novo ceramide synthesis is usually the C18:0 lipid dihydrosphingosine. Ceramide synthesis is catalyzed by a family of six ceramide synthases (CERS1-6), each of which preferentially transfers fatty acids of different lengths to the amine group of dihydrosphingosine
physiological function
differences in the expression patterns of CerS family members may play an important role in the production of the CER/2-hydroxy ceramide (CER) compositions of different chain lengths observed in different cell types and even in the altered production that occurring during keratinocyte differentiation
physiological function
selective tissue and subcellular distribution of the six mammalian CerS isoforms, combined with distinct fatty acyl chain length substrate preferences, implicate differential functions of specific ceramide species in cellular signaling. Ionizing radiation (IR) induces de novo synthesis of ceramide to influence HeLa cell apoptosis by specifically activating isozymes CerS isoforms 2, 5, and 6 that generate opposing anti- and pro-apoptotic ceramides in mitochondrial membranes. Isozyme CerS2 is responsible for all observable IR-induced C24:0 CerS activity. IR-induced CerS-mediated ceramide generation, and subsequent apoptosis, occurs in a cell-type specific manner. CerS2 and CerS5 overexpressions defines opposing roles in radiation-induced mitochondrial apoptosis
physiological function
sphingolipid ceramides are widely implicated in the regulation of programmed cell death or apoptosis. CerS2 regulates very long-chain Cer synthesis. CerS2 and CerS6 are the major very long-chain and long-chain CerS isoforms in MCF-7 cells, respectively
physiological function
very long chain ceramides synthesized by CERS2 are essential constituents of myelin. CERS2 demonstrates a preference for the monounsaturated C24:1 fatty acid substrate compared to the saturated C24:0 substrate, potentially explaining why myelin is enriched in ceramides containing the monounsaturated form of very long chain fatty acids
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CERS2_HUMAN
380
5
44876
Swiss-Prot
Secretory Pathway (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer CerS activity can be modulated by dimer formation. CerS2 activity is enhanced by co-expression with a catalytically active form of CerS5 or CerS6. CerS dimers are formed rapidly upon stimulation of ceramide synthesis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
cloning of a chimeric HA-tagged CerS5:CerS2 isozymes heterodimer, insertion of a transmembrane (TM) domain3 between the two monomers of the dimer (CerS5:TM:CerS5-HA). Chimeric mutant CerS5:TM:CerS2-HA displays slightly more activity using C16-CoA as substrate than CerS5, but remarkably, CerS2 activity measured using C22-CoA is elevated by 3fold. Isozymes CerS5 and CerS6 modulate CerS2 activity upon coexpression. This increase in CerS2 activity is abolished using a noncatalytically active form of CerS5 in the constitutive dimer (CerS5HH:TM:CerS2-HA), demonstrating that optimal CerS2 activity depends on an interaction with a catalytically active form of CerS5
additional information
in HeLa cells overproducing the fatty acid 2-hydroxylase FA2H, knockdown of CerS2 by siRNA results in a reduction in total long-chain 2-hydroxy-ceramides, confirming enzyme substrate specificity for chain length. Profiles of non-hydroxylated and 2-hydroxy-ceramides in transgenic HeLa cells expressing different CerS isozymes and or different specific interfence RNAs, overview
additional information
in HeLa cells overproducing the fatty acid 2-hydroxylase FA2H, knockdown of CerS2 by siRNA results in a reduction in total long-chain 2-hydroxy-ceramides, confirming enzyme substrate specificity for chain length. Profiles of non-hydroxylated and 2-hydroxy-ceramides in transgenic HeLa cells expressing different CerS isozymes and or different specific interfence RNAs, overview
additional information
profiles of non-hydroxylated and 2-hydroxy-ceramides in transgenic HeLa cells expressing different CerS isozymes and or different specific interfence RNAs, overview
additional information
profiles of non-hydroxylated and 2-hydroxy-ceramides in transgenic HeLa cells expressing different CerS isozymes and or different specific interfence RNAs, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
subcellular fractionation of HeLa cells recombinantly expressing the CerS isozyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CERS2, recombinant expression in HEK-293T cells, quantitative real-time quantitative PCR enzyme expression analysis
gene CERS2, recombinant expression of C-terminally HA-tagged CerS2 and of chimeric HA-tagged CerS5:CerS2 heterodimer in HEK-293 cells, recombinant expression of FLAG-tagged CerS2 in HEK-293 cells. Isozymes CerS5 and CerS6 modulate CerS2 activity upon coexpression
gene CERS2, recombinant FLAG-tagged isozyme overexpression in HeLa cells, quantitative real-time PCR enzyme expression analysis. CerS2, CerS5, and CerS6 form heterocomplexes in transformed HeLa cells
gene CERS4, recombinant expression in HEK-293T cells, quantitative real-time quantitative PCR enzyme expression analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ionizing radiation (IR) induces de novo synthesis of ceramide by specifically activating CerS isoforms 2, 5, and 6
the mRNA level of the enzyme increases 1.23fold in the presence of 0.03 mM Asterias amurensis-derived sphingoid bases
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant HA-tagged chimeric mutant CerS5:TM:CerS2 is reconstituted in 1,2-dioleoyl-sn-glycero-3-phosphocholine liposomes
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
important role for the CerS genes in breast cancer etiology or diagnosis, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Erez-Roman, R.; Pienik, R.; Futerman, A.H.
Increased ceramide synthase 2 and 6 mRNA levels in breast cancer tissues and correlation with sphingosine kinase expression
Biochem. Biophys. Res. Commun.
391
219-223
2010
Homo sapiens (Q96G23), Homo sapiens
Mesicek, J.; Lee, H.; Feldman, T.; Jiang, X.; Skobeleva, A.; Berdyshev, E.V.; Haimovitz-Friedman, A.; Fuks, Z.; Kolesnick, R.
Ceramide synthases 2, 5, and 6 confer distinct roles in radiation-induced apoptosis in HeLa cells
Cell. Signal.
22
1300-1307
2010
Homo sapiens (Q96G23)
Lahiri, S.; Park, H.; Laviad, E.L.; Lu, X.; Bittman, R.; Futerman, A.H.
Ceramide synthesis is modulated by the sphingosine analog FTY720 via a mixture of uncompetitive and noncompetitive inhibition in an Acyl-CoA chain length-dependent manner
J. Biol. Chem.
284
16090-16098
2009
Homo sapiens (Q96G23)
Berdyshev, E.V.; Gorshkova, I.; Skobeleva, A.; Bittman, R.; Lu, X.; Dudek, S.M.; Mirzapoiazova, T.; Garcia, J.G.; Natarajan, V.
FTY720 inhibits ceramide synthases and up-regulates dihydrosphingosine 1-phosphate formation in human lung endothelial cells
J. Biol. Chem.
284
5467-5477
2009
Homo sapiens
Mullen, T.D.; Jenkins, R.W.; Clarke, C.J.; Bielawski, J.; Hannun, Y.A.; Obeid, L.M.
Ceramide synthase-dependent ceramide generation and programmed cell death involvement of salvage pathway in regulating postmitochondrial events
J. Biol. Chem.
286
15929-15942
2011
Homo sapiens (Q96G23)
Laviad, E.L.; Kelly, S.; Merrill, A.H.; Futerman, A.H.
Modulation of ceramide synthase activity via dimerization
J. Biol. Chem.
287
21025-21033
2012
Homo sapiens (Q96G23)
Mizutani, Y.; Kihara, A.; Chiba, H.; Tojo, H.; Igarashi, Y.
2-Hydroxy-ceramide synthesis by ceramide synthase family enzymatic basis for the preference of FA chain length
J. Lipid Res.
49
2356-2364
2008
Homo sapiens (Q96G23), Homo sapiens (Q9HA82)
Couttas, T.A.; Lim, X.Y.; Don, A.S.
A three-step assay for ceramide synthase activity using a fluorescent substrate and HPLC
Lipids
50
101-109
2015
Homo sapiens (Q96G23)
Lim, X.Y.; Pickford, R.; Don, A.S.
Assaying ceramide synthase activity in vitro and in living cells using liquid chromatography-mass spectrometry
Methods Mol. Biol.
1376
11-22
2016
Homo sapiens (Q96G23)
Mikami, D.; Sakai, S.; Sasaki, S.; Igarashi, Y.
Effects of Asterias amurensis-derived sphingoid bases on the de novo ceramide synthesis in cultured normal human epidermal keratinocytes
J. Oleo Sci.
65
671-680
2016
Homo sapiens
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