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Information on EC 3.1.1.3 - triacylglycerol lipase and Organism(s) Mus musculus and UniProt Accession Q8BJ56
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3.1.1.3 triacylglycerol lipaseIUBMB Comments
The enzyme is found in diverse organisms including animals, plants, fungi, and bacteria. It hydrolyses triglycerides into diglycerides and subsequently into monoglycerides and free fatty acids. The enzyme is highly soluble in water and acts at the surface of oil droplets. Access to the active site is controlled by the opening of a lid, which, when closed, hides the hydrophobic surface that surrounds the active site. The lid opens when the enzyme contacts an oil-water interface (interfacial activation). The pancreatic enzyme requires a protein cofactor, namely colipase, to counteract the inhibitory effects of bile salts.
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Word Map
- 3.1.1.3
- amylase
- lipoprotein
- pancreas
- triacylglycerols
-
lipolytic
- phospholipid
- antarctica
- esterification
- obesity
- abdominal
- hdl
-
biocatalyst
-
apolipoproteins
- pain
-
exocrine
- adipocytes
-
oleic
- milk
-
cholesteryl
- droplet
- palmitate
- meal
- phosphatidylcholine
-
high-density
- p-nitrophenyl
-
hormone-sensitive
- olive
-
acinar
- duodenal
-
enantioselectivity
-
obese
- hypertriglyceridemia
-
interfacial
-
phosphatidic
-
esterify
-
micelle
- juice
-
arachidonic
-
emulsify
- oleate
-
postprandial
-
endoscopic
- cholecystokinin
-
reusable
- lecithin
- hexane
-
endocannabinoids
-
hdl-cholesterol
- taurocholate
- trypsinogen
- detergent
- synthesis
- paper production
- nutrition
- food industry
- environmental protection
- biofuel production
- medicine
- biotechnology
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
lipase, acyltransferase, pancreatic lipase, hepatic lipase, adipose triglyceride lipase, cholesterol esterase, lipase b, triglyceride lipase, tgl, diacylglycerol lipase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
amano AP
-
-
-
-
amano B
-
-
-
-
amano CE
-
-
-
-
amano CES
-
-
-
-
amano P
-
-
-
-
amno N-AP
-
-
-
-
BAL
-
-
-
-
Bile-salt-stimulated lipase
-
-
-
-
BSSL
-
-
-
-
butyrinase
-
-
-
-
cacordase
-
-
-
-
CALB
-
-
-
-
capalase L
-
-
-
-
Carboxyl ester lipase
-
-
-
-
cholesterol esterase
-
-
-
-
Cytotoxic T lymphocyte lipase
-
-
-
-
EDL
-
-
-
-
endothelial cell-derived lipase
-
-
-
-
endothelial-derived lipase
-
-
-
-
GA 56 (enzyme)
-
-
-
-
Gastric lipase
-
-
-
-
GEH
-
-
-
-
glycerol ester hydrolase
-
-
-
-
glycerol-ester hydrolase
-
-
-
-
heparin releasable hepatic lipase
-
-
-
-
hepatic lipase
hepatic monoacylglycerol acyltransferase
-
-
-
-
Lingual lipase
-
-
-
-
lipase
lipase, triacylglycerol
-
-
-
-
lipazin
-
-
-
-
liver lipase
-
-
-
-
meito MY 30
-
-
-
-
meito Sangyo OF lipase
-
-
-
-
Pancreatic lipase
-
-
-
-
Pancreatic lysophospholipase
-
-
-
-
PGE
-
-
-
-
PL-RP2
-
-
-
-
post-heparin plasma protamine-resistant lipase
-
-
-
-
PPL
-
-
-
-
Pregastric esterase
-
-
-
-
Pregastric lipase
-
-
-
-
salt-resistant post-heparin lipase
-
-
-
-
steapsin
-
-
-
-
Sterol esterase
-
-
-
-
takedo 1969-4-9
-
-
-
-
teenesterase
-
-
-
-
tiacetinase
-
-
-
-
tibutyrin esterase
-
-
-
-
triacylglycerol ester hydrolase
-
-
-
-
Triacylglycerol lipase
-
-
-
-
tributyrase
-
-
-
-
tributyrinase
-
-
-
-
triglyceridase
-
-
-
-
triglyceride hydrolase
-
-
-
-
triglyceride lipase
-
-
-
-
triolein hydrolase
-
-
-
-
tween hydrolase
-
-
-
-
tween-hydrolyzing esterase
-
-
-
-
Tweenase
-
-
-
-
hepatic lipase
-
-
-
-
lipase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
triacylglycerol + H2O = diacylglycerol + a carboxylate
active site structure, reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
triacylglycerol acylhydrolase
The enzyme is found in diverse organisms including animals, plants, fungi, and bacteria. It hydrolyses triglycerides into diglycerides and subsequently into monoglycerides and free fatty acids. The enzyme is highly soluble in water and acts at the surface of oil droplets. Access to the active site is controlled by the opening of a lid, which, when closed, hides the hydrophobic surface that surrounds the active site. The lid opens when the enzyme contacts an oil-water interface (interfacial activation). The pancreatic enzyme requires a protein cofactor, namely colipase, to counteract the inhibitory effects of bile salts.
CAS REGISTRY NUMBER
COMMENTARY
9001-62-1
-
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
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
the enzyme specifically generates sn-1,3 and, in the presence of its co-activator CGI-58, sn-1,3 and sn-2,3 diacylglycerol
-
?
additional information
?
-
lipolysis is regulated by the opposing functions of the enzyme ATGL and adiponutrin, overview
-
-
?
additional information
?
-
-
lipolysis is regulated by the opposing functions of the enzyme ATGL and adiponutrin, overview
-
-
?
additional information
?
-
-
the enzyme is involved in basal lipolysis of storage triacylglycerides, and hormonally as well as developmentally regulated, the hormone-sensitive lipase is negatively regulated by perilipin in adipose tissue, physiological functions, role in apoB-containing lipoprotein assembly in the endoplasmic reticulum, overview
-
-
?
additional information
?
-
-
ATGL and diacylglycerol acyltransferase-1, DGAT-1, may be cooperatively involved in rosiglitazone-stimulated triglyceride hydrolysis and fatty acid re-esterification in 3T3-L1 adipocytes, overview
-
-
?
additional information
?
-
-
ATGL and hormone sensitive lipase, HSL, regulate lipolysis in a serial manner, with ATGL cleaving the first fatty acid and HSL the second fatty acid of triacylglycerol, lipolysis control, detailed overview
-
-
?
additional information
?
-
-
ATGL selectively performs the first step in triacylglyceride hydrolysis resulting in the formation of diacylglyceride and free fatty acid. The specific activity against triacylglycerides is more than 10fold higher than against diacylglyceride, and the enzyme shows essentially no hydrolytic activity when other lipid substrates are used such as cholesteryl esters or retinyl esters. Molecular mechanisms that regulate ATGL activity, detailed overview
-
-
?
additional information
?
-
-
HSL translocates from the cytoplasm to the lipid droplet surface and interacts with Peri A in stimulated lipolysis
-
-
?
additional information
?
-
-
structure, function, and regulation of ATGL and HSL, overview
-
-
?
additional information
?
-
-
ATGL binds to the pigment epithelium derived factor
-
-
?
additional information
?
-
-
ATGLalso possesses phospholipase and transacylase activity
-
-
?
additional information
?
-
-
the enzyme hydrolyzes long-chain fatty acid esters in vivo with a modest substrate preference for C16:1
-
-
?
additional information
?
-
-
the enzyme lacks the ability to hydrolyze diacylglycerols, monoacylglycerols, cholesteryl esters, or retinyl esters
-
-
?
additional information
?
-
-
the enzyme lacks the ability to hydrolyze monoacylglycerol, CEs, or retinyl esters
-
-
?
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
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
the enzyme specifically generates sn-1,3 and, in the presence of its co-activator CGI-58, sn-1,3 and sn-2,3 diacylglycerol
-
?
additional information
?
-
lipolysis is regulated by the opposing functions of the enzyme ATGL and adiponutrin, overview
-
-
?
additional information
?
-
-
lipolysis is regulated by the opposing functions of the enzyme ATGL and adiponutrin, overview
-
-
?
additional information
?
-
-
the enzyme is involved in basal lipolysis of storage triacylglycerides, and hormonally as well as developmentally regulated, the hormone-sensitive lipase is negatively regulated by perilipin in adipose tissue, physiological functions, role in apoB-containing lipoprotein assembly in the endoplasmic reticulum, overview
-
-
?
additional information
?
-
-
ATGL and diacylglycerol acyltransferase-1, DGAT-1, may be cooperatively involved in rosiglitazone-stimulated triglyceride hydrolysis and fatty acid re-esterification in 3T3-L1 adipocytes, overview
-
-
?
additional information
?
-
-
ATGL and hormone sensitive lipase, HSL, regulate lipolysis in a serial manner, with ATGL cleaving the first fatty acid and HSL the second fatty acid of triacylglycerol, lipolysis control, detailed overview
-
-
?
additional information
?
-
-
ATGL selectively performs the first step in triacylglyceride hydrolysis resulting in the formation of diacylglyceride and free fatty acid. The specific activity against triacylglycerides is more than 10fold higher than against diacylglyceride, and the enzyme shows essentially no hydrolytic activity when other lipid substrates are used such as cholesteryl esters or retinyl esters. Molecular mechanisms that regulate ATGL activity, detailed overview
-
-
?
additional information
?
-
-
HSL translocates from the cytoplasm to the lipid droplet surface and interacts with Peri A in stimulated lipolysis
-
-
?
additional information
?
-
-
structure, function, and regulation of ATGL and HSL, overview
-
-
?
additional information
?
-
-
the enzyme hydrolyzes long-chain fatty acid esters in vivo with a modest substrate preference for C16:1
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(4-chlorophenyl)-1-methyl-3-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]urea
-
-
1-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]-3-[(1S)-1-phenylethyl]urea
-
-
deoxycholate
-
no carboxyl esterase activity in presence of 2-hydroxy bile salts, such as deoxycholate and taurodeoxycholate
N-(2-methoxyethyl)-N,5-dimethyl-4-[(phenylcarbamoyl)amino]furan-2-sulfonamide
-
-
taurodeoxycholate
-
no carboxyl esterase activity in presence of 2-hydroxy bile salts, such as deoxycholate and taurodeoxycholate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
perilipin A
-
phosphorylation of perilipin specifically at serine 517 by protein kinase A is essential for ATGL activation, overview
-
CGI-58
-
ATGL activity is greatly enhanced by the protein annotated as alpha/beta hydrolase domain-containing protein 5, ABHD5, or comparative gene identification-58, CGI-58. CGI-58 does not affect HSL enzyme activity
-
CGI-58
-
ATGL binds to CGI-58, and ATGL activity is strongly stimulated, about 20fold, by an activator protein annotated as alpha/beta hydrolase domain containing protein 5, ABHD5, also known as comparative gene identification-58, CGI-58. Phosphorylation of perilipin interferes with CGI-58 interaction in vitro and in vivo
-
CGI-58
-
for maximal lipolytic activity the enzyme requires CGI-58 as a co-activator
-
additional information
-
hepatic lipase activity increases with increased visceral fat
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00013
1-(2-chlorophenyl)-3-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]urea
Mus musculus
-
-
0.05
1-(4-chlorophenyl)-1-methyl-3-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]urea
Mus musculus
-
IC50 above 0.05 mM
0.0002
1-(4-chlorophenyl)-3-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]urea
Mus musculus
-
-
0.00013
1-(4-methoxyphenyl)-3-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]urea
Mus musculus
-
-
0.00016
1-(diphenylmethyl)-3-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]urea
Mus musculus
-
-
0.05
1-benzyl-3-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]urea
Mus musculus
-
IC50 above 0.05 mM
0.025
1-methyl-1-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]-3-phenylurea
Mus musculus
-
-
0.05
1-methyl-3-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]-1-phenylurea
Mus musculus
-
IC50 above 0.05 mM
0.05
1-[1,2-dimethyl-5-(piperidin-1-ylsulfonyl)-1H-pyrrol-3-yl]-3-phenylurea
Mus musculus
-
IC50 above 0.05 mM
0.05
1-[1-methyl-3-(piperidin-1-ylsulfonyl)-1H-pyrazol-5-yl]-3-phenylurea
Mus musculus
-
IC50 above 0.05 mM
0.05
1-[2,4-dimethyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]-3-phenylurea
Mus musculus
-
IC50 above 0.05 mM
0.05
1-[2-methyl-4-(morpholin-4-ylsulfonyl)phenyl]-3-phenylurea
Mus musculus
-
IC50 above 0.05 mM
0.05
1-[2-methyl-5-(piperidin-1-ylsulfonyl)-1H-pyrrol-3-yl]-3-phenylurea
Mus musculus
-
IC50 above 0.05 mM
0.00006
1-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]-3-[(1S)-1-phenylethyl]urea
Mus musculus
-
-
0.0013
1-[2-methyl-5-[(4-methylpiperazin-1-yl)sulfonyl]furan-3-yl]-3-phenylurea
Mus musculus
-
-
0.05
1-[2-methyl-6-(piperidin-1-ylsulfonyl)pyridin-3-yl]-3-phenylurea
Mus musculus
-
IC50 above 0.05 mM
0.05
2-methyl-N-phenyl-5-(piperidin-1-ylsulfonyl)furan-3-carboxamide
Mus musculus
-
IC50 above 0.05 mM
0.00025
N-(2-methoxyethyl)-N,5-dimethyl-4-[(phenylcarbamoyl)amino]furan-2-sulfonamide
Mus musculus
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
adipocytes, enzyme expression during differentiation of adipocytes, maximal at day 8, overview
-
ATGL is highly expressed in the pigment epithelium and can be found on the plasma membrane
additional information
-
hormone-sensitive lipase is negatively regulated by perilipin, lipolysis of storage triacylglycerides
additional information
-
no expression in brain, skeletal muscle, or spleen, tissue-specific functions, expression is developmentally regulated, detailed overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
ATGL-deficiency decreases the release of fatty acids from white adipose tissue by about 70% in response to isoproterenol treatment, and this decreased lipolytic rate results in substantially reduced plasma fatty acid levels in ATGL-KO mice. Moreover, ATGL deficient mice are extremely cold-sensitive. Upon fasting, they reduce their oxygen consumption and drop their body temperature, phenotype, overview
malfunction
-
hepatic lipase deficiency reduces body fate stores and protects against diet-induced obesity
malfunction
-
enzyme-deficient mice show an increased utilization of carbohydrates as an energy source, leading to improved glucose tolerance and insulin sensitivity. Enzyme-deficient male mice are fertile, whereas females lack the ability to suckle their offspring due to impaired milk production. Enzyme-deficient mice exhibit defective thermogenesis in brown adipose tissue. Enzyme-deficient macrophages accumulate triacylglycerol-rich lipid droplets resulting in altered cell morphology that resemble macrophage foam cells. ATGL deficiency attenuates the mRNA expression of the proinflammatory chemokine (C-X-C motif) ligand 1 (Gro1) and the release of interleukin-6 from macrophages. Enzyme deficiency limits adipose tissue macrophage accumulation during fasting
malfunction
-
the absence of adipose triglyceride lipase has pleiotropic roles in mitochondrial function
metabolism
-
ATGL selectively performs the first step in triacylglyceride hydrolysis resulting in the formation of diacylglyceride and free fatty acid. ATGL is important in the lipolysis, the coordinated catabolism of triacylglycerol stored in cellular lipid droplets, providing fatty acids, di-, and monoglycerides, besides the hormone sensitive lipase, and the lipid droplet binding proteins, perilipin, adipophilin, and Tip47, detailed pathway overview
physiological function
-
adipose TG lipase, ATGL, is the predominant TG lipase in adipose tissue and an important regulator of triacyglycerol degradation in skeletal muscle
physiological function
-
ATGL participates in basal lipolysis in adipocytes, whereas the role of HSl is minor. In the basal state ATGL is a major regulator of triacylglyceride storage in adipocytes and its effects are independent of Peri A expression. HSL expression does not affect lipid droplet size regardless of Peri A expression
physiological function
-
hepatic lipase-mediated lipoprotein hydrolysis provides free fatty acids for energy, storage, and nutrient signaling and may play a role in energy homeostasis. The enzyme activity favors weight gain and obesity
physiological function
-
mobilization of fatty acids from all fat depots depends on the activity of TG hydrolases. The physiological function of ATGL/CGI-58 is not restricted to adipose tissue but is also crucially important in many nonadipose tissues, detailed overview. ATGL activity may be associated with improved insulin sensitivity in mice and humans
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). PLPL2_MOUSE
486
0
53657
Swiss-Prot
Secretory Pathway (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
secondary and three-dimensional structure analysis, overview
additional information
-
comparison of primary structures of the human and murine ATGL, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
posttranslational regulation by N-glycosylation at Asn79 and Asn489
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
knockdown of ATGL in 3T3-L1 cells by siRNA transfection, the cells show decreased lipolysis
additional information
-
knockdown of ATGL in 3T3-L1 cells by siRNA transfection, the cells show decreased lipolysis
additional information
-
a perilipin-regulation mutant shows increased enzyme activity in adipose tissue and increased lipolysis leading to lean mice
additional information
-
ATGL-/- mice are obese, exhibit impaired thermogenesis, oxidize more carbohydrate, and die prematurely due to cardiac dysfunction. ATGL-/- mice developed heart failure due to myocardial fibrosis and a mechanical contraction defect, thereby reducing their life span. HSL-/- mice show defective beta-adrenergic stimulated lipolysis, protection against high-fat diet-induced obesity, and possible impairments in insulin secretion. Phenotypes, overview
additional information
-
ATGL-deficiency decreases the release of fatty acids from white adipose tissue by about 70% in response to isoproterenol treatment, and this decreased lipolytic rate results in substantially reduced plasma fatty acid levels in ATGL-KO mice. Moreover, ATGL deficient mice are extremely cold-sensitive. Upon fasting, they reduce their oxygen consumption and drop their body temperature, phenotype, overview
additional information
-
genotyping and gene expression analysis of ATGL-/- and and HSL-/- mice, overview. Lipid metabolism up-regulation in ATGL-/- mice and down-regulation in HSL-/- mice
additional information
-
hepatic lipase deficiency reduces body fate stores and reduces adipose tissue macrophage content, fully prevents development of hepatic steatosis, and is consistent with reduced inflammation and a lean phenotype, overview
additional information
-
HSL knockout mice are not overweight or obese. To the contrary, with increased age, they have reduced white adipose tissue weight and are resistant to genetically or diet-induced obesity. HSL-deficient adipocytes respond to beta-adrenergic stimulation and, compared with control mice, exhibit only a moderate decrease in their capacity to release fatty acid. Importantly, HSL deficiency results in diacylglyceride accumulation in several tissues. Phenotypes of ATGL-deficient and HSL-deficient mice, overview
additional information
-
HSL-directed shRNAi does not significantly alter basal glycerol or fatty acid release when compared with control. ATGL-directed shRNAi significantly decreases both glycerol and fatty acid release in the absence of Peri A. Knockdown of ATGL dramatically increases triacyl glyceride storage compared with control both in the absence or presence of Peri A. In contrast, knockdown of HSL does not alter triacyl glyceride storage significantly regardless of Peri A expression
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of ATGL in 3T3-L1 cells via retroviral infection system, the cells show increased lipolysis
DNA and amino acid sequence determination and analysis, the genes encoding the enzyme are located on chromosome 8 within a cluster of carboxylesterase genes, genetic organization, expression analysis
-
expression of ATGL and HSL in Peri A-deficient and wild-type mouse embryonic fibroblasts
-
the Atgl gene Pnpla2 contains nine exons and spans a region of approximately 6 kb on chromosome 7F5
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ATGL mRNA concentrations are markedly affected by nutritional status, and increase during fasting and decrease during refeeding
-
low ATGL mRNA levels upon TNFalpha treatment. TNFalpha-mediated inhibition of PPARg reduces ATGL mRNA expression. TNFalpha suppresses the expression of a large number of adipose-specific genes, leading to an adipocyte dedifferentiation process
-
rosiglitazone concomitantly promotes differentiation of pre-adipocytes to functional adipocytes and induces mRNA levels of ATGL. Peroxisome proliferator-activated receptor-gamma, PPARgamma, antagonist bisphenol A diglycidyl ether significantly abrogates the induction of mRNA, but not protein levels of ATGL by rosiglitazone in differentiated 3T3-L1 adipocytes
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Van Bennekum, A.M.; Fisher, E.A.; Blaner, W.S.; Harrison, E.H.
Hydrolysis of retinyl esters by pancreatic triglyceride lipase
Biochemistry
39
4900-4906
2000
Mus musculus, Rattus norvegicus
Dolinsky, V.W.; Gilham, D.; Alam, M.; Vance, D.E.; Lehner, R.
Triacylglycerol hydrolase: role in intracellular lipid metabolism
Cell. Mol. Life Sci.
61
1633-1651
2004
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Kershaw, E.E.; Hamm, J.K.; Verhagen, L.A.; Peroni, O.; Katic, M.; Flier, J.S.
Adipose triglyceride lipase: function, regulation by insulin, and comparison with adiponutrin
Diabetes
55
148-157
2006
Mus musculus (Q8BJ56), Mus musculus
Goodman, K.B.; Bury, M.J.; Cheung, M.; Cichy-Knight, M.A.; Dowdell, S.E.; Dunn, A.K.; Lee, D.; Lieby, J.A.; Moore, M.L.; Scherzer, D.A.; Sha, D.; Suarez, D.P.; Murphy, D.J.; Harpel, M.R.; Manas, E.S.; McNulty, D.E.; Annan, R.S.; Matico, R.E.; Schwartz, B.K.; Trill, J.J.; Sweitzer, T.D.; Wang, D.Y.; Keller, P.M.; Krawie, K.r.a.w.i.e.c.
Discovery of potent, selective sulfonylfuran urea endothelial lipase inhibitors
Bioorg. Med. Chem. Lett.
19
27-30
2009
Mus musculus
Kobayashi, K.; Yamada, K.; Murata, T.; Hasegawa, T.; Takano, F.; Koga, K.; Fushiya, S.; Batkhuu, J.; Yoshizaki, F.
Constituents of Rhodiola rosea showing inhibitory effect on lipase activity in mouse plasma and alimentary canal
Planta Med.
74
1716-1719
2008
Mus musculus
Watt, M.J.
Triglyceride lipases alter fuel metabolism and mitochondrial gene expression
Appl. Physiol. Nutr. Metab.
34
340-347
2009
Homo sapiens, Mus musculus
Zimmermann, R.; Lass, A.; Haemmerle, G.; Zechner, R.
Fate of fat: the role of adipose triglyceride lipase in lipolysis
Biochim. Biophys. Acta
1791
494-500
2009
Homo sapiens, Mus musculus
Liu, L.F.; Purushotham, A.; Wendel, A.A.; Koba, K.; DeIuliis, J.; Lee, K.; Belury, M.A.
Regulation of adipose triglyceride lipase by rosiglitazone
Diabetes Obes. Metab.
11
131-142
2009
Mus musculus
Chiu, H.K.; Qian, K.; Ogimoto, K.; Morton, G.J.; Wisse, B.E.; Agrawal, N.; McDonald, T.O.; Schwartz, M.W.; Dichek, H.L.
Mice lacking hepatic lipase are lean and protected against diet-induced obesity and hepatic steatosis
Endocrinology
151
993-1001
2010
Mus musculus
Pinent, M.; Hackl, H.; Burkard, T.R.; Prokesch, A.; Papak, C.; Scheideler, M.; Haemmerle, G.; Zechner, R.; Trajanoski, Z.; Strauss, J.G.
Differential transcriptional modulation of biological processes in adipocyte triglyceride lipase and hormone-sensitive lipase-deficient mice
Genomics
92
26-32
2008
Mus musculus
Miyoshi, H.; Perfield, J.W.; Obin, M.S.; Greenberg, A.S.
Adipose triglyceride lipase regulates basal lipolysis and lipid droplet size in adipocytes
J. Cell. Biochem.
105
1430-1436
2008
Mus musculus
Zechner, R.; Kienesberger, P.C.; Haemmerle, G.; Zimmermann, R.; Lass, A.
Adipose triglyceride lipase and the lipolytic catabolism of cellular fat stores
J. Lipid Res.
50
3-21
2009
Homo sapiens, Mus musculus
Kratky, D.; Obrowsky, S.; Kolb, D.; Radovic, B.
Pleiotropic regulation of mitochondrial function by adipose triglyceride lipase-mediated lipolysis
Biochimie
96
106-112
2014
Mus musculus
Radovic, B.; Aflaki, E.; Kratky, D.
Adipose triglyceride lipase in immune response, inflammation, and atherosclerosis
Biol. Chem.
393
1005-1011
2012
Mus musculus
Eichmann, T.O.; Kumari, M.; Haas, J.T.; Farese, R.V.; Zimmermann, R.; Lass, A.; Zechner, R.
Studies on the substrate and stereo/regioselectivity of adipose triglyceride lipase, hormone-sensitive lipase, and diacylglycerol-O-acyltransferases
J. Biol. Chem.
287
41446-41457
2012
Mus musculus
EXTERNAL LINKS (specific for EC-Number 3.1.1.3)
Transporter Classification Database (TCDB): 8.A.178.1.1, 1.A.115.1.1
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