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Information on EC 3.1.1.34 - lipoprotein lipase and Organism(s) Mus musculus and UniProt Accession P11152
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3.1.1.34 lipoprotein lipaseIUBMB Comments
Hydrolyses triacylglycerols and diacylglycerol in chylomicrons and low-density lipoprotein particles. Human protein purified from post-heparin plasma (LPL) shows no activity against triglyceride in the absence of added lipoprotein. The principal reaction sequence of that enzyme is triglyceride -> 1,2-diglyceride -> 2-monoglyceride. The hepatic enzyme (LIPC) also hydrolyses triglycerides and phospholipids present in circulating plasma lipoproteins.
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Word Map
- 3.1.1.34
- triglyceride
- cholesterol
-
apolipoproteins
- hdl
- adipocytes
- hypertriglyceridemia
-
lipolysis
-
high-density
-
low-density
- peroxisome
- obesity
- atherosclerosis
- triacylglycerols
- chylomicron
- cardiovascular
-
proliferator-activated
-
post-heparin
- coronary
- milk
-
triglyceride-rich
-
obese
-
remnant
-
postprandial
-
atherogenic
-
high-fat
- hyperlipidemia
- dyslipidemia
-
ppars
- lipases
-
very-low-density
- hyperlipoproteinemia
- preadipocytes
-
lipogenesis
-
depot
-
angiopoietin-like
- epididymal
- leptin
-
normolipidemic
-
adipogenic
-
hormone-sensitive
-
hdl-cholesterol
-
heparin-sepharose
- nefas
-
lecithin:cholesterol
- triolein
- medicine
- intralipid
- synthesis
-
perirenal
- pvuii
-
lipoprotein-cholesterol
- emulsions
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
lipoprotein lipase, adipose tissue lpl, dag lipase, diglyceride lipase, clearing factor, postheparin lipase, postheparin esterase, placental lipoprotein lipase, diacylglycerol hydrolase, triacylglycero-protein acylhydrolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
clearing factor
-
-
-
-
diacylglycerol hydrolase
-
-
-
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diacylglycerol lipase
-
-
-
-
diglyceride lipase
-
-
-
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lipemia-clearing factor
-
-
-
-
LPL
postheparin esterase
-
-
-
-
postheparin lipase
-
-
-
-
LPL
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
triacylglycero-protein acylhydrolase
Hydrolyses triacylglycerols and diacylglycerol in chylomicrons and low-density lipoprotein particles. Human protein purified from post-heparin plasma (LPL) shows no activity against triglyceride in the absence of added lipoprotein. The principal reaction sequence of that enzyme is triglyceride -> 1,2-diglyceride -> 2-monoglyceride. The hepatic enzyme (LIPC) also hydrolyses triglycerides and phospholipids present in circulating plasma lipoproteins.
CAS REGISTRY NUMBER
COMMENTARY
9004-02-8
-
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
1,2-O-dilauryl-DL-glycero-3-glutaric acid-(6-methylresorufin ester) + H2O
?
-
-
-
-
?
EnzChek lipase substrate + H2O
?
-
a commercially available BODIPY, Dabcyl-labeled triglyceride analog substrate, C58H85BF2N6O6
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-
?
additional information
?
-
lipoprotein lipase plays a central role in the removal of plasma triglyceride
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-
?
additional information
?
-
enzymatic activity of cell-surface heparin-released LPL is measured using a phospholipid (PL)/3H-triolein substrate with human serum as a source of ApoC2
-
-
?
additional information
?
-
-
the enzyme is rate limiting for the supply of muscle tissue with triglyceride-derived free fatty acids. Improper regulation of the muscle enzyme can lead to major pathogenesis of some human myopathies
-
-
?
additional information
?
-
-
lipoprotein lipase activity is required for normal cardiac metabolic compensation to hypertensive stress
-
-
?
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
additional information
?
-
lipoprotein lipase plays a central role in the removal of plasma triglyceride
-
-
?
additional information
?
-
-
the enzyme is rate limiting for the supply of muscle tissue with triglyceride-derived free fatty acids. Improper regulation of the muscle enzyme can lead to major pathogenesis of some human myopathies
-
-
?
additional information
?
-
-
lipoprotein lipase activity is required for normal cardiac metabolic compensation to hypertensive stress
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
angiopoietin-like protein 3
-
i.e. Angptl3, human, commercial preparation of recombinant enzyme, inhibits LPL activity in vitro and in vivo, structural basis for inhibition, overview. The highly conserved motif LAXGLLXLGXGL, where X represents polar amino acid residues, corresponding to amino acid residues 46-57 within the NH2-terminal coiled-coil domain, confers its inhibitory effects on lipoprotein lipase
-
angiopoietin-like protein 4
-
i.e. Angptl4, human, recombinantly expressed in Escherichia coli. It inhibits LPL activity in vitro and in vivo. The highly conserved motif LAXGLLXLGXGL, where X represents polar amino acid residues, corresponding to amino acid residues 44-55 within the NH2-terminal coiled-coil domain, confers its inhibitory effects on lipoprotein lipase, involving amino acid residues His46, Gln50, and Gln53, by disrupting the enzyme dimerization, overview. Structural basis for inhibition, overview. Mutants H46A, Q50A, and Q53A are not active against the enzyme
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heat-inactivated rat serum
-
heat-inactivated rat serum added from 0-10%, decreases the enzyme activity by 12%. HIS also contains lipoprotein lipase-inhibitory factors such as angiopoietin-like protein-3, angiopoietin-like protein-4, apoC-I, and apoC-III
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NaCl
-
1 M NaCl inhibits the reaction with triolein by 80%, but there is no inhibition of lipoprotein lipase activity by NaCl if apoC-II is not used in the assay
additional information
-
protein kinase Calpha depletion inhibits LPL translation through protein kinase A activation, LPL translational inhibition occurs through an RNA-binding complex involving protein kinase A subunits and A-kinase-anchoring protein 121, LPL is also translationally repressed following depletion of cellular protein kinase C either through prolonged treatment with phorbol esters or through the use of antisense oligonucleotides to protein kinase Calpha
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
angiopoietin-like protein 4
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major physiological regulator of enzyme activity under conditions of fasting and exercise
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apoC-II
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apoC-II activates the enzyme 3.5fold in a saturable fashion. Heat-inactivated rat serum is often used as a source of apoC-II for activation of lipoprotein lipase
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glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1
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binds lipoprotein lipase and chylomicrons and is a platform for lipolysis within capillaries
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NaCl
-
addition of NaCl increases the reaction rate with EnzChek lipase substrate dramatically with the highest rate, 46% higher than that without salt, occurring at 0.15 M
additional information
-
glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 represents an important binding site for LPL in vivo
-
additional information
-
oral administration of 120 mg/kg/d body weight of polysaccharides from Auricularia auricula significantly decreases LPL activity in cholesterol-enriched diet-fed mice (the neutral sugars are mainly composed of D-rhamnose, D-xylose, D-glucose and smaller amounts of D-mannose, D-galactose, and D-arabinose)
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
scopoletin significantly increases lipoprotein lipase activity in 3T3-L1 adipocytes
-
transgenic animals with beta-cell-specific overexpression or inactivation of enzyme. Enzyme activity and triglyceride content is increased in overexpressing islets, decreased enzyme activity enzyme-inactivated islets does not affect islets triglyceride content. Both overexpressing and enzyme-inactivited mice are strikingly hyperglycemic during glucose tolerance testing, and both show impaired glucose-simulated insulin secretion
additional information
-
LPL is expressed in a wide variety of cell types, particularly in adipocytes and myocytes
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significantly reduced LPL activity in parametrial adipose tissue from mice fed with conjugated linoleic acid
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range of enzyme activity differs up to 4fold among mink, mice, chinese hamster, rat and guinea pig
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heparin releases LPL from its in vivo binding sites allowing it to enter the blood plasma
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range of enzyme activity differs up to 6fold among mink, mice, chinese hamster, rat and guinea pig
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activity decreases by 50% on food deprivation for 6 h without corresponding changes in enzyme mRNA or mass. Range of enzyme activity differs up to 500fold among mink, mice, chinese hamster, rat and guinea pig. Mink shows the highest kidney enzyme activity, guinea pig the lowest.
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LPL activity increases in homone-sensitive lipase ko-mice
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
lipoprotein lipase (LPL)-deficient cells show dramatically reduced expression of anti-inflammatory markers, YM1, and arginase 1 and increased expression of pro-inflammatory markers, such as iNOS compared to wild-type cells. LPL is increased during the onset of remyelination, which is associated with an anti-inflammatory reparative microglial phenotype, and may facilitate the uptake of myelin-derived lipids in the CNS
physiological function
malfunction
metabolism
physiological function
physiological function
lipasin/Angptl8 monoclonal antibody lowers mouse serum triglycerides involving increased postprandial activity of the cardiac lipoprotein lipase. Lipasin/Angptl8 is a feeding-induced hepatokine that regulates triglyceride (TAG) metabolism. Lipasin-deficient mice exhibit elevated postprandial activity of LPL in the heart and skeletal muscle, but not in white adipose tissue, suggesting that lipasin suppresses the activity of LPL specifically in cardiac and skeletal muscles. During fasting, LPL activity is upregulated in the heart and skeletal muscle, which, in turn, take up fatty acids for energy production. In the fed state, LPL activity is upregulated in white adipose tissue, which, in turn, takes up fatty acids for storage
physiological function
lipoprotein lipase is a feature of alternatively-activated microglia, reparative microglia cells, and may facilitate lipid uptake in the CNS during demyelination. Lipoprotein lipase is involved in microglial lipid uptake. LPL may support repair through the clearance of myelin-derived lipids. Lipoprotein lipase (LPL) is the rate-limiting enzyme in the hydrolysis of triglyceride-rich lipoproteins and is increased in Schwann cells and macrophages following nerve crush injury in the peripheral nervous system (PNS), suggesting that LPL may help scavenge myelin-derived lipids. Role of LPL in microglia, overview
malfunction
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lipoprotein lipase knock-out mice die 18 h after birth, probably because of hypoglycemia
malfunction
-
selective loss of adipocyte enzyme in mice leads to mild hypertriglyceridemia. Enzyme-deficient mice display a profound increase in de novo lipogenesis-fatty acids, especially palmitoleate and myristoleate in brown adipose tissue and white adipose tissue depots while essential dietary fatty acids are markedly decreased. High fat diet-fed enzyme-deficient mice exhibit less adiposity and improved plasma adipokines but not increased glucose tolerance
metabolism
-
the phosphoinositide-3-kinase pathway is involved in the regulation of LPL gene transcription through Sp1/Sp3, signalling pathways that impact on the IFN-mediated regulation of Sp1/Sp3 binding and LPL gene transcription in macrophages, overview. The synergism between IFN- and TNF- on LPL gene transcription is not mediated at the level of Sp1/Sp3 DNA binding
metabolism
-
lipoprotein lipase is a major enzyme in lipid metabolism responsible for the hydrolysis of the core triglycerides in chylomicrons and very low density lipoprotein and subsequent release of free fatty acids
physiological function
-
lipoprotein lipase is a principal enzyme responsible for the clearance of chylomicrons and very low density lipoproteins from the bloodstream. The activity of LPL is tightly modulated by multiple mechanisms in a tissue-specific manner in response to nutritional changes
physiological function
-
lipoprotein lipase LPL expressed in placenta facilitates uptake of retinoids by this organ and their transfer to the embryo, mainly through its catalytic activity. In addition, LPL can mediate the acquisition of nascent chylomicrons by the placenta, although less efficiently. Placental LPL acts in concert with low density lipoprotein receptor and LRP1
physiological function
-
the enzyme is rate limiting for plasma triglyceride clearance and tissue uptake of 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). LIPL_MOUSE
474
0
53109
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
transgenic animals with beta-cell-specific overexpression or inactivation of enzyme. Enzyme activity and triglyceride content is increased in overexpressing islets, decreased enzyme activity enzyme-inactivated islets does not affect islets triglyceride content. Both overexpressing and enzyme-inactivited mice are strikingly hyperglycemic during glucose tolerance testing, and both show impaired glucose-simulated insulin secretion
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
lipasin suppresses the activity of LPL specifically in cardiac and skeletal muscles
insulin, dexamethasone and cortisol increase mRNA and activity in adipose organs. Cold markedly stimulates enzyme activity in brown adipose tissue
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interferon mediates inhibition of lipoprotein lipase gene transcription in macrophages, the mechanism involves a reduction in the binding of transcription factors Sp1 and Sp3 to regulatory sequences in the LPL gene with casein kinase 2- and phosphoinositide-3-kinase-mediated regulation of transcription factors Sp1 and Sp3, overview
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skeletal muscle lipoprotein lipase activity is increased in leptin-treated (2 mg/kg body weight over 2 weeks) compared with pair-fed and wild type mice
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stress and catecholamines reduce adipose enzyme activity. Tissue necrosis factpor alpha represses enzyme activity by downregulating transcription
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there is no effect of leptin treatment (2 mg/kg body weight over 2 weeks) or pair feeding on postprandial adipose tissue lipoprotein lipase activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
retinoid X receptor gamma-deficient mice, increase in activity of skeletal muscle enzyme isoform, but no increase in enzyme activity in adipose and cardiac tissue. Resistance of animals to gain in fat mass in response to high-fat feeding through up-regulation of enzyme activity in skeletal muscle
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kirchgessner, T.G.; Svenson, K.L.; Lusis, A.J.; Schotz, M.C.
The sequence of cDNA encoding lipoprotein lipase. A member of a lipase gene family
J. Biol. Chem.
262
8463-8466
1987
Mus musculus
Frank, S.L.; Radner, H.; Walsh, A.; Stollberger, R.; Knipping, G.; Hoefler, G.; Sattler, W.; Weinstock, P.H.; Breslow, J.L.; Zecher, R.
Muscle-specific overexpression of lipoprotein lipase causes a severe myopathy characterized by proliferation of mitochondria and peroxisomes in transgenic mice
J. Clin. Invest.
96
976-986
1995
Mus musculus
Wang, C.S.; Hartsuck, J.; McConathy, J.
Structure and functional properties of lipoprotein lipase
Biochim. Biophys. Acta
1123
1-17
1992
Bos taurus, Cavia porcellus, Gallus gallus, Homo sapiens, Mus musculus
Haemmerle, G.; Zimmermann, R.; Strauss, J.G.; Kratky, D.; Riederer, M.; Knipping, G.; Zechner, R.
Hormone-sensitive lipase deficiency in mice changes the plasma lipid profile by affecting the tissue-specific expression pattern of lipoprotein lipase in adipose tissue and muscle
J. Biol. Chem.
277
12946-12952
2002
Mus musculus
Xu, X.; Storkson, J.; Kim, S.; Sugimoto, K.; Park, Y.; Pariza, M.W.
Short-term intake of conjugated linoleic acid inhibits lipoprotein lipase and glucose metabolism but does not enhance lipolysis in mouse adipose tissue
J. Nutr.
133
663-667
2003
Mus musculus
Haugen, B.R.; Jensen, D.R.; Sharma, V.; Pulawa, L.K.; Hays, W.R.; Krezel, W.; Chambon, P.; Eckel, R.H.
Retinoid X receptor gamma-deficient mice have increased skeletal muscle lipoprotein lipase activity and less weight gain when fed a high-fat diet
Endocrinology
145
3679-3685
2004
Mus musculus
Ruge, T.; Sukonina, V.; Myrnas, T.; Lundgren, M.; Eriksson, J.W.; Olivecrona, G.
Lipoprotein lipase activity/mass ratio is higher in omental than in subcutaneous adipose tissue
Eur. J. Clin. Invest.
36
16-21
2006
Cavia porcellus, Cricetulus griseus, Mus musculus, Rattus norvegicus, Mustela lutreola
Pappan, K.L.; Pan, Z.; Kwon, G.; Marshall, C.A.; Coleman, T.; Goldberg, I.J.; McDaniel, M.L.; Semenkovich, C.F.
Pancreatic beta-cell lipoprotein lipase independently regulates islet glucose metabolism and normal insulin secretion
J. Biol. Chem.
280
9023-9029
2005
Mus musculus
Yang, J.Y.; Koo, J.H.; Yoon, H.Y.; Lee, J.H.; Park, B.H.; Kim, J.S.; Chi, M.S.; Park, J.W.
Effect of scopoletin on lipoprotein lipase activity in 3T3-L1 adipocytes
Int. J. Mol. Med.
20
527-531
2007
Mus musculus (P11152)
Dallinga-Thie, G.M.; Zonneveld-de Boer, A.J.; van Vark-van der Zee, L.C.; van Haperen, R.; van Gent, T.; Jansen, H.; De Crom, R.; van Tol, A.
Appraisal of hepatic lipase and lipoprotein lipase activities in mice
J. Lipid Res.
48
2788-2791
2007
Mus musculus
Yamashita, H.; Bharadwaj, K.G.; Ikeda, S.; Park, T.S.; Goldberg, I.J.
Cardiac metabolic compensation to hypertension requires lipoprotein lipase
Am. J. Physiol. Endocrinol. Metab.
295
E705-E713
2008
Mus musculus
Unal, R.; Pokrovskaya, I.; Tripathi, P.; Monia, B.P.; Kern, P.A.; Ranganathan, G.
Translational regulation of lipoprotein lipase in adipocytes: depletion of cellular protein kinase Calpha activates binding of the C subunit of protein kinase A to the 3-untranslated region of the lipoprotein lipase mRNA
Biochem. J.
413
315-322
2008
Mus musculus
Weinstein, M.M.; Yin, L.; Beigneux, A.P.; Davies, B.S.; Gin, P.; Estrada, K.; Melford, K.; Bishop, J.R.; Esko, J.D.; Dallinga-Thie, G.M.; Fong, L.G.; Bensadoun, A.; Young, S.G.
Abnormal patterns of lipoprotein lipase release into the plasma in GPIHBP1-deficient mice
J. Biol. Chem.
283
34511-34518
2008
Mus musculus
Chen, G.; Luo, Y.; Ji, B.; Li, B.; Guo, Y.; Li, Y.; Su, W.; Xiao, Z.
Effect of polysaccharide from Auricularia auricula on blood lipid metabolism and lipoprotein lipase activity of ICR mice fed a cholesterol-enriched diet
J. Food Sci.
73
H103-H108
2008
Mus musculus, Mus musculus ICR
Davies, B.S.; Waki, H.; Beigneux, A.P.; Farber, E.; Weinstein, M.M.; Wilpitz, D.C.; Tai, L.J.; Evans, R.M.; Fong, L.G.; Tontonoz, P.; Young, S.G.
The expression of GPIHBP1, an endothelial cell binding site for lipoprotein lipase and chylomicrons, is induced by peroxisome proliferator-activated receptor-gamma
Mol. Endocrinol.
22
2496-2504
2008
Mus musculus
Harris, S.M.; Harvey, E.J.; Hughes, T.R.; Ramji, D.P.
The interferon- -mediated inhibition of lipoprotein lipase gene transcription in macrophages involves casein kinase 2- and phosphoinositide-3-kinase-mediated regulation of transcription factors Sp1 and Sp3
Cell. Signal.
20
2296-2301
2008
Homo sapiens, Mus musculus
Yau, M.H.; Wang, Y.; Lam, K.S.; Zhang, J.; Wu, D.; Xu, A.
A highly conserved motif within the NH2-terminal coiled-coil domain of angiopoietin-like protein 4 confers its inhibitory effects on lipoprotein lipase by disrupting the enzyme dimerization
J. Biol. Chem.
284
11942-11952
2009
Bos taurus, Mus musculus, Mus musculus C57/BL6J
Wassef, L.; Quadro, L.
Uptake of dietary retinoids at the maternal-fetal barrier: in vivo evidence for the role of lipoprotein lipase and alternative pathways
J. Biol. Chem.
286
32198-32207
2011
Mus musculus
Basu, D.; Manjur, J.; Jin, W.
Determination of lipoprotein lipase activity using a novel fluorescent lipase assay
J. Lipid Res.
52
826-832
2011
Bos taurus, Mus musculus
Donahoo, W.T.; Stob, N.R.; Ammon, S.; Levin, N.; Eckel, R.H.
Leptin increases skeletal muscle lipoprotein lipase and postprandial lipid metabolism in mice
Metab. Clin. Exp.
60
438-443
2011
Mus musculus
Bartelt, A.; Weigelt, C.; Cherradi, M.L.; Niemeier, A.; Toedter, K.; Heeren, J.; Scheja, L.
Effects of adipocyte lipoprotein lipase on de novo lipogenesis and white adipose tissue browning
Biochim. Biophys. Acta
1831
934-942
2013
Mus musculus
Kersten, S.
Physiological regulation of lipoprotein lipase
Biochim. Biophys. Acta
1841
919-933
2014
Mus musculus
Bruce, K.D.; Gorkhali, S.; Given, K.; Coates, A.M.; Boyle, K.E.; Macklin, W.B.; Eckel, R.H.
Lipoprotein lipase is a feature of alternatively-activated microglia and may facilitate lipid uptake in the CNS during demyelination
Front. Mol. Neurosci.
11
57
2018
Homo sapiens (P06858), Homo sapiens, Mus musculus (P11152), Mus musculus C57BL/6J (P11152)
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