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Information on EC 3.1.1.34 - lipoprotein lipase
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3.1.1.34 lipoprotein lipaseIUBMB Comments
Hydrolyses triacylglycerols in chylomicrons and low-density lipoproteins. Also hydrolyses diacylglycerol.
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Word Map
- 3.1.1.34
- triglyceride
- cholesterol
- insulin
-
apolipoproteins
- hdl
- adipocytes
-
lipolysis
- diabetes
- hypertriglyceridemia
- obesity
- triacylglycerols
-
low-density
- peroxisome
- chylomicron
- atherosclerosis
-
high-density
-
proliferator-activated
-
obese
-
post-heparin
- milk
- coronary
- artery
- cardiovascular
-
triglyceride-rich
-
remnant
-
ppars
-
postprandial
- hyperlipidemia
- lipases
-
atherogenic
-
high-fat
- hyperlipoproteinemia
-
very-low-density
-
normolipidemic
-
hdl-cholesterol
-
hormone-sensitive
- dyslipidemia
- preadipocytes
-
lipogenesis
-
adipogenic
- epididymal
- leptin
-
depot
-
perirenal
- nefas
- emulsions
- medicine
- triolein
-
heparin-sepharose
- synthesis
-
lecithin:cholesterol
-
lipoprotein-cholesterol
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
adipose tissue LPL, BSLPL, Burkholderia species lipoprotein lipase, clearing factor, DAG lipase, DAGL, diacylglycerol hydrolase, diacylglycerol lipase, diglyceride lipase, heparin-releasable protein lipase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
clearing factor
-
-
-
-
diacylglycerol hydrolase
-
-
-
-
diacylglycerol lipase
diglyceride lipase
-
-
-
-
lipemia-clearing factor
-
-
-
-
LPL
postheparin esterase
-
-
-
-
postheparin lipase
-
-
-
-
diacylglycerol lipase
-
-
-
-
LPL
-
-
-
-
LPL
-
-
LPL
-
-
LPL
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
triacylglycerol + H2O = diacylglycerol + a carboxylate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
triacylglycero-protein acylhydrolase
Hydrolyses triacylglycerols in chylomicrons and low-density lipoproteins. Also hydrolyses diacylglycerol.
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CAS REGISTRY NUMBER
COMMENTARY
9004-02-8
-
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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-di-O-lauryl-rac-glycero-3-(glutaric acid 6-methylresorufin ester) + H2O
?
-
DGGR, a synthetic substrate that produces a fluorescent signal upon hydrolysis
-
-
?
1,2-O-dilauryl-rac-glycero-3-glutaric acid-(6'-methylresorufin) ester + H2O
?
-
-
-
-
?
1-myristol-2[9(1-pyrenyl)-nonanoyl]-phosphatidylcholine + H2O
myristic acid + 2[9(1-pyrenyl)-nonanoyl]-phosphatidylcholine
-
-
-
?
L-alpha-dimyristoylphosphatidylcholine + H2O
?
-
necessity of a lipid bilayer structure
-
-
?
triolein + H2O
dioleylglycerol + oleate
-
mutant D204 E, very low activity in presence of emulsifier Triton X-100 or phosphatidylcholine. In presence of phosphatidylethenolamine, phospatidylserine, and cardiolipin as emulsifier, triolein-hydrolizing activity of the mutant is higher than wild-type activity
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-
?
1,2-O-dilauryl-DL-glycero-3-glutaric acid-(6-methylresorufin ester) + H2O
?
-
-
-
-
?
1,2-O-dilauryl-DL-glycero-3-glutaric acid-(6-methylresorufin ester) + H2O
?
-
-
-
-
?
EnzChek lipase substrate + H2O
?
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a commercially available BODIPY, Dabcyl-labeled triglyceride analog substrate, C58H85BF2N6O6
-
-
?
EnzChek lipase substrate + H2O
?
-
a commercially available BODIPY, Dabcyl-labeled triglyceride analog substrate, C58H85BF2N6O6
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
catalyzes the hydrolysis of triglycerides in circulating chylomicrons and very-low density lipoproteins
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-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
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lipoproteins with high triglyceride
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-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
a 14C-triolein phosphatidylcholine-stabilized substrate containing ApoC2 is used for in vitro enzyme activity assays
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
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from chylomicrons, lipoproteins isolated from human blood
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
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the lipase substrate used is plasma or VLDL with or without added ligands, enzyme source is postheparin plasma, lipoproteins with high triglyceride
-
-
?
triolein + H2O
oleate + diolein
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-
-
-
?
triolein + H2O
oleate + diolein
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10 mM of triolein with 5% (w/v) bovine serum albumin, 1% (w/v) Gum arabic, and acetonitrile show the optimum conditions for measuring LPL activity
-
-
?
additional information
?
-
-
lipoprotein lipase hydrolyses the triacylglycerols secreted by the liver and, thus, allows the storage of lipids onto the extrahepatic tissue. Lipoprotein lipase appears to be an important factor for a large or moderate overfeeding induced liver steatosis in different genotypes of ducks
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-
-
additional information
?
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-
the commercially cheaply available lipase lipoprotein (LPL) from Aspergillus niger efficiently catalyzes the Knoevenagel condensation of aromatic aldehydes with various active methylene compounds in good to excellent yields with Z configuration exclusively. Enzyme-catalyzed Knoevenagel condensation of 4-nitrobenzaldehyde and acetylacetone, optimization of reaction conditions for improved catalytic activity, method overview
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additional information
?
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plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
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-
-
additional information
?
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plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
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lipoprotein lipase mediates hepatitis C virus cell entry and inhibits HCV infection
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-
-
additional information
?
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glucose-headed surfactant (GHS)-treated lipoprotein lipase are determined for the hydrolysis or alcoholysis of p-nitrophenyl acetate
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-
-
additional information
?
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lipoprotein lipase (LPL) from Burkholderia species is also highly active in organic solvent if it is coated with both dextrin (D) and ionic surfactant (i) via lyophilization. Successful application of this LPL preparation (LPL-D1) to the dynamic kinetic resolution (DKR) of diarylmethanols including aryl heteroarylmethanols. Enzyme assay performing hydrolysis and alcoholysis of 4-nitrophenyl acetate. The enantioselectivity of LPL-D1 increases with increasing difference in size between two aryl groups at the hydroxymethine center of substrate. The enantioselectivity is low for monohalogenated phenyl acetate but increases significantly in the case that the halogen is substituted by a bulkier substituent such as isopropyl, tert-butyl or trimethylsilyl
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-
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additional information
?
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lipoprotein lipase hydrolyses the triacylglycerols secreted by the liver and, thus, allows the storage of lipids onto the extrahepatic tissue. Lipoprotein lipase appears to be an important factor for a large or moderate overfeeding induced liver steatosis in different genotypes of ducks
-
-
-
additional information
?
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inverse relationship between the hydrolytic rate and the increased acyl-chain unsaturation of monoacid triacylglycerols: C18:1, C18:2, C18:3
-
-
-
additional information
?
-
-
hydrolytic rate of C12 triacylglycerols is higher than C14 triacylglycerols and C16 triacylglycerol
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-
-
additional information
?
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the obligatory step in the transport of triglyceride fatty acids from circulating chylomicrons and very low density lipoproteins into tissues is hydrolysis of triglyceride core in the lipoprotein particles by lipoprotein lipase
-
-
-
additional information
?
-
-
plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
-
-
plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
-
-
lipoprotein lipase mediates hepatitis C virus cell entry and inhibits HCV infection
-
-
-
additional information
?
-
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the enzyme shows no activity toward cholesterol and high-density lipoprotein
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-
-
additional information
?
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tic activity of cell-surface heparin-released LPL is measured using a phospholipid (PL)/3H-triolein substrate with human serum as a source of ApoC2
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-
additional information
?
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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 plays a central role in the removal of plasma triglyceride
-
-
-
additional information
?
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lipoprotein lipase activity is required for normal cardiac metabolic compensation to hypertensive stress
-
-
-
additional information
?
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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
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additional information
?
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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
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-
-
additional information
?
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inverse relationship between the hydrolytic rate and the increased acyl-chain unsaturation of monoacid triacylglycerols: C18:1, C18:2, C18:3
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-
-
additional information
?
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hydrolysis of saturated monoacid triacylglycerol increases with increase of chain length as C16, C14, C12
-
-
-
additional information
?
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no absolute specificity for monolayers of triglycerides, hydrolysis of diglyceride monolayers at comparable rates
-
-
-
additional information
?
-
-
the enzyme is responsible for the harvesting of fatty acids from the triacylglycerols of circulating serum lipoproteins in those tissues that utilize these triacylglycerols
-
-
-
additional information
?
-
-
plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
-
-
plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
-
-
the obligatory step in the transport of triglyceride fatty acids from circulating chylomicrons and very low density lipoproteins into tissues is hydrolysis of triglyceride core in the lipoprotein particles by lipoprotein lipase
-
-
-
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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
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
lipoproteins with high triglyceride
-
-
?
additional information
?
-
-
plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
-
-
plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
-
P11151
lipoprotein lipase mediates hepatitis C virus cell entry and inhibits HCV infection
-
-
-
additional information
?
-
-
the obligatory step in the transport of triglyceride fatty acids from circulating chylomicrons and very low density lipoproteins into tissues is hydrolysis of triglyceride core in the lipoprotein particles by lipoprotein lipase
-
-
-
additional information
?
-
-
plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
-
-
plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
-
-
lipoprotein lipase mediates hepatitis C virus cell entry and inhibits HCV infection
-
-
-
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
?
-
P11152
lipoprotein lipase plays a central role in the removal of plasma triglyceride
-
-
-
additional information
?
-
-
lipoprotein lipase activity is required for normal cardiac metabolic compensation to hypertensive stress
-
-
-
additional information
?
-
-
the enzyme is responsible for the harvesting of fatty acids from the triacylglycerols of circulating serum lipoproteins in those tissues that utilize these triacylglycerols
-
-
-
additional information
?
-
-
plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
-
-
plays a key role in the metabolism of the triglyceride-rich lipoproteins, namely chylomicrons and very-low-density lipoproteins
-
-
-
additional information
?
-
-
the obligatory step in the transport of triglyceride fatty acids from circulating chylomicrons and very low density lipoproteins into tissues is hydrolysis of triglyceride core in the lipoprotein particles by lipoprotein lipase
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
0.01-0.015 mM, almost complete inhibition of tributyrin and tripropionin hydrolysis, competes for binding with apoprotein CII, inhibition is prevented or restored by apoprotein CII
3-[4'-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)biphenyl-3-yl]propanoic acid
-
-
4-tert-butyl-N-[4-(5-methoxy-2-oxo-1,3,4-oxadiazol-3(2H)-yl)phenyl]benzamide
-
-
Apo AI
-
0.001 mM, 25% inhibitiion of 1-myristol-2[9(1-pyrenyl)-nonanoyl]-phosphatidylcholine hydrolysis
-
Apo AII
-
0.001 mM, 50% inhibitiion of 1-myristol-2[9(1-pyrenyl)-nonanoyl]-phosphatidylcholine hydrolysis
-
Apo CI
-
0.0005 mM, 72% inhibitiion of 1-myristol-2[9(1-pyrenyl)-nonanoyl]-phosphatidylcholine hydrolysis
-
cytochalasin D
-
preincubation with cytochalasin D prevents the increase in dexmethasone-induced lipoprotein lipase activity
dodecanesulfonyl fluoride
-
0.01 mM-0.02 mM, 50% inhibition, complete inhibition after 24 h
ethanol
-
inhibits the enzyme, LPL activity is reduced by 23-25% 2-4 hours after the administration of alcohol, respectively, with respect to controls, in vivo or in post-heparin plasma. The concentrations of inhibitors ANGPTL3 and ANGPTL4 drops to 67% and 86% of baseline values, respectively, at 280 min after alcohol consumption. The acute effects of alcohol consumption, especially on postprandial lipemia, seem to be accentuated in hypertriglyceridemic subjects
hexadecanesulfonyl fluoride
-
0.01 mM-0.02 mM, 50% inhibition, complete inhibition after 24 h
LG268
-
retinoid X receptor selective retinoid, almost complete inactivation of LPL activity in heart muscle after administration of 30 mg/kg/d, approx. 50% inhibition in skeletal muscle
N-[3-aminopropyl-[4-(3-aminopropylamino)butyl]amino]-N-hydroxynitrous amide
-
i.e. spermine NONOate, tissue LPL activity tends to decrease 5 min after the addition of 0.1 mM spermine NONOate
RHC-80267
-
i.e. 1,6-di(O-(carbamoyl)cyclohexanone oxime)hexane, is a highly selective DAGL inhibitor. It significantly reduces L- and N-current inhibition by the muscarinic agonist oxotremorine-M, Oxo-M, but does not affect their inhibition by exogenous arachidonic acid, currents by Ba2+ or Ca2+. Moreover, voltage-dependent inhibition of N-current by Oxo-M remains in the presence of RHC-80267, indicating selective action on the slow pathway, i.e. the voltage-independent, pertussis-toxin insensitive pathway. RHC-80267 also blocks inhibition of recombinant N-current, but has no effect on native M-current inhibition
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 3
-
mainly exhibits reversible inhibition of the catalytic activity of LPL, heparin is able to overcome the inhibitory effect of angiopoietin-like protein 3 on LPL at a concentration as low as 0.8 units/ml
-
angiopoietin-like protein 3
-
ANGPTL3 causes reduction of the activity of LPL via a two-step mechanism
-
angiopoietin-like protein 3
-
ANGPTL3 inhibits the enzyme. The concentrations of inhibitor ANGPTL3 drops to 67% of baseline value at 280 min after alcohol consumption
-
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
-
angiopoietin-like protein 4
-
heparin is not able to overcome the inhibitory effect of angiopoietin-like protein 4 on LPL at concentrations up to 10 units/ml
-
angiopoietin-like protein 4
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ANGPTL4, ANGPTL4 inhibits LPL by a noncompetitive mechanism, unaltered in the presence or absence of glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1), inhibits wild-type and mutant LPLS447X enzymes to the same extent
-
angiopoietin-like protein 4
-
ANGPTL4 causes reduction of the activity of LPL via a two-step mechanism. The N-terminal coiled-coil domain of human ANGPTL4, residues 26-184, is expressed in Escherichia coli and purified
-
angiopoietin-like protein 4
-
ANGPTL4 inhibits the enzyme. The concentrations of inhibitor ANGPTL4 drops to 86% of baseline value at 280 min after alcohol consumption
-
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
-
apoC-III
-
derived from chylomicrons of a patient with severe hypertriglyceridemia, inhibits wild-type and enzyme mutant LPLS447X
-
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
-
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
-
Lys-Gly-Glu-Glu
-
not only inhibits the basal activity of lipoprotein lipase, but also blocks the activation effect of native apolipoprotein C II
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
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
sodium deoxycholate
-
81.8% relative activity in the presence of 5% (w/v) sodium deoxycholate
additional information
-
Morinda citrifolia leaf extract shows 66% inhibitory effect at 0.2 mg/ml, Morinda citrifolia fruit extract shows 54.5% inhibitory effect at 0.2 mg/ml, green tea extract shows 54.5% inhibitory effect at 0.2 mg/ml toward lipoprotein lipase
-
additional information
-
LPL activity in post-heparin normal human plasma is suppressed following co-incubation with 0.02 mg/ml cyclosporin A for 90 min, LPL activity in post-heparin normal human plasma is suppressed following co-incubation with 20 ng/ml rapamycin for 90 min, LPL activity in post-heparin normal human plasma is suppressed following co-incubation with 20 ng/ml tacrolimus for 90 min, LPL activity in post-heparin normal human plasma is suppressed following co-incubation with 0.01 mg/ml mycophenolate mofetil for 90 min
-
additional information
-
polyaspartate, polyglutamate and a a rabbit antiserum against the acidic domain of glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) block the binding of LPL to GPIHBP1
-
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
-
additional information
-
LPL activity decreases in the adipose tissue of diabetic rats without significant change in LPL mRNA
-
additional information
-
rottlerin, a protein kinase Calpha inhibitor, prevents protein kinase D phosphorylation and the subsequent increase in lipoprotein lipase
-
additional information
-
LPL activity in adipose tissue of rats fed chickpea or lentil flour is 1.7 or 1.5fold lower than that of rats fed casein
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
angiopoietin-like protein 4
-
major physiological regulator of enzyme activity under conditions of fasting and exercise
-
dexamethasone
-
induces increase in coronary lipoprotein lipase, combination of 100 nM dexmethasone with 100 nM insulin appreciably enhances lipoprotein lipase activity
glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1
-
binds lipoprotein lipase and chylomicrons and is a platform for lipolysis within capillaries
-
Gum arabic
-
197.6% relative activity in the presence of 1% (w/v) Gum Arabic, emulsifier for determination of LPL activity
-
Insulin
-
combination of 100 nM dexmethasone with 100 nM insulin appreciably enhances lipoprotein lipase activity
-
apoC-II
-
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
-
apoC-II
-
derived from chylomicrons of a patient with severe hypertriglyceridemia, activates wild-type and enzyme mutant LPLS447X
-
apoC-II
-
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
-
apoprotein C II
-
requirde for activity, approx. 7fold activation, amino acid residues 65-68 and 73-79 of the LPL N-terminal domain appear to act cooperatively to enable substantial activation
-
apoprotein CII
-
activation of triolein and phosphatidylcholine hydrolysis in emulsions
-
apoprotein CII
-
100% and 300% of increase in LPL activity for phosphatidyl-choline and triglyceride hydrolysis, respectively
-
heparin
-
heparin treatment results in an 11.75fold increase of LPL in the cell culture medium
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
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
-
2.4 higher LPL activity in patients treated with prednisolone is most probably due to an increase in the active dimeric form of LPL
-
additional information
-
lipoprotein lipase is upregulated at the transcriptional/translational level in patients with mucoskeletal sarcoma
-
additional information
-
treatment of macrophages with native C-reactive protein increases LPL protein expression and secretion in a dose- and time-dependent manner with maximum stimulatory effect at 0.003 mg/ml, incubation of LPL with vitamin E (0.05 mM) or NAC (10 mM) prevents the stimulatory effect of C-reactive protein on LPL
-
additional information
-
LpL is regulated by feeding/fasting and muscle contraction, insulin stimulates LpL by increasing the level of LpL mRNA and regulating LpL activity through both posttranscriptional and posttranslational mechanisms
-
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
initial rates and kinetics for complete hydrolysis of plasma lipids in postheparin plasma
-
additional information
additional information
-
Km-values of the chimeric molecule between human lipoprotein lipase and rat hepatic lipase
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00004
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25°C, pH 8.5, hydrolysis of p-nitrophenyl butyrate
0.00028
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25°C, pH 8.5, hydrolysis of tripropionin
0.00038
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25°C, pH 8.5, hydrolysis of tributyrin
0.0017
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25°C, pH 8.5, hydrolysis of tricaprylin
0.0031
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25°C, pH 8.5, hydrolysis of triacetin
0.0047
1,1'-bis(anilino)-4-,4'-bis(naphthalen)-8,8'-disulfonate
-
25°C, pH 8.5, hydrolysis of triolein
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.5
3-[4'-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)biphenyl-3-yl]propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.02
4-ethylphenylboronic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0014
4-nonylphenylboronic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0002
4-tert-butyl-N-[4-(5-methoxy-2-oxo-1,3,4-oxadiazol-3(2H)-yl)phenyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
8.7
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2 - 8.9
-
pH 7.2: about 45% of maximal activity, pH 8.9: about 95% of maximal activity
7.5 - 9.8
-
pH 7.5: about 80% of maximal activity, pH 9.8: about 55% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
-
20°C: about 35% of maximal activity, 40°C: about 50% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
650396, 650554, 651409, 652039, 652405, 652457, 652703, 664462, 665589, 665688, 693431, 709009, 715654, 715839, 716990, 80883, 80884, 80887, 80888, 80890, 80897, 80904, 80905, 80908, 80912, 80913, 80918, 80922
-
-
brenda
wild-type enzyme and mutant enzymes W382A, W390A, W393A, W394A, W393A/W394A and W114A
-
-
brenda
-
650369, 650738, 651409, 652186, 652428, 652702, 652707, 665343, 665649, 679124, 681258, 682283, 690453, 690660, 692579, 692691, 693158, 693229, 693348, 693511, 693516, 693523, 693527, 708067, 714778, 715190, 716707, 716787, 729143, 80840, 80845, 80846, 80847, 80887, 80888, 80890, 80894, 80899, 80909, 80912, 80913
-
-
brenda
-
SwissProt
brenda
functional deficiency of enzyme in a patient with severe hypertriglyceridemia
-
-
brenda
-
652229, 652987, 664839, 690348, 690827, 693188, 693433, 694184, 708067, 715633, 715839, 716101, 729291, 729306, 80886, 80911, 80912
-
-
brenda
retinoid X receptor gamma-deficient mice, increase in activity of skeletal enzyme isoform
-
-
brenda
transgenic animals with beta-cell-specific overexpression or inactivation of enzyme
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
limb muscle, increase of enzyme activity and mRNA level upon chronic stress
brenda
-
GPIHBP1 shuttles lipoprotein lipase from subendothelial spaces to the capillary lumen
brenda
-
noncancer tissue. Lipoprotein lipase activity is higher in cancer tissue than in noncancer tissue. Lipoprotein lipase gene expression is higher in noncancer tissue compared to cancer tissue
brenda
-
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
brenda
-
LPL is synthesized by parenchymal cells, from which it is secreted and then transported to the lumen surface of endothelial cells
brenda
-
fasting for 2 weeks or insulin administration has no effect on activity
brenda
additional information
scopoletin significantly increases lipoprotein lipase activity in 3T3-L1 adipocytes
brenda
-
range of enzyme activity differs up to 4fold among mink, mice, chinese hamster, rat and guinea pig
brenda
-
range of enzyme activity differs up to 4fold among mink, mice, chinese hamster, rat and guinea pig
brenda
-
significantly reduced LPL activity in parametrial adipose tissue from mice fed with conjugated linoleic acid
brenda
-
range of enzyme activity differs up to 4fold among mink, mice, chinese hamster, rat and guinea pig
brenda
-
range of enzyme activity differs up to 4fold among mink, mice, chinese hamster, rat and guinea pig
brenda
-
increase in enzyme activity in presponse to feeding, during 4 h, then decrease to basal levels at 6 h. Fasting produces down-regulation of enzyme activity, concomitant with low levels of plasma insulin. Stimulation of enzyme activity by injection of insulin, especially stimulation of the proportion of enzyme in active conformation at the extracellular level
brenda
-
range of enzyme activity differs up to 4fold among mink, mice, chinese hamster, rat and guinea pig
brenda
-
decrease of enzyme activity in mesenteric and epididymal white adipose tissue upon chronic stress, accompanied by weight reduction of tissue. Decrease of enzyme activity upon acute stress only in retroperitoneal white adipose tissue
brenda
-
-
brenda
-
fasting for 2 weeks provokes a clear decrease in activity. Insulin administration induces an increase in activity 3 h after the injection
brenda
-
decreased to 78% and 73% of baseline values 2 h and 4 h after glucose administration, respectively
brenda
-
measurable LPL activity is present only in postheparin plasma
brenda
-
heparin releases LPL from its in vivo binding sites allowing it to enter the blood plasma
brenda
-
limb muscle, increase of enzyme activity and mRNA level upon chronic and acute stress
brenda
-
in vivo administration of adrenaline and acute stress causes an increase in plasma lipoprotein lipase activity
brenda
-
LPL activity increases in homone-sensitive lipase ko-mice
brenda
-
LPL is synthesized by parenchymal cells, from which it is secreted and then transported to the lumen surface of endothelial cells
brenda
-
range of enzyme activity differs up to 6fold among mink, mice, chinese hamster, rat and guinea pig
brenda
-
range of enzyme activity differs up to 6fold among mink, mice, chinese hamster, rat and guinea pig
brenda
-
range of enzyme activity differs up to 6fold among mink, mice, chinese hamster, rat and guinea pig
brenda
-
range of enzyme activity differs up to 6fold among mink, mice, chinese hamster, rat and guinea pig
brenda
-
range of enzyme activity differs up to 6fold among mink, mice, chinese hamster, rat and guinea pig
brenda
-
limb muscle, increase of enzyme activity and mRNA level upon chronic stress
brenda
when actinomycin is given to fed rats, heparin-releasable lipoprotein lipase activity increases by 160% in 6 h
brenda
-
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
brenda
-
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
brenda
-
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.
brenda
-
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
brenda
-
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
brenda
-
injection of labelled enzyme. Uptake of enzyme through sinusoidal membrane, where it becomes internalized and degraded. Injection of heparin prior to injection of enzyme results in increased enzyme-immunostaining in Kupffer cells. Injection of inactive enzyme also results in increased staining of Kupffer cells
brenda
-
patient with severe hypertriglyceridemia, post-heparin enzyme mass is almost normal, but the enzyme activity is remarkably decreased
brenda
-
LpL is present in the liver during fetal and early postnatal life, but is then suppressed by a putative transcriptional regulatory mechanism
brenda
-
presence of substantial amounts of inactive enzyme. After injection of heparin, enzyme mass in liver increases, and enzyme activity also increases, but in protportion to mass
brenda
-
noncancer tissue. Lipoprotein lipase activity is higher in cancer tissue than in noncancer tissue. Lipoprotein lipase gene expression is higher in noncancer tissue compared to cancer tissue
brenda
-
in the mammary gland, synthesis of LpL is induced during late pregnancy and lactation
brenda
-
-
650396, 650554, 652039, 652457, 652703, 665589, 693431, 715654, 80883, 80884, 80885, 80887, 80888, 80890, 80904, 80905, 80908, 80913, 80922
brenda
-
red or white muscle, no stimulation of enzyme activity after injection of insulin
brenda
-
limb muscle, increase of enzyme activity and mRNA level upon chronic stress
brenda
LPL is highly expressed and active in the ovary during gonadal development, the LPL mRNA expression is localised to the follicle cells surrounding the oocyte
brenda
-
LPL activity increases in homone-sensitive lipase ko-mice
brenda
soleus, when actinomycin is given to fed rats, heparin-releasable lipoprotein lipase activity increases by 150% in 6 h
brenda
-
highest expression is found in white adipose tissue
brenda
-
LPL activity increases in homone-sensitive lipase ko-mice
brenda
-
retroperitoneal white adipose tissue lipoprotein lipase activity is rapidly down-regulated in response to acute stress
brenda
additional information
-
LPL is expressed in a wide variety of cell types, particularly in adipocytes and myocytes
brenda
additional information
-
almost no expression in brain, heart, intestine, and testis
brenda
additional information
almost no expression in brain, heart, intestine, and testis
brenda
additional information
no mRNA transcripts are found in intestine, liver, brain, heart, kidney, muscle, and spleen
brenda
additional information
-
no mRNA transcripts are found in intestine, liver, brain, heart, kidney, muscle, and spleen
brenda
additional information
-
LpL mRNA is not detected in peritoneal macrophages or plasma white cells of transgenic mice
brenda
additional information
-
GPIHBP1 is the protein responsible for translocation of enzyme LPL to the capillary lumen
brenda
additional information
-
enzyme LPL is produced and secreted from parenchymal cells like adipocytes and myocytes for transport to the luminal side of the endothelium via interaction with the glycosylphosphatidylinositol-anchored high density lipoprotein binding protein 1 (GPIHBP1)
brenda
additional information
-
adipose tissue LPL activity is markedly higher than placental LPL activity. In pregnant women, adipose tissue LPL activity, which hydrolyzes triglycerides to free fatty acids for uptake into maternal fat, is not correlated with body weight or newborn adiposity
brenda
additional information
A0A076L550
LPL gene expression occurs in various tissues, real-time quantitative PCR enzyme expression analysis, effects of different dietary lipids on the expression of LPL in different tissues, overview
brenda
additional information
-
LPL is expressed in a wide variety of cell types, particularly in adipocytes and myocytes
brenda
additional information
-
LPL is expressed in a wide variety of cell types, particularly in adipocytes and myocytes
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
small pool is present in low density membrane vesicles
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
A0A076L550
phylogenetic tree based on lipoprotein lipase amino acid sequences
malfunction
metabolism
physiological function
additional information
malfunction
-
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
malfunction
-
lipoprotein lipase (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
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
malfunction
-
acute hypoxia strongly inhibits lipoprotein lipase activity in differentiated human preadipocytes and increases non-esterified fatty acid release, adversely affecting postprandial lipemia. In differentiated preadipocytes, acute hypoxia induces a 6fold reduction in lipoprotein lipase activity. Acute intermittent hypoxia increases circulating plasma non-esterified fatty acid in young healthy men, but does not seem to affect postprandial triglyceride levels, nor subcutaneous abdominal adipose tissue lipoprotein lipase activity and adipocyte lipolysis. The reduction in adipose tissue LPL activity appears to be explained by the upregulation of an important posttranslational repressor of LPL, angiopoietin-like protein 4 (ANGPTL4)
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
-
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
-
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
metabolism
A0A076L550
lipoprotein lipase (LPL) is a key enzyme in lipid deposition and metabolism. Nutritional regulation of LPL in redlip mullet
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 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
-
arachidonic acid signaling requires DAGL in many systems. L- and N-current but not M-current inhibition by M1 muscarinic receptors requires DAG lipase activity, overview. The signaling pathway mediating L- and N-current inhibition diverges from the pathway initiating M-current inhibition
physiological function
-
lipoprotein lipase serves a dual function as a triglyceride lipase of circulating chylomicrons and very-low-density lipoproteins and facilitates receptor-mediated lipoprotein uptake into heart, muscle and adipose tissue
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
-
lipoprotein lipase is an amyloid beta-binding protein that promotes glycosaminoglycan-dependent cellular uptake of amyloid beta in astrocytes
physiological function
-
lipoprotein lipase plays a potential role in the pathophysiological response of the brain to cerebral ischemia-reperfusion
physiological function
-
overexpression of human lipoprotein lipase in mouse mammary glands leads to reduction of milk triglyceride and delayed growth of suckling pups
physiological function
-
lipoprotein lipase (LPL) reduces the infectivity of hepatitis C virus through its catalytic activity on hepatitis C virus-associated lipoproteins. LPL treatment reduces association of hepatitis C virus with ApoE
physiological function
-
the enzyme is rate limiting for plasma triglyceride clearance and tissue uptake of fatty acids
physiological function
-
the up-regulation of enzyme activity may be beneficial in obesity and diabetes
physiological function
A0A076L550
lipoprotein lipase (LPL) is a key enzyme in lipid deposition and metabolism. Nutritional regulation of LPL in redlip mullet
physiological function
-
LPL is responsible for bridging the uptake of LDL and VLDL particles by the liver through an interaction mediated by the C-terminus of LPL. Angiopoietin-like protein 4 (ANGPTL4) and apolipoproteins regulate LPL, ANGPTL4 inhibits LPL by a noncompetitive mechanism
physiological function
-
lipoprotein lipase is a feature of alternatively-activated microglia and may facilitate lipid uptake in the CNS during demyelination. Lipoprotein lipase is involved in microglial lipid uptake. 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
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
physiological function
-
the hydrolytic breakdown of plasma triglycerides by LPL at the capillary endothelium is a crucial event that contributes to control of the levels of triglycerides in plasma. LPL hydrolyzes triglycerides in plasma lipoproteins through a complex regulation mechanism
physiological function
-
adipose tissue regulates postprandial lipid metabolism by storing dietary fat through lipoprotein lipase-mediated hydrolysis of exogenous triglycerides, and by inhibiting delivery of endogenous non-esterified fatty acid to nonadipose tissues. In humans, the rise in postprandial triglyceride levels does not differ between normoxia and intermittent hypoxia. Nonesterified fatty acid levels are higher during intermittent hypoxia session. Intermittent hypoxia does not affect subcutaneous abdominal adipose tissue lipoprotein lipase activity. No differences are observed in lipolytic responses of isolated subcutaneous abdominal adipocytes between normoxia and intermittent hypoxia sessions
physiological function
-
the enzyme is the key enzyme responsible for intravascular triglyceride lipolysis. The acute alcohol consumption can induce hypertriglyceridemia, partly by influencing of lipoprotein lipase (LPL) through alcohol. LPL is the key enzyme responsible for triglyceride hydrolysis in circulation. The acute effects of alcohol consumption, especially on postprandial lipemia, seem to be accentuated in hypertriglyceridemic subjects
physiological function
-
placental lipoprotein lipase activity is positively associated with newborn adiposity. Placental lipoprotein lipase (pLPL) hydrolyzes triglycerides (TG), both dietary chylomicron TG (CM-TG) and very-low density lipoprotein TG (VLDL-TG), to free fatty acids (FFA). This may promote fetal fat accretion by increasing the available FFA pool for placental uptake. pLPL activity, but not maternal adipose tissue LPL activity, is associated with newborn adiposity and higher maternal TG. Placental LPL activity is positively correlated with birthweight and newborn percent body fat, but maternal adipose tissue LPL is not. Maternal TG and BMI are not correlated with pLPL. pLPL gene expression, while modestly correlated with enzymatic activity, is not correlated with newborn adiposity. Placental lipase regulation and the role of pLPL in pregnancies, overview
physiological function
-
lipoprotein lipase (LPL) is a key enzyme in facilitating fatty acid uptake from lipoproteins. Very low-density lipoprotein-triglyceride (VLDL-TG) is a quantitative important substrate for lipid oxidation contributing with 10-20% to total energy expenditure, but only 3-6% during exercise despite an increase in total lipid oxidation. VLDL-TG storage is measured in adipose tissue biopsies. Exercise does not affect muscle LPL activity. No association is observed between muscle LPL activity and VLDL-TG oxidation, neither in the basal state nor during exercise. Exercise does not affect upper body or lower body adipose tissue LPL activity. The basal adipose tissue fractional VLDL-TG storage is not associated with upper body or lower body subcutaneous adipose tissue LPL activity. Muscle LPL activity does not predict VLDL-TG oxidation during rest or exercise. In addition, adipose tissue LPL activity is not associated with VLDL-TG storage
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
-
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
-
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
-
additional information
-
the enzyme interacts with glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1) and lipoprotein receptor-related protein (LRP), enzyme ligand interaction analysis by surface plasmon resonance. Enzyme structure modeling
additional information
-
enzyme ligand interaction analysis by isothermal titration calorimetry (ITC) using human plasma as substrate. ITC can be used for quantitative measurements of LPL activity and interactions under in vivo-like conditions, for comparisons of the properties of plasma samples from patients and control subjects as substrates for LPL, as well as for testing of drug candidates, method evaluation, overview
Show AA Sequence and Transmembrane Helices (316 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34000
-
x * 34000, SDS-PAGE, equilibrium sedimentation in presence of 6 M guanidine HCl and 0.1% mercaptoethanol
48300
-
2 * 48300, equilibrium sedimentation in guanidine under reducing und nonreducing conditions
55000
-
2 * 55000, dissociation of the dimer into monomers leads to irreversible loss of activity
56000
60000
96900
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
additional information
?
-
x * 34000, SDS-PAGE, equilibrium sedimentation in presence of 6 M guanidine HCl and 0.1% mercaptoethanol
dimer
-
mass spectrometry, dynamic light scattering. Enzyme is a dynamice dimer in which the subunits rapidly exchange partners. Presence of heparin or lipoproteins does not markedly slow the exchange rate
dimer
-
2 * 48300, equilibrium sedimentation in guanidine under reducing und nonreducing conditions
dimer
-
2 * 55000, dissociation of the dimer into monomers leads to irreversible loss of activity
homodimer
-
dissociation of the dimeric form to the monomeric form is associated with a conformational change of the molecule and irreversible loss of catalytic activity
additional information
-
heparin-resistant binding of monomeric enzyme to monocytes and macrophages
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
side-chain modification
side-chain modification
-
8.3% carbohydrate including mannose, galactose, glucose, N-acetylglucosamine and sialic acid; glycoprotein
side-chain modification
-
8% carbohydrate, 2% mannose, 2% galactose, 3% glucosamine; glycoprotein
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
W390A
-
decreased activity with monoclonal antibody 5D2, decreased activity against a synthetic emulsion of long-chain triacylglycerols and in particular against rat lymph chylomicrons
C418Y
-
the mutation abolishes lipoprotein lipases's ability to bind to GPIHBP1 and therefore abolishes LPL transport across endothelial cells byGPIHBP1, without interfering with the enzyme catalytic activity or binding to heparin
D204E
-
homozygous missense mutation identified in a patient with severe hypertriglyceridemia, post-heparin enzyme mass is almost normal, but the enzyme activity is remarkably decreased. In presence of phosphatidylethenolamine, phospatidylserine, and cardiolipin as emulsifier, triolein-hydrolizing activity of the mutant is higher than wild-type activity
D9N
-
the mutation is associated with partial changes in enzyme function, plasma high density lipoprotein-C, triglyceride levels, and differential susceptibility to cardiovascular disease
E421K
-
the mutation abolishes lipoprotein lipases's ability to bind to GPIHBP1 and therefore abolishes LPL transport across endothelial cells byGPIHBP1, without interfering with the enzyme catalytic activity or binding to heparin
K430A/R432A/K434A/K440A/K441A
-
the mutant LPL has little or no ability to bind to GPIHBP1 on the surface of cells
N291S
-
the mutation is associated with partial changes in enzyme function, plasma high density lipoprotein-C, triglyceride levels, and differential susceptibility to cardiovascular disease
S447X
additional information
S447X
-
the mutation is associated with a higher risk for pancreatic calcification and steatorrhea in hyperlipidemic pancreatitis
S447X
-
the mutation results in truncation of the last two amino acids of the mature LPL and is the only mutation reported to increase enzymatic activity, the mutation is associated with differential susceptibility to cardiovascular disease
S447X
-
site-directed mutagenesis, the mutant is inhibited by angiopoietin-like protein 4 in the same way as the wild-type enzyme
additional information
-
enzyme coated with both dextrin (D) and ionic surfactant (i) via lyophilization, LPL-D1, is prepared by freeze-drying a solution containing LPL (52% protein), dextrin (D), and surfactant at a 1:2:1 weight ratio in 1:1 (v/v) water-dioxane. LPL-D1 is as active as its native counterpart in water but about 3000fold more active than the latter in organic solvent
additional information
-
exchanging lids between lipoprotein lipase and endothelial lipase only partially shifts the substrate specificity of the enzymes. Studies of a double chimera possessing both the lid and the C-terminal domain (C-domain) of endothelial lipase in the lipoprotein lipase backbone showed that the role of the lid in determining substrate specificity does not depend on the nature of the C-domain of the lipase
additional information
-
two LPL intronic variants may be associated with development of the hypertension endophenotype with elevated plasma triglycerid level (cSNPs g.7663364C4A in exon 8 and g.7664652C4G in exon 9)
additional information
-
construction of the lipoprotein lipase truncation variant, LPLS447X, the truncation leads to increased lipoprotein uptake of the cells, gain-of-function phenotype in vivo. Mutant LPLS447X enhances lipoprotein uptake to a greater degree than wild-type LPL does
additional information
-
chimeric molecule between human lipoprotein lipase and rat hepatic lipase
additional information
-
chimeric lipase consisting of the amino-terminal 314 amino acids of human lipoprotein lipase and the carboxyl-terminal 146 amino acids of human hepatic lipase. The chimeric enzyme hydrolyzes both long chain and short chain fatty acid triacylglycerols and has catalytic properties that are similar to lipoprotein lipase
additional information
-
chimeric lipase constructed of the N-terminal 329 residues of rat hepatic lipase linked to the C-terminal 136 residues of human lipoprotein lipase. The chimera hydrolyzes both monodisperse short-chain (esterase) and emulsified long-chain (lipase) triacylglycerol substrates with catalytic and kinetic properties closely resembling those of native lipase
additional information
-
nonsense mutation Gln106Stop, missense mutations: Gly142Glu, Ala176Thr, Gly188Glu, Ile194Thr, Pro207Leu and Arg243His
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18
-
5 mM sodium barbital buffer, pH 7.5, 20% v/v glycerol, 0.1% v/v Triton X-100, 2 M NaCl, half-life: 40 h
25
37
additional information
-
high concentrations of glycerol or glycine prevent inactivation at 37°C and at 4°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme has a strong propensity to aggregate. No aggregation is observed at 0.3 M NaCl concentration or higher. Albumin or heparin may prevent aggregation at 0.15 M NaCl
-
the partially purified enzyme at later stages is stabilized by the inclusion of 20% glycerol in the buffer
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
lipoprotein lipase (LPL) from Burkholderia species is also highly active in organic solvent if it is coated with both dextrin (D) and ionic surfactant (i) via lyophilization. LPL-D1 is as active as its native counterpart in water but about 3000fold more active than the latter in organic solvent
additional information
-
activation of a lipoprotein lipase from Burkholderia species by glucose-headed surfactants (GHSs) for enhancing its catalytic activity in organic solvent, three different GHSs, resulting in BSLPL-1a-G, BSLPL-1b-G, and BSLPL-1c-G, are evaluated, overview. Nearly aqueous-like activity of lipoprotein lipase treated with GHS in organic solvent. GHS-treated lipoprotein lipase are determined for the hydrolysis or alcoholysis of p-nitrophenyl acetate. GHS-treated lipoprotein lipase is 4 to 5 orders of magnitude more active than its native counterpart in organic solvent
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
biotinylated enzyme by sucrose density gradient centrifugation and heparin affinity chromatography
-
partial
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
chimeric lipase consisting of the amino-terminal 314 amino acids of human lipoprotein lipase and the carboxyl-terminal 146 amino acids of human hepatic lipase
-
expression in rabbit inhibits diet-induced hypercholesterolemia and atherosclerosis
-
expression in Sf21 insect cells, coexpression with calreticulin enhances yield of active LPL by a factor 9
-
fusion protein consisting of the complete lipoprotein lipase molecule and the mature form of apolipoprotein CII, expression in human embryonic kidney 293 cells
-
gene Lpl, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree based on lipoprotein lipase amino acid sequences, real-time quantitative PCR enzyme expression analysis
A0A076L550
gene Lpl, real-time PCR enzyme expression analysis
LPL overexpression in Mus musculus skeletal muscle increases cold tolerance by enhancing capacity for fat oxidation, producing an avian-like phenotype in which skeletal muscle contributes significantly to the thermogenic response to cold temperatures
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
effects of dietary lipid levels on the expression of LPL in the redlip mullet
A0A076L550
insulin, dexamethasone and cortisol increase mRNA and activity in adipose organs. Cold markedly stimulates enzyme activity in brown adipose tissue
-
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
lipasin suppresses the activity of LPL specifically in cardiac and skeletal muscles
lipoprotein lipase activity is significantly decreased in the ischemic side cortex at 2 h ischemia
-
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
-
stress and catecholamines reduce adipose enzyme activity. Tissue necrosis factpor alpha represses enzyme activity by downregulating transcription
-
the mRNA expression and activity of brain lipoprotein lipase (LPL) is increased after acute cerebral ischemia-reperfusion in rats. Increase of LPL immunopositive cells in the cerebral cortex around the infarction area is observed at 4, 6, 12 h ischemia, 2 h ischemia 2 h reperfusion, and 4 h ischemia 2 h reperfusion
-
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
-
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
-
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
-
lipasin suppresses the activity of LPL specifically in cardiac and skeletal muscles
-
lipasin suppresses the activity of LPL specifically in cardiac and skeletal muscles
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
after fulll denaturation in 6 M guanidinium choride or after dissociation in monomers in 1 M guanidinium chloride. Presence of Ca2+ is crucial for reactivation, which involves at least two steps. First step is rapid and results in formation of an inactive monomer with a completely folded C-terminal domain, second step is promoted by Ca2+ and converts enzyme monomers to dimerization-competent and more tightly folded monomers that rapidly form active dimers. Proline isomerization is rate-limiting for the second step
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
synthesis
-
enantiomerically enriched diarylmethanols are useful as the precursors or building blocks for the synthesis of pharmaceutically important compounds such as antihistaminic, antiarrhythmic, and anticholinergic agents. Successful application of this LPL preparation (LPL-D1) to the dynamic kinetic resolution (DKR) of diarylmethanols including aryl heteroarylmethanols, method, overview
medicine
-
heparin-resistant binding of monomeric enzyme to monocytes and macrophages. Enzyme-mediated binding of low density lipoproteins to cell surfaces is enhanced in presence of dexamethasone
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
medicine
-
determination of enzyme and of hepatic triacylglycerol lipase activity and comparison with serum adiponectin levels in Japanese hyperlipidemic men. Co-linearity between insulin sensitivity and adiponectin as well as insulin sensitivity and enzyme/hepatic triacylglycerol lipase activity
medicine
-
comparison of protein and mRNA levels of enzyme and several muscle lipid-binding proteins in healthy, nonobese, nontrained, moderately trained, and endurance-trained women and men. In the nontrained state, women have higher muscle RNA levels of several proteins related to lipid metabolism compared with men. In the endurance-trained state, only the gender difference in lipoprotein lipase mRNA persists
medicine
-
enzyme significantly suppresses TNF-alpha-induced gene expression, and this suppression is reversed by tetrahydrolipstatin and heparinase. In contrast, enzyme synergistically enhances IFN-gamma-induced gene expression
medicine
-
expression of enzyme in transgenic rabbit, no significant difference in plasma glucose clearance rate between transgenic and control animals. Transgenic animals show reduced plasma levels for free fatty acids and glucose and increased postheparin plasma enzyme activity
medicine
-
measurement of enzyme activity using intravenous fat tolerance test before and after oral administration of glucose. Enzyme activity decreases to 78% and 73% of control levels 2 and 4 h after glucose administration, resp. Use of intravenous fat tolerance test for studying acute changes in enzyme activity
medicine
-
the intravenous fat tolerance test is a promising approach for studying acute changes in LPL activity in circulation
medicine
-
excess vascular wall LpL augments vascular dysfunction in the setting of inflammation
medicine
-
LPL mutations represent a risk factor which contributes to the development of cardiovascular disease
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