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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
the enzyme is responsible for the harvesting of fatty acids from the triacylglycerols of circulating serum lipoproteins in those tissues that utilize these triacylglycerols
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
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
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
the enzyme is responsible for the harvesting of fatty acids from the triacylglycerols of circulating serum lipoproteins in those tissues that utilize these triacylglycerols
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
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
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
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
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
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
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
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
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
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 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
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
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
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
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
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
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 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
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
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
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
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
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
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)
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
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
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
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
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
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
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.
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
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
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
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
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
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
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
dissociation of the dimeric form to the monomeric form is associated with a conformational change of the molecule and irreversible loss of catalytic activity
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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
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
fusion protein consisting of the complete lipoprotein lipase molecule and the mature form of apolipoprotein CII, expression in human embryonic kidney 293 cells
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
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
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
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
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
decreased activity with monoclonal antibody 5D2, decreased activity against a synthetic emulsion of long-chain triacylglycerols and in particular against rat lymph chylomicrons
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
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
the mutation is associated with partial changes in enzyme function, plasma high density lipoprotein-C, triglyceride levels, and differential susceptibility to cardiovascular disease
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
the mutation is associated with partial changes in enzyme function, plasma high density lipoprotein-C, triglyceride levels, and differential susceptibility to cardiovascular disease
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
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
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)
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
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
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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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
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
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
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
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
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
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
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