PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25138789-1 2014 Angiopoietin-like protein 4 (ANGPTL4) may regulate lipoprotein lipase-dependent plasma clearance of triacylglycerol from skeletal muscle during exercise. Triglycerides 100-115 lipoprotein lipase Mus musculus 51-69 25685701-1 2015 OBJECTIVE: Lipoprotein lipase (LPL) is a key regulator of circulating triglyceride rich lipoprotein hydrolysis. Triglycerides 70-82 lipoprotein lipase Mus musculus 11-29 25685701-1 2015 OBJECTIVE: Lipoprotein lipase (LPL) is a key regulator of circulating triglyceride rich lipoprotein hydrolysis. Triglycerides 70-82 lipoprotein lipase Mus musculus 31-34 25395613-6 2015 Diabetic mice had a marked decrease in postprandial triglycerides clearance, which was associated with decreased lipoprotein lipase and peroxisome proliferator-activated receptor alpha mRNA levels in peripheral tissues and decreased lipoprotein lipase activity in skeletal muscle, heart, and brown adipose tissue. Triglycerides 52-65 lipoprotein lipase Mus musculus 113-131 25395613-6 2015 Diabetic mice had a marked decrease in postprandial triglycerides clearance, which was associated with decreased lipoprotein lipase and peroxisome proliferator-activated receptor alpha mRNA levels in peripheral tissues and decreased lipoprotein lipase activity in skeletal muscle, heart, and brown adipose tissue. Triglycerides 52-65 lipoprotein lipase Mus musculus 233-251 25395613-7 2015 Diabetic heterozygous lipoprotein lipase knockout mice had markedly elevated fasting plasma triglyceride levels and prolonged postprandial triglycerides clearance. Triglycerides 92-104 lipoprotein lipase Mus musculus 22-40 25395613-7 2015 Diabetic heterozygous lipoprotein lipase knockout mice had markedly elevated fasting plasma triglyceride levels and prolonged postprandial triglycerides clearance. Triglycerides 139-152 lipoprotein lipase Mus musculus 22-40 23542081-1 2013 Adipose fat storage is thought to require uptake of circulating triglyceride (TG)-derived fatty acids via lipoprotein lipase (LpL). Triglycerides 64-76 lipoprotein lipase Mus musculus 106-124 23001493-14 2014 ORAL ADMINISTRATION OF APE [200 AND 400 MG/(KG DAY)] DOSE-DEPENDENTLY ELEVATED THE EXPRESSION OF PPARalpha IN HYPERLIPIDEMIC MICE (P<0.05 OR P<0.01): CONCLUSION: APE could reduce TG level via up-regulation of LPL activity, which provides new evidence to elucidate the anti-hyperlipidemic effects of APE. Triglycerides 185-187 lipoprotein lipase Mus musculus 215-218 23597845-0 2013 Estimation of plasma triglycerides with correction for free glycerol by orlistat inhibition of lipoprotein lipase activity. Triglycerides 21-34 lipoprotein lipase Mus musculus 95-113 23597845-1 2013 This report presents a modification of the enzymatic method (lipoprotein lipase/glycerol kinase/glycerol-3-phosphate oxidase/peroxidase) for determination of plasma triglyceride levels in order to achieve correction for the free glycerol content. Triglycerides 165-177 lipoprotein lipase Mus musculus 61-79 24085031-0 2013 Rescue of heart lipoprotein lipase-knockout mice confirms a role for triglyceride in optimal heart metabolism and function. Triglycerides 69-81 lipoprotein lipase Mus musculus 16-34 24085031-3 2013 Deletion of the primary triglyceride-hydrolyzing enzyme lipoprotein lipase (LPL) leads to cardiac dysfunction. Triglycerides 24-36 lipoprotein lipase Mus musculus 56-74 24085031-3 2013 Deletion of the primary triglyceride-hydrolyzing enzyme lipoprotein lipase (LPL) leads to cardiac dysfunction. Triglycerides 24-36 lipoprotein lipase Mus musculus 76-79 24086538-2 2013 Mutated-LPL (MLPL) gene transfer significantly increased the concentrations of plasma MLPL and triglyceride (TG) but significantly decreased the activity of plasma LPL. Triglycerides 95-107 lipoprotein lipase Mus musculus 8-11 24086538-2 2013 Mutated-LPL (MLPL) gene transfer significantly increased the concentrations of plasma MLPL and triglyceride (TG) but significantly decreased the activity of plasma LPL. Triglycerides 95-107 lipoprotein lipase Mus musculus 14-17 24086538-2 2013 Mutated-LPL (MLPL) gene transfer significantly increased the concentrations of plasma MLPL and triglyceride (TG) but significantly decreased the activity of plasma LPL. Triglycerides 109-111 lipoprotein lipase Mus musculus 8-11 24086538-2 2013 Mutated-LPL (MLPL) gene transfer significantly increased the concentrations of plasma MLPL and triglyceride (TG) but significantly decreased the activity of plasma LPL. Triglycerides 109-111 lipoprotein lipase Mus musculus 14-17 23650188-2 2013 This has been attributed to a stimulating role for APOA5 in lipoprotein lipase-mediated triglyceride hydrolysis and hepatic clearance of lipoprotein remnant particles. Triglycerides 88-100 lipoprotein lipase Mus musculus 60-78 23542081-1 2013 Adipose fat storage is thought to require uptake of circulating triglyceride (TG)-derived fatty acids via lipoprotein lipase (LpL). Triglycerides 64-76 lipoprotein lipase Mus musculus 126-129 23542081-1 2013 Adipose fat storage is thought to require uptake of circulating triglyceride (TG)-derived fatty acids via lipoprotein lipase (LpL). Triglycerides 78-80 lipoprotein lipase Mus musculus 106-124 23542081-1 2013 Adipose fat storage is thought to require uptake of circulating triglyceride (TG)-derived fatty acids via lipoprotein lipase (LpL). Triglycerides 78-80 lipoprotein lipase Mus musculus 126-129 23386706-9 2013 In conclusion, CIH inactivates LPL by upregulating Angptl4, but inhibition of TG uptake occurs predominantly via an Angptl4/LPL-independent mechanism. Triglycerides 78-80 lipoprotein lipase Mus musculus 124-127 22963823-1 2012 LPL (lipoprotein lipase) is a rate-limiting enzyme involved in the hydrolysis of triglycerides. Triglycerides 81-94 lipoprotein lipase Mus musculus 0-3 22963823-1 2012 LPL (lipoprotein lipase) is a rate-limiting enzyme involved in the hydrolysis of triglycerides. Triglycerides 81-94 lipoprotein lipase Mus musculus 5-23 23186339-1 2012 BACKGROUND: Lipoprotein lipase (LPL) hydrolyzes triglycerides in plasma lipoproteins and enables uptake of lipolysis products for energy production or storage in tissues. Triglycerides 48-61 lipoprotein lipase Mus musculus 12-30 23186339-1 2012 BACKGROUND: Lipoprotein lipase (LPL) hydrolyzes triglycerides in plasma lipoproteins and enables uptake of lipolysis products for energy production or storage in tissues. Triglycerides 48-61 lipoprotein lipase Mus musculus 32-35 22809513-9 2012 Therefore, a potential mechanism for Lipasin-mediated triglyceride elevation is through reduced triglyceride clearance by LPL inhibition. Triglycerides 54-66 lipoprotein lipase Mus musculus 122-125 22732211-1 2012 Lipoprotein lipase (LPL) is important for clearance of triacylglycerols (TG) from plasma both as an enzyme and as a bridging factor between lipoproteins and receptors for endocytosis. Triglycerides 55-71 lipoprotein lipase Mus musculus 0-18 22732211-1 2012 Lipoprotein lipase (LPL) is important for clearance of triacylglycerols (TG) from plasma both as an enzyme and as a bridging factor between lipoproteins and receptors for endocytosis. Triglycerides 55-71 lipoprotein lipase Mus musculus 20-23 22732211-1 2012 Lipoprotein lipase (LPL) is important for clearance of triacylglycerols (TG) from plasma both as an enzyme and as a bridging factor between lipoproteins and receptors for endocytosis. Triglycerides 73-75 lipoprotein lipase Mus musculus 0-18 22732211-1 2012 Lipoprotein lipase (LPL) is important for clearance of triacylglycerols (TG) from plasma both as an enzyme and as a bridging factor between lipoproteins and receptors for endocytosis. Triglycerides 73-75 lipoprotein lipase Mus musculus 20-23 22732211-7 2012 In vivo, postprandial TG protected LPL from inactivation by recombinant NT-ANGPTL4 injected to mice. Triglycerides 22-24 lipoprotein lipase Mus musculus 35-38 22540257-1 2012 Lipoprotein lipase (LPL) is rate limiting in the provision of triglyceride-rich lipoprotein-derived lipids into tissues. Triglycerides 62-74 lipoprotein lipase Mus musculus 0-18 22540257-1 2012 Lipoprotein lipase (LPL) is rate limiting in the provision of triglyceride-rich lipoprotein-derived lipids into tissues. Triglycerides 62-74 lipoprotein lipase Mus musculus 20-23 22809513-9 2012 Therefore, a potential mechanism for Lipasin-mediated triglyceride elevation is through reduced triglyceride clearance by LPL inhibition. Triglycerides 96-108 lipoprotein lipase Mus musculus 122-125 22262056-4 2012 Consistent with the essential role of LPL in triglyceride clearance, CREB-H-deficient mice showed hypertriglyceridemia, associated with defective production of these apolipoproteins and decreased LPL activity. Triglycerides 45-57 lipoprotein lipase Mus musculus 38-41 22018640-9 2011 Inhibition of lipoprotein lipase (LPL) appeared to suppress inflammation and triglyceride accumulation by Ctrl-VLDL suggesting that hydrolysis of VLDL is required for the pro-inflammatory properties of VLDL. Triglycerides 77-89 lipoprotein lipase Mus musculus 14-32 22018640-9 2011 Inhibition of lipoprotein lipase (LPL) appeared to suppress inflammation and triglyceride accumulation by Ctrl-VLDL suggesting that hydrolysis of VLDL is required for the pro-inflammatory properties of VLDL. Triglycerides 77-89 lipoprotein lipase Mus musculus 34-37 21177248-1 2011 Lipoprotein lipase (LPL) is a member of a lipase family known to hydrolyze triglyceride molecules in plasma lipoprotein particles. Triglycerides 75-87 lipoprotein lipase Mus musculus 20-23 21705711-6 2011 The decrease in very low-density lipoprotein (VLDL) was caused by enhanced lipoprotein lipase-mediated VLDL-TG clearance and by decreased production of VLDL-TG and VLDL-apolipoprotein B. Triglycerides 108-110 lipoprotein lipase Mus musculus 75-93 21367960-7 2011 Microarray and real-time reverse transcriptase PCR analyses revealed that diosgenin administration increased 12-fold the expression of lipoprotein lipase, which may contribute to reduced serum triglyceride levels. Triglycerides 193-205 lipoprotein lipase Mus musculus 135-153 21195353-2 2011 To examine whether lipoprotein lipase (LPL), a serine hydrolase that releases FFAs from circulating triglyceride (TG)-rich lipoproteins, might contribute to FFA-mediated signaling in the brain, we created neuron-specific LPL-deficient mice. Triglycerides 100-112 lipoprotein lipase Mus musculus 19-37 21195353-2 2011 To examine whether lipoprotein lipase (LPL), a serine hydrolase that releases FFAs from circulating triglyceride (TG)-rich lipoproteins, might contribute to FFA-mediated signaling in the brain, we created neuron-specific LPL-deficient mice. Triglycerides 100-112 lipoprotein lipase Mus musculus 39-42 21980507-7 2011 Liver triglyceride content in LPL+/+ LPL-/- mice was also significantly increased, compared with LPL-/- LPL-/- mice (6.8+-0.7 vs. 4.6+-0.5 mg/g wet tissue, p<0.05, n = 6). Triglycerides 6-18 lipoprotein lipase Mus musculus 30-33 21980507-7 2011 Liver triglyceride content in LPL+/+ LPL-/- mice was also significantly increased, compared with LPL-/- LPL-/- mice (6.8+-0.7 vs. 4.6+-0.5 mg/g wet tissue, p<0.05, n = 6). Triglycerides 6-18 lipoprotein lipase Mus musculus 37-40 21980507-7 2011 Liver triglyceride content in LPL+/+ LPL-/- mice was also significantly increased, compared with LPL-/- LPL-/- mice (6.8+-0.7 vs. 4.6+-0.5 mg/g wet tissue, p<0.05, n = 6). Triglycerides 6-18 lipoprotein lipase Mus musculus 37-40 21980507-7 2011 Liver triglyceride content in LPL+/+ LPL-/- mice was also significantly increased, compared with LPL-/- LPL-/- mice (6.8+-0.7 vs. 4.6+-0.5 mg/g wet tissue, p<0.05, n = 6). Triglycerides 6-18 lipoprotein lipase Mus musculus 37-40 21980507-9 2011 CONCLUSIONS: Hematopoietic cell-derived LPL could efficiently ameliorate severe hypertriglyceridemia and hypo-alpha-cholesterolemia at the compensation of increased triglyceride content of liver in LPL-/- mice. Triglycerides 85-97 lipoprotein lipase Mus musculus 40-43 19318514-2 2009 LPL is the rate-limiting enzyme for the hydrolysis of the triglyceride (TG) core of circulating TG-rich lipoproteins, chylomicrons, and very low-density lipoproteins (VLDL). Triglycerides 58-70 lipoprotein lipase Mus musculus 0-3 20927337-4 2010 Angiopoietin-like 4 (ANGPTL4) is a circulating lipoprotein lipase (LPL) inhibitor that controls triglyceride deposition into adipocytes and has been reported to be regulated by gut microbes. Triglycerides 96-108 lipoprotein lipase Mus musculus 47-65 20927337-4 2010 Angiopoietin-like 4 (ANGPTL4) is a circulating lipoprotein lipase (LPL) inhibitor that controls triglyceride deposition into adipocytes and has been reported to be regulated by gut microbes. Triglycerides 96-108 lipoprotein lipase Mus musculus 67-70 20927337-8 2010 This increase, together with total body fat and triglyceride levels told a story of inhibited LPL action through ANGPTL4 leading to decreased fat storage. Triglycerides 48-60 lipoprotein lipase Mus musculus 94-97 20501652-9 2010 We conclude that fenofibrate decreases plasma TG by enhancing LPL-mediated VLDL-TG clearance, which results in a compensatory increase in VLDL-TG production by the liver. Triglycerides 46-48 lipoprotein lipase Mus musculus 62-65 20501652-9 2010 We conclude that fenofibrate decreases plasma TG by enhancing LPL-mediated VLDL-TG clearance, which results in a compensatory increase in VLDL-TG production by the liver. Triglycerides 80-82 lipoprotein lipase Mus musculus 62-65 20501652-9 2010 We conclude that fenofibrate decreases plasma TG by enhancing LPL-mediated VLDL-TG clearance, which results in a compensatory increase in VLDL-TG production by the liver. Triglycerides 80-82 lipoprotein lipase Mus musculus 62-65 20117784-1 2010 Peripheral lipoprotein lipase (LPL)-mediated lipolysis of triglycerides is the first step in chylomicron/VLDL clearance involving heparan sulfate proteoglycans (HSPGs) displayed at the cell surface of the capillaries in adipose tissue, heart and skeletal muscle. Triglycerides 58-71 lipoprotein lipase Mus musculus 31-34 20043872-1 2010 The acute phase response is characterized by elevations in serum triglyceride levels due to both an increase in hepatic VLDL production and a delay in the clearance of triglyceride rich lipoproteins secondary to a decrease in lipoprotein lipase (LPL) activity. Triglycerides 65-77 lipoprotein lipase Mus musculus 246-249 19544529-2 2009 We have reported that induction of LPL expression reduces serum lipid, especially TG, improves fatty change of the liver and inhibits intestinal polyp formation in the mice. Triglycerides 82-84 lipoprotein lipase Mus musculus 35-38 20889497-1 2010 Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1), a GPI-anchored endothelial cell protein, binds lipoprotein lipase (LPL) and transports it into the lumen of capillaries where it hydrolyzes triglycerides in lipoproteins. Triglycerides 232-245 lipoprotein lipase Mus musculus 139-157 19540497-1 2009 OBJECTIVE: Angiopoietin-like protein 3, a liver-derived plasma protein, increases plasma triglycerides (TG) in mice by suppressing the activity of lipoprotein lipase, a key enzyme in plasma TG clearance. Triglycerides 89-102 lipoprotein lipase Mus musculus 147-165 19540497-1 2009 OBJECTIVE: Angiopoietin-like protein 3, a liver-derived plasma protein, increases plasma triglycerides (TG) in mice by suppressing the activity of lipoprotein lipase, a key enzyme in plasma TG clearance. Triglycerides 190-192 lipoprotein lipase Mus musculus 147-165 19318514-2 2009 LPL is the rate-limiting enzyme for the hydrolysis of the triglyceride (TG) core of circulating TG-rich lipoproteins, chylomicrons, and very low-density lipoproteins (VLDL). Triglycerides 72-74 lipoprotein lipase Mus musculus 0-3 19318514-3 2009 LPL-catalyzed reaction products, fatty acids, and monoacylglycerol are in part taken up by the tissues locally and processed differentially; e.g., they are stored as neutral lipids in adipose tissue, oxidized, or stored in skeletal and cardiac muscle or as cholesteryl ester and TG in macrophages. Triglycerides 279-281 lipoprotein lipase Mus musculus 0-3 19318514-7 2009 Mice with overexpression of LPL in skeletal muscle accumulate TG in muscle, develop insulin resistance, are protected from excessive weight gain, and increase their metabolic rate in the cold. Triglycerides 62-64 lipoprotein lipase Mus musculus 28-31 18827440-9 2008 Since Lpl is the primary enzyme responsible for hydrolysis of lipids in lipoproteins, the serum triglyceride levels were determined. Triglycerides 96-108 lipoprotein lipase Mus musculus 6-9 19542565-1 2009 Glycosylphosphatidylinositol-anchored HDL-binding protein (GPIHBP1) binds both LPL and chylomicrons, suggesting that GPIHBP1 is a platform for LPL-dependent processing of triglyceride (TG)-rich lipoproteins. Triglycerides 171-183 lipoprotein lipase Mus musculus 79-82 19542565-1 2009 Glycosylphosphatidylinositol-anchored HDL-binding protein (GPIHBP1) binds both LPL and chylomicrons, suggesting that GPIHBP1 is a platform for LPL-dependent processing of triglyceride (TG)-rich lipoproteins. Triglycerides 171-183 lipoprotein lipase Mus musculus 143-146 19542565-1 2009 Glycosylphosphatidylinositol-anchored HDL-binding protein (GPIHBP1) binds both LPL and chylomicrons, suggesting that GPIHBP1 is a platform for LPL-dependent processing of triglyceride (TG)-rich lipoproteins. Triglycerides 185-187 lipoprotein lipase Mus musculus 79-82 19542565-1 2009 Glycosylphosphatidylinositol-anchored HDL-binding protein (GPIHBP1) binds both LPL and chylomicrons, suggesting that GPIHBP1 is a platform for LPL-dependent processing of triglyceride (TG)-rich lipoproteins. Triglycerides 185-187 lipoprotein lipase Mus musculus 143-146 19318355-1 2009 Angiopoietin-like 3 (ANGPTL3) and angiopoietin-like 4 (ANGPTL4) are secreted proteins that regulate triglyceride (TG) metabolism in part by inhibiting lipoprotein lipase (LPL). Triglycerides 100-112 lipoprotein lipase Mus musculus 151-169 19318355-1 2009 Angiopoietin-like 3 (ANGPTL3) and angiopoietin-like 4 (ANGPTL4) are secreted proteins that regulate triglyceride (TG) metabolism in part by inhibiting lipoprotein lipase (LPL). Triglycerides 100-112 lipoprotein lipase Mus musculus 171-174 19318355-1 2009 Angiopoietin-like 3 (ANGPTL3) and angiopoietin-like 4 (ANGPTL4) are secreted proteins that regulate triglyceride (TG) metabolism in part by inhibiting lipoprotein lipase (LPL). Triglycerides 114-116 lipoprotein lipase Mus musculus 151-169 19318355-1 2009 Angiopoietin-like 3 (ANGPTL3) and angiopoietin-like 4 (ANGPTL4) are secreted proteins that regulate triglyceride (TG) metabolism in part by inhibiting lipoprotein lipase (LPL). Triglycerides 114-116 lipoprotein lipase Mus musculus 171-174 18827440-10 2008 Indeed, the serum triglyceride levels in Ahr KO mice was lower than that in wild-type mice in accordance with the Lpl mRNA levels. Triglycerides 18-30 lipoprotein lipase Mus musculus 114-117 17609525-8 2007 To investigate the LPL-mediated TG clearance, mice were injected intravenously with glycerol tri[(3)H]oleate-labeled VLDL-like emulsion particles. Triglycerides 32-34 lipoprotein lipase Mus musculus 19-22 18767813-7 2008 Formation of apoCIII-containing HDL prevents excess accumulation of plasma apoCIII on VLDL and allows for the efficient lipolysis of VLDL triglycerides by LpL. Triglycerides 138-151 lipoprotein lipase Mus musculus 155-158 18647880-1 2008 Fatty acids (FAs) are acquired from free FA associated with albumin and lipoprotein triglyceride that is hydrolyzed by lipoprotein lipase (LpL). Triglycerides 84-96 lipoprotein lipase Mus musculus 119-137 18647880-1 2008 Fatty acids (FAs) are acquired from free FA associated with albumin and lipoprotein triglyceride that is hydrolyzed by lipoprotein lipase (LpL). Triglycerides 84-96 lipoprotein lipase Mus musculus 139-142 18367731-3 2008 Administration of an adenovirus expressing LPL (AdLPL) into lrp(-)ldlr(-/-)vldlr(-/-) mice reduced both VLDL-triglyceride (TG) and VLDL-total cholesterol (TC) levels. Triglycerides 109-121 lipoprotein lipase Mus musculus 43-46 18263930-2 2008 Because excess apoE2 inhibits LPL-mediated triglyceride (TG) hydrolysis in vitro, we investigated whether direct or indirect stimulation of LPL activity in vivo reduces the apoE2-associated hypertriglyceridemia. Triglycerides 43-55 lipoprotein lipase Mus musculus 30-33 18263930-2 2008 Because excess apoE2 inhibits LPL-mediated triglyceride (TG) hydrolysis in vitro, we investigated whether direct or indirect stimulation of LPL activity in vivo reduces the apoE2-associated hypertriglyceridemia. Triglycerides 57-59 lipoprotein lipase Mus musculus 30-33 18263930-5 2008 Adenovirus-mediated overexpression of LPL reduced plasma TG by 85% and TC by 40%. Triglycerides 57-59 lipoprotein lipase Mus musculus 38-41 18258607-3 2008 In these mice, messenger RNA (mRNA) expression of lipoprotein lipase, which catalyzes hydrolysis of TG, is downregulated. Triglycerides 100-102 lipoprotein lipase Mus musculus 50-68 18175800-1 2008 LPL is an enzyme involved in the breakdown and uptake of lipoprotein triglycerides. Triglycerides 69-82 lipoprotein lipase Mus musculus 0-3 18258818-2 2008 To investigate whether increased endothelial cell expression of lipoprotein lipase (LpL), the primary enzyme creating free fatty acids from circulating triglycerides (TG), affects vascular function, we created transgenic mice that express human LpL (hLpL) driven by the promoter and enhancer of the Tie2 receptor. Triglycerides 152-165 lipoprotein lipase Mus musculus 84-87 18258818-2 2008 To investigate whether increased endothelial cell expression of lipoprotein lipase (LpL), the primary enzyme creating free fatty acids from circulating triglycerides (TG), affects vascular function, we created transgenic mice that express human LpL (hLpL) driven by the promoter and enhancer of the Tie2 receptor. Triglycerides 167-169 lipoprotein lipase Mus musculus 64-82 18258818-2 2008 To investigate whether increased endothelial cell expression of lipoprotein lipase (LpL), the primary enzyme creating free fatty acids from circulating triglycerides (TG), affects vascular function, we created transgenic mice that express human LpL (hLpL) driven by the promoter and enhancer of the Tie2 receptor. Triglycerides 167-169 lipoprotein lipase Mus musculus 84-87 18367009-1 2007 Under normal circumstances, most energy substrate used for heart contraction derives from fatty acids in the form of nonesterified fatty acids bound to albumin or fatty acids derived from lipolysis of lipoprotein-bound triglyceride by lipoprotein lipase (LpL). Triglycerides 219-231 lipoprotein lipase Mus musculus 235-253 18367009-1 2007 Under normal circumstances, most energy substrate used for heart contraction derives from fatty acids in the form of nonesterified fatty acids bound to albumin or fatty acids derived from lipolysis of lipoprotein-bound triglyceride by lipoprotein lipase (LpL). Triglycerides 219-231 lipoprotein lipase Mus musculus 255-258 17761937-6 2007 In fasted but not fed state, Angptl4 overexpression severely impaired LPL-dependent plasma TG and cholesteryl ester clearance and subsequent uptake of fatty acids and cholesterol into tissues. Triglycerides 91-93 lipoprotein lipase Mus musculus 70-73 17087965-10 2007 CONCLUSIONS: The data show that transgenic hLPL(S447X) on top of endogenous murine LPL reduces fasting TG levels in plasma but has no effect on atherosclerosis in LDLr-/- mice. Triglycerides 103-105 lipoprotein lipase Mus musculus 44-47 17403372-1 2007 The triglycerides in chylomicrons are hydrolyzed by lipoprotein lipase (LpL) along the luminal surface of the capillaries. Triglycerides 4-17 lipoprotein lipase Mus musculus 52-70 17620854-2 2007 RECENT FINDINGS: Lipoprotein lipase hydrolyses triglycerides in chylomicrons at the luminal surface of the capillaries in heart, adipose tissue, and skeletal muscle. Triglycerides 47-60 lipoprotein lipase Mus musculus 17-35 17277355-8 2007 In conclusion, reduced plasma TG levels, after oral or intravenous DAG, result from more efficient clearance of DAG by both LPL lipolysis and apoE-mediated hepatic endocytosis. Triglycerides 30-32 lipoprotein lipase Mus musculus 124-127 17403372-1 2007 The triglycerides in chylomicrons are hydrolyzed by lipoprotein lipase (LpL) along the luminal surface of the capillaries. Triglycerides 4-17 lipoprotein lipase Mus musculus 72-75 16684851-5 2006 One week after tamoxifen was completed, triglyceride was increased with LPL deletion, 162 +/- 53 vs. 91 +/- 21 mg/dl, P < 0.01. Triglycerides 40-52 lipoprotein lipase Mus musculus 72-75 17018885-1 2007 LPL and its specific physiological activator, apolipoprotein C-II (apoC-II), regulate the hydrolysis of triglycerides (TGs) from circulating TG-rich lipoproteins. Triglycerides 104-117 lipoprotein lipase Mus musculus 0-3 17018885-1 2007 LPL and its specific physiological activator, apolipoprotein C-II (apoC-II), regulate the hydrolysis of triglycerides (TGs) from circulating TG-rich lipoproteins. Triglycerides 119-122 lipoprotein lipase Mus musculus 0-3 17018885-2 2007 Previously, we developed a skeletal muscle-specific LPL transgenic mouse that had lower plasma TG levels. Triglycerides 95-97 lipoprotein lipase Mus musculus 52-55 17018885-6 2007 Compared with CII mice, apoC-II transgenic mice with the higher level of LPL overexpression (CIILPL-H) had a 50% reduction in plasma TG levels (P = 0.013). Triglycerides 133-135 lipoprotein lipase Mus musculus 73-76 17189607-3 2007 One possible pathway is mediated by LPL, an enzyme that primarily hydrolyzes plasma triglyceride into fatty acids. Triglycerides 84-96 lipoprotein lipase Mus musculus 36-39 16894240-1 2006 Acyl-coenzyme A:diacylglycerol transferase (DGAT), fatty acid synthetase (FAS), and LPL are three enzymes important in adipose tissue triglyceride accumulation. Triglycerides 134-146 lipoprotein lipase Mus musculus 84-87 16990047-2 2006 The current study addresses whether AAV1-LPL(S447X) can reduce elevated triglyceride (TG) levels in mice with attenuated clearance of TG-rich remnant particles. Triglycerides 72-84 lipoprotein lipase Mus musculus 41-44 16990047-2 2006 The current study addresses whether AAV1-LPL(S447X) can reduce elevated triglyceride (TG) levels in mice with attenuated clearance of TG-rich remnant particles. Triglycerides 86-88 lipoprotein lipase Mus musculus 41-44 16990047-5 2006 RESULTS: In the mice that received LPL gene therapy, a marked increase of post-heparin hLPL protein levels (averaging 517+/-277 ng/mL vs. 4+/-3 ng/mL in apoE2KI-untreated) induced 20% reductions of fasting plasma TG levels (p<0.05). Triglycerides 213-215 lipoprotein lipase Mus musculus 35-38 16990047-8 2006 CONCLUSIONS: IM application of AAV1-LPL(S447X) is effective in reducing TG levels in a mouse model for type III dyslipidemia. Triglycerides 72-74 lipoprotein lipase Mus musculus 36-39 16537411-7 2006 There is also a unexpected further reduction of the plasma triglyceride levels that is associated with increased levels of lipoprotein lipase in the Rad tg mice. Triglycerides 59-71 lipoprotein lipase Mus musculus 123-141 17046550-1 2006 Skeletal muscle lipoprotein lipase (LPL) overexpression in mice results in whole-body insulin resistance and increased intramuscular triglyceride stores, but decreased plasma triglyceride concentration and unchanged plasma free fatty acid (FFA) concentration. Triglycerides 133-145 lipoprotein lipase Mus musculus 36-39 17046550-1 2006 Skeletal muscle lipoprotein lipase (LPL) overexpression in mice results in whole-body insulin resistance and increased intramuscular triglyceride stores, but decreased plasma triglyceride concentration and unchanged plasma free fatty acid (FFA) concentration. Triglycerides 175-187 lipoprotein lipase Mus musculus 36-39 16941273-2 2006 In addition to the hydrolyzing activity of triglycerides, LPL modulates various cellular functions via its binding ability to the cell surface. Triglycerides 43-56 lipoprotein lipase Mus musculus 58-61 16684851-7 2006 Four weeks after tamoxifen, MCM/Lpl(flox/flox) mice had triglyceride levels of 190 +/- 27 mg/dl, similar to those of mice with prenatal LPL deletion. Triglycerides 56-68 lipoprotein lipase Mus musculus 32-35 16226489-9 2005 Further, fenofibrate-treated mice presented decreased in vivo [3H]VLDL catabolism and decreased VLDL-triglyceride hydrolysis by exogenous LPL. Triglycerides 101-113 lipoprotein lipase Mus musculus 138-141 16478678-1 2006 We have recently shown that the predominant hypertriglyceridemia in human apolipoprotein C1 (APOC1) transgenic mice is mainly explained by apoCI-mediated inhibition of the lipoprotein lipase (LPL)-dependent triglyceride (TG)-hydrolysis pathway. Triglycerides 49-61 lipoprotein lipase Mus musculus 172-190 16478678-1 2006 We have recently shown that the predominant hypertriglyceridemia in human apolipoprotein C1 (APOC1) transgenic mice is mainly explained by apoCI-mediated inhibition of the lipoprotein lipase (LPL)-dependent triglyceride (TG)-hydrolysis pathway. Triglycerides 49-61 lipoprotein lipase Mus musculus 192-195 16478678-1 2006 We have recently shown that the predominant hypertriglyceridemia in human apolipoprotein C1 (APOC1) transgenic mice is mainly explained by apoCI-mediated inhibition of the lipoprotein lipase (LPL)-dependent triglyceride (TG)-hydrolysis pathway. Triglycerides 221-223 lipoprotein lipase Mus musculus 192-195 15774484-4 2005 In human APOA5 transgenic mice (hAPOA5tr), catabolism of chylomicrons and very low density lipoprotein (VLDL) was accelerated due to a faster plasma hydrolysis of triglycerides by lipoprotein lipase (LPL). Triglycerides 163-176 lipoprotein lipase Mus musculus 180-198 16002740-1 2005 The naturally occurring human lipoprotein lipase S447X variant (LPLS447X) exemplifies a gain-of function mutation with significant benefits including decreased plasma triglycerides (TG), increased high-density lipoprotein (HDL) cholesterol, and reduced risk of coronary artery disease. Triglycerides 167-180 lipoprotein lipase Mus musculus 30-48 16002740-1 2005 The naturally occurring human lipoprotein lipase S447X variant (LPLS447X) exemplifies a gain-of function mutation with significant benefits including decreased plasma triglycerides (TG), increased high-density lipoprotein (HDL) cholesterol, and reduced risk of coronary artery disease. Triglycerides 182-184 lipoprotein lipase Mus musculus 30-48 16024917-10 2005 We conclude that the increased plasma TG levels observed in cd36(-)(/)(-) mice are caused by decreased LPL-mediated hydrolysis of TG-rich lipoproteins resulting from FFA-induced product inhibition of LPL. Triglycerides 38-40 lipoprotein lipase Mus musculus 103-106 16024917-10 2005 We conclude that the increased plasma TG levels observed in cd36(-)(/)(-) mice are caused by decreased LPL-mediated hydrolysis of TG-rich lipoproteins resulting from FFA-induced product inhibition of LPL. Triglycerides 38-40 lipoprotein lipase Mus musculus 200-203 16081640-1 2005 Lipoprotein lipase (LPL) is a key regulator of triglyceride clearance. Triglycerides 47-59 lipoprotein lipase Mus musculus 0-18 16081640-1 2005 Lipoprotein lipase (LPL) is a key regulator of triglyceride clearance. Triglycerides 47-59 lipoprotein lipase Mus musculus 20-23 16081640-3 2005 Angiopoietin-like (Angptl)3 and Angptl4 are secreted proteins that have been demonstrated to regulate triglyceride metabolism by inhibiting LPL. Triglycerides 102-114 lipoprotein lipase Mus musculus 140-143 15995182-3 2005 The TG production rate is determined by measuring temporal increases in plasma TG under conditions in which TG hydrolysis by lipoprotein lipase (LPL) is inhibited. Triglycerides 4-6 lipoprotein lipase Mus musculus 125-143 15995182-3 2005 The TG production rate is determined by measuring temporal increases in plasma TG under conditions in which TG hydrolysis by lipoprotein lipase (LPL) is inhibited. Triglycerides 4-6 lipoprotein lipase Mus musculus 145-148 15774484-4 2005 In human APOA5 transgenic mice (hAPOA5tr), catabolism of chylomicrons and very low density lipoprotein (VLDL) was accelerated due to a faster plasma hydrolysis of triglycerides by lipoprotein lipase (LPL). Triglycerides 163-176 lipoprotein lipase Mus musculus 200-203 15774484-7 2005 Increased LPL activity completely normalized hypertriglyceridemia of apoa5-deficient mice; however, overexpression of human apoAV modulated triglyceride levels only slightly when LPL was reduced. Triglycerides 50-62 lipoprotein lipase Mus musculus 10-13 15630456-1 2005 Lipoprotein lipase (LPL) is thought to be the only enzyme responsible for the catabolism of triglycerides (TGs) associated with TG-rich lipoproteins in adipose tissue (AT). Triglycerides 92-105 lipoprotein lipase Mus musculus 0-18 15630456-1 2005 Lipoprotein lipase (LPL) is thought to be the only enzyme responsible for the catabolism of triglycerides (TGs) associated with TG-rich lipoproteins in adipose tissue (AT). Triglycerides 92-105 lipoprotein lipase Mus musculus 20-23 15630456-1 2005 Lipoprotein lipase (LPL) is thought to be the only enzyme responsible for the catabolism of triglycerides (TGs) associated with TG-rich lipoproteins in adipose tissue (AT). Triglycerides 107-110 lipoprotein lipase Mus musculus 0-18 15630456-1 2005 Lipoprotein lipase (LPL) is thought to be the only enzyme responsible for the catabolism of triglycerides (TGs) associated with TG-rich lipoproteins in adipose tissue (AT). Triglycerides 107-110 lipoprotein lipase Mus musculus 20-23 15353045-6 2004 At 8 months after administration of AAV1-LPL(S447X), an intravenous lipid challenge showed efficient, near-normal clearance of plasma TG. Triglycerides 134-136 lipoprotein lipase Mus musculus 41-44 15576844-6 2005 Although total postheparin plasma LPL activity was not lower in APOC1 mice compared with controls, apoC-I was able to dose-dependently inhibit the LPL-mediated lipolysis of [3H]TG-VLDL-mimicking particles in vitro with a 60% efficiency compared with the main endogenous LPL inhibitor apoC-III. Triglycerides 177-179 lipoprotein lipase Mus musculus 147-150 15576844-6 2005 Although total postheparin plasma LPL activity was not lower in APOC1 mice compared with controls, apoC-I was able to dose-dependently inhibit the LPL-mediated lipolysis of [3H]TG-VLDL-mimicking particles in vitro with a 60% efficiency compared with the main endogenous LPL inhibitor apoC-III. Triglycerides 177-179 lipoprotein lipase Mus musculus 147-150 15576844-8 2005 Therefore, we conclude that apoC-I is a potent inhibitor of LPL-mediated TG-lipolysis. Triglycerides 73-75 lipoprotein lipase Mus musculus 60-63 15145981-0 2004 The VLDL receptor plays a major role in chylomicron metabolism by enhancing LPL-mediated triglyceride hydrolysis. Triglycerides 89-101 lipoprotein lipase Mus musculus 76-79 15145981-1 2004 The VLDL receptor (VLDLr) is involved in tissue delivery of VLDL-triglyceride (TG)-derived FFA by facilitating the expression of lipoprotein lipase (LPL). Triglycerides 65-77 lipoprotein lipase Mus musculus 129-147 15145981-1 2004 The VLDL receptor (VLDLr) is involved in tissue delivery of VLDL-triglyceride (TG)-derived FFA by facilitating the expression of lipoprotein lipase (LPL). Triglycerides 65-77 lipoprotein lipase Mus musculus 149-152 15056458-1 2004 Lipoprotein lipase (LPL) is a member of a lipase family known to hydrolyze triglyceride molecules found in lipoprotein particles. Triglycerides 75-87 lipoprotein lipase Mus musculus 0-18 15178420-3 2004 Initially we found that triglyceride turnover was faster in hAPOA5 transgenic mice compared to controls, and this strongly correlated with increased LPL activity in postheparin plasma. Triglycerides 24-36 lipoprotein lipase Mus musculus 149-152 15178420-11 2004 This shift of apoAV in VLDL appears to limit the increase of triglyceride by activating the lipoprotein lipase. Triglycerides 61-73 lipoprotein lipase Mus musculus 92-110 15028738-0 2004 Cardiac-specific knock-out of lipoprotein lipase alters plasma lipoprotein triglyceride metabolism and cardiac gene expression. Triglycerides 75-87 lipoprotein lipase Mus musculus 30-48 15028738-2 2004 The heart acquires fatty acids associated with albumin or derived from lipoprotein lipase (LpL)-mediated hydrolysis of lipoprotein triglyceride (TG). Triglycerides 131-143 lipoprotein lipase Mus musculus 71-89 15028738-2 2004 The heart acquires fatty acids associated with albumin or derived from lipoprotein lipase (LpL)-mediated hydrolysis of lipoprotein triglyceride (TG). Triglycerides 131-143 lipoprotein lipase Mus musculus 91-94 15028738-2 2004 The heart acquires fatty acids associated with albumin or derived from lipoprotein lipase (LpL)-mediated hydrolysis of lipoprotein triglyceride (TG). Triglycerides 145-147 lipoprotein lipase Mus musculus 71-89 15028738-2 2004 The heart acquires fatty acids associated with albumin or derived from lipoprotein lipase (LpL)-mediated hydrolysis of lipoprotein triglyceride (TG). Triglycerides 145-147 lipoprotein lipase Mus musculus 91-94 15028738-4 2004 Male hLpL0 mice had significantly elevated plasma TG levels and decreased clearance of postprandial lipids despite normal postheparin plasma LpL activity. Triglycerides 50-52 lipoprotein lipase Mus musculus 6-9 15056458-1 2004 Lipoprotein lipase (LPL) is a member of a lipase family known to hydrolyze triglyceride molecules found in lipoprotein particles. Triglycerides 75-87 lipoprotein lipase Mus musculus 20-23 14570890-1 2004 Lipoprotein lipase (LpL) hydrolyzes triglycerides of circulating lipoproteins while bound as homodimers to endothelial cell surface heparan sulfate proteoglycans. Triglycerides 36-49 lipoprotein lipase Mus musculus 0-18 15001574-8 2004 Together, these results indicate a clear role for PPARbeta in regulating levels of serum triglycerides in mice on a high fat Western diet by modulating both VLDL production and LPL-mediated catabolism of VLDL-triglycerides and also suggest a potential therapeutic role for PPARbeta in the improvement of serum lipids in the setting of metabolic syndrome. Triglycerides 89-102 lipoprotein lipase Mus musculus 177-180 15001574-8 2004 Together, these results indicate a clear role for PPARbeta in regulating levels of serum triglycerides in mice on a high fat Western diet by modulating both VLDL production and LPL-mediated catabolism of VLDL-triglycerides and also suggest a potential therapeutic role for PPARbeta in the improvement of serum lipids in the setting of metabolic syndrome. Triglycerides 209-222 lipoprotein lipase Mus musculus 177-180 14594997-1 2004 Lipoprotein lipase (LPL) is the only known enzyme in the capillary endothelium of peripheral tissues that hydrolizes plasma triglycerides and provides fatty acids (FAs) for their subsequent tissue uptake. Triglycerides 124-137 lipoprotein lipase Mus musculus 0-18 14594997-1 2004 Lipoprotein lipase (LPL) is the only known enzyme in the capillary endothelium of peripheral tissues that hydrolizes plasma triglycerides and provides fatty acids (FAs) for their subsequent tissue uptake. Triglycerides 124-137 lipoprotein lipase Mus musculus 20-23 14570890-1 2004 Lipoprotein lipase (LpL) hydrolyzes triglycerides of circulating lipoproteins while bound as homodimers to endothelial cell surface heparan sulfate proteoglycans. Triglycerides 36-49 lipoprotein lipase Mus musculus 20-23 15356379-4 2004 It is likely that VLDL receptor functions in concert with lipoprotein lipase (LPL), which hydrolyses TG in VLDL and chylomicron. Triglycerides 101-103 lipoprotein lipase Mus musculus 58-76 15356379-4 2004 It is likely that VLDL receptor functions in concert with lipoprotein lipase (LPL), which hydrolyses TG in VLDL and chylomicron. Triglycerides 101-103 lipoprotein lipase Mus musculus 78-81 12586369-1 2003 Lipoprotein lipase (LPL) plays a role in lipid usage in skeletal muscle by hydrolyzing plasma triglycerides into fatty acids, which are further utilized for beta-oxidation. Triglycerides 94-107 lipoprotein lipase Mus musculus 0-18 14685668-1 2003 BACKGROUND: Lipoprotein lipase (LPL) is the central enzyme in plasma triglyceride hydrolysis. Triglycerides 69-81 lipoprotein lipase Mus musculus 12-30 14685668-1 2003 BACKGROUND: Lipoprotein lipase (LPL) is the central enzyme in plasma triglyceride hydrolysis. Triglycerides 69-81 lipoprotein lipase Mus musculus 32-35 12870663-3 2003 Lipoprotein lipase (LPL) modulates the binding of triglyceride (TG)-rich lipoprotein particles to the VLDL receptor. Triglycerides 50-62 lipoprotein lipase Mus musculus 0-18 12870663-3 2003 Lipoprotein lipase (LPL) modulates the binding of triglyceride (TG)-rich lipoprotein particles to the VLDL receptor. Triglycerides 50-62 lipoprotein lipase Mus musculus 20-23 12732191-1 2003 Lipoprotein lipase (LPL), a key enzyme for triglyceride hydrolysis, is an insulin-dependent enzyme and mainly synthesized in white adipose tissue (WAT) and skeletal muscles (SM). Triglycerides 43-55 lipoprotein lipase Mus musculus 0-18 12732191-1 2003 Lipoprotein lipase (LPL), a key enzyme for triglyceride hydrolysis, is an insulin-dependent enzyme and mainly synthesized in white adipose tissue (WAT) and skeletal muscles (SM). Triglycerides 43-55 lipoprotein lipase Mus musculus 20-23 12565906-4 2003 ANGPTL3 inhibited the activity of lipoprotein lipase, which accounted for the increase of plasma triglyceride. Triglycerides 97-109 lipoprotein lipase Mus musculus 34-52 12388125-5 2003 Inhibition of lipoprotein lipase (LPL) with tetrahydrolipstatin or dissociation of LPL from the heart with heparin reduced cardiac uptake of TG by 82 and 64%, respectively (P < 0.01). Triglycerides 141-143 lipoprotein lipase Mus musculus 14-32 12388125-5 2003 Inhibition of lipoprotein lipase (LPL) with tetrahydrolipstatin or dissociation of LPL from the heart with heparin reduced cardiac uptake of TG by 82 and 64%, respectively (P < 0.01). Triglycerides 141-143 lipoprotein lipase Mus musculus 34-37 12388125-5 2003 Inhibition of lipoprotein lipase (LPL) with tetrahydrolipstatin or dissociation of LPL from the heart with heparin reduced cardiac uptake of TG by 82 and 64%, respectively (P < 0.01). Triglycerides 141-143 lipoprotein lipase Mus musculus 83-86 15013626-1 2004 Lipoprotein lipase (LPL) is well known for its role in the catabolism of plasma triglyceride (Tg)-rich lipoproteins, such as very low density lipoproteins (VLDL) and chylomicrons. Triglycerides 80-92 lipoprotein lipase Mus musculus 0-18 15013626-1 2004 Lipoprotein lipase (LPL) is well known for its role in the catabolism of plasma triglyceride (Tg)-rich lipoproteins, such as very low density lipoproteins (VLDL) and chylomicrons. Triglycerides 80-92 lipoprotein lipase Mus musculus 20-23 12671033-2 2003 Recently, we proposed that Angptl3 is a new class of lipid metabolism modulator regulating VLDL triglyceride (TG) levels through the inhibition of lipoprotein lipase (LPL) activity. Triglycerides 96-108 lipoprotein lipase Mus musculus 147-165 12671033-2 2003 Recently, we proposed that Angptl3 is a new class of lipid metabolism modulator regulating VLDL triglyceride (TG) levels through the inhibition of lipoprotein lipase (LPL) activity. Triglycerides 96-108 lipoprotein lipase Mus musculus 167-170 12671033-2 2003 Recently, we proposed that Angptl3 is a new class of lipid metabolism modulator regulating VLDL triglyceride (TG) levels through the inhibition of lipoprotein lipase (LPL) activity. Triglycerides 110-112 lipoprotein lipase Mus musculus 147-165 12671033-2 2003 Recently, we proposed that Angptl3 is a new class of lipid metabolism modulator regulating VLDL triglyceride (TG) levels through the inhibition of lipoprotein lipase (LPL) activity. Triglycerides 110-112 lipoprotein lipase Mus musculus 167-170 12586369-1 2003 Lipoprotein lipase (LPL) plays a role in lipid usage in skeletal muscle by hydrolyzing plasma triglycerides into fatty acids, which are further utilized for beta-oxidation. Triglycerides 94-107 lipoprotein lipase Mus musculus 20-23 11863451-11 2002 Removal of chylomicron-sized n-6 TG emulsions is modulated by lipoprotein lipase (LPL), apoE, LDL-R, and lactoferrin-sensitive pathways. Triglycerides 33-35 lipoprotein lipase Mus musculus 62-80 12093671-4 2002 Lipoprotein lipase (LPL), the enzyme responsible for plasma triglyceride (TG) clearance and partitioning among tissues, is under tissue-specific modulation associated with energy balance. Triglycerides 60-72 lipoprotein lipase Mus musculus 20-23 12093671-4 2002 Lipoprotein lipase (LPL), the enzyme responsible for plasma triglyceride (TG) clearance and partitioning among tissues, is under tissue-specific modulation associated with energy balance. Triglycerides 74-76 lipoprotein lipase Mus musculus 20-23 12397026-1 2003 Hydrolysis of triacylglycerols (TG) in circulating chylomicrons by endothelium-bound lipoprotein lipase (LPL) provides a source of fatty acids (FA) for cardiac metabolism. Triglycerides 14-30 lipoprotein lipase Mus musculus 105-108 12397026-1 2003 Hydrolysis of triacylglycerols (TG) in circulating chylomicrons by endothelium-bound lipoprotein lipase (LPL) provides a source of fatty acids (FA) for cardiac metabolism. Triglycerides 32-34 lipoprotein lipase Mus musculus 105-108 12397026-4 2003 The metabolism of LPL-derived FA was examined by perfusing hearts with chylomicrons containing radiolabeled TG and by measuring (3)H(2)O accumulation in the perfusate (oxidation) and incorporation of radioactivity into tissue TG (esterification). Triglycerides 108-110 lipoprotein lipase Mus musculus 18-21 12397026-4 2003 The metabolism of LPL-derived FA was examined by perfusing hearts with chylomicrons containing radiolabeled TG and by measuring (3)H(2)O accumulation in the perfusate (oxidation) and incorporation of radioactivity into tissue TG (esterification). Triglycerides 226-228 lipoprotein lipase Mus musculus 18-21 12569168-1 2003 Lipoprotein lipase is the principal enzyme that hydrolyzes circulating triglycerides and liberates free fatty acids that can be used as energy by cardiac muscle. Triglycerides 71-84 lipoprotein lipase Mus musculus 0-18 12097324-9 2002 These data strongly support the hypothesis that ANGPTL3 is a new class of lipid metabolism modulator, which regulates VLDL triglyceride levels through the inhibition of LPL activity. Triglycerides 123-135 lipoprotein lipase Mus musculus 169-172 12145151-6 2002 Antisense treatment also influenced the triglyceride content in adipocytes, correlating with a downregulation of genes encoding proteins involved in lipogenesis, such as sterol regulatory element-binding protein 1 and their downstream targets spot14 and fatty acid synthase, as well as other adipogenic genes, lipoprotein lipase, and peroxisome proliferator-activated receptor gamma. Triglycerides 40-52 lipoprotein lipase Mus musculus 310-328 11751882-0 2002 Inactive lipoprotein lipase (LPL) alone increases selective cholesterol ester uptake in vivo, whereas in the presence of active LPL it also increases triglyceride hydrolysis and whole particle lipoprotein uptake. Triglycerides 150-162 lipoprotein lipase Mus musculus 9-27 11751882-0 2002 Inactive lipoprotein lipase (LPL) alone increases selective cholesterol ester uptake in vivo, whereas in the presence of active LPL it also increases triglyceride hydrolysis and whole particle lipoprotein uptake. Triglycerides 150-162 lipoprotein lipase Mus musculus 29-32 11751882-0 2002 Inactive lipoprotein lipase (LPL) alone increases selective cholesterol ester uptake in vivo, whereas in the presence of active LPL it also increases triglyceride hydrolysis and whole particle lipoprotein uptake. Triglycerides 150-162 lipoprotein lipase Mus musculus 128-131 11751882-1 2002 We have previously shown that transgenic expression of catalytically inactive lipoprotein lipase (LPL) in muscle (Mck-N-LPL) enhances triglyceride hydrolysis as well as whole particle lipoprotein and selective cholesterol ester uptake. Triglycerides 134-146 lipoprotein lipase Mus musculus 78-96 11751882-1 2002 We have previously shown that transgenic expression of catalytically inactive lipoprotein lipase (LPL) in muscle (Mck-N-LPL) enhances triglyceride hydrolysis as well as whole particle lipoprotein and selective cholesterol ester uptake. Triglycerides 134-146 lipoprotein lipase Mus musculus 98-101 11751882-1 2002 We have previously shown that transgenic expression of catalytically inactive lipoprotein lipase (LPL) in muscle (Mck-N-LPL) enhances triglyceride hydrolysis as well as whole particle lipoprotein and selective cholesterol ester uptake. Triglycerides 134-146 lipoprotein lipase Mus musculus 120-123 11751882-4 2002 At 18 h of age, Mck-N-LPL reduced triglycerides by 35% and markedly increased muscle lipid droplets. Triglycerides 34-47 lipoprotein lipase Mus musculus 22-25 11751882-11 2002 Thus, in the presence of active LPL in the same tissue, inactive LPL augments triglyceride hydrolysis and increases whole particle triglyceride-rich lipoprotein and selective cholesterol ester uptake. Triglycerides 78-90 lipoprotein lipase Mus musculus 65-68 11751882-11 2002 Thus, in the presence of active LPL in the same tissue, inactive LPL augments triglyceride hydrolysis and increases whole particle triglyceride-rich lipoprotein and selective cholesterol ester uptake. Triglycerides 131-143 lipoprotein lipase Mus musculus 65-68 11809748-8 2002 Decreased plasma NEFA and TG levels in fasted HSL-ko mice were associated with increased fractional catabolic rates of VLDL-TG and an induction of the tissue-specific lipoprotein lipase (LPL) activity in cardiac muscle, skeletal muscle, and white AT. Triglycerides 26-28 lipoprotein lipase Mus musculus 167-185 11863451-11 2002 Removal of chylomicron-sized n-6 TG emulsions is modulated by lipoprotein lipase (LPL), apoE, LDL-R, and lactoferrin-sensitive pathways. Triglycerides 33-35 lipoprotein lipase Mus musculus 82-85 11809748-8 2002 Decreased plasma NEFA and TG levels in fasted HSL-ko mice were associated with increased fractional catabolic rates of VLDL-TG and an induction of the tissue-specific lipoprotein lipase (LPL) activity in cardiac muscle, skeletal muscle, and white AT. Triglycerides 26-28 lipoprotein lipase Mus musculus 187-190 11590213-0 2001 Apolipoprotein C-III deficiency accelerates triglyceride hydrolysis by lipoprotein lipase in wild-type and apoE knockout mice. Triglycerides 44-56 lipoprotein lipase Mus musculus 71-89 11787060-6 2002 Furthermore, native, aggregated, acetylated, and moderately macrophage-oxidized low density lipoprotein stimulate the uptake of a triacylglycerol-rich emulsion through several mechanisms such as an actin-dependent pathway, scavenger receptors, and lipolysis mediated by lipoprotein lipase. Triglycerides 130-145 lipoprotein lipase Mus musculus 270-288 11787060-7 2002 On the other hand, in spite of the interaction of low density lipoprotein forms with a triacylglycerol-rich emulsion, the cellular triacylglycerol-rich emulsion uptake is impaired by copper-oxidized low density lipoprotein, possibly due to its diminished affinity towards lipoprotein lipase. Triglycerides 131-146 lipoprotein lipase Mus musculus 272-290 11562371-1 2001 Lipoprotein lipase (LPL) is a key enzyme for lipoprotein metabolism and is responsible for hydrolysis of triglycerides in circulating lipoproteins, releasing free fatty acids to peripheral tissues. Triglycerides 105-118 lipoprotein lipase Mus musculus 0-18 11562371-1 2001 Lipoprotein lipase (LPL) is a key enzyme for lipoprotein metabolism and is responsible for hydrolysis of triglycerides in circulating lipoproteins, releasing free fatty acids to peripheral tissues. Triglycerides 105-118 lipoprotein lipase Mus musculus 20-23 11432868-2 2001 Lipoprotein lipase (LPL) is the rate-limiting enzyme for the hydrolysis of triglycerides and the subsequent uptake of free fatty acids in extrahepatic tissues. Triglycerides 75-88 lipoprotein lipase Mus musculus 0-18 11432868-2 2001 Lipoprotein lipase (LPL) is the rate-limiting enzyme for the hydrolysis of triglycerides and the subsequent uptake of free fatty acids in extrahepatic tissues. Triglycerides 75-88 lipoprotein lipase Mus musculus 20-23 11440913-4 2001 Endothelium-bound LPL hydrolyzed radiolabeled (3)H-labeled chylomicrons (0.4 mM TG); the fate of LPL-derived (3)H-labeled fatty acids was split evenly between oxidation (production of (3)H(2)O) and esterification (incorporation into tissue lipids, mainly TG). Triglycerides 80-82 lipoprotein lipase Mus musculus 18-21 11440913-4 2001 Endothelium-bound LPL hydrolyzed radiolabeled (3)H-labeled chylomicrons (0.4 mM TG); the fate of LPL-derived (3)H-labeled fatty acids was split evenly between oxidation (production of (3)H(2)O) and esterification (incorporation into tissue lipids, mainly TG). Triglycerides 255-257 lipoprotein lipase Mus musculus 18-21 11440913-4 2001 Endothelium-bound LPL hydrolyzed radiolabeled (3)H-labeled chylomicrons (0.4 mM TG); the fate of LPL-derived (3)H-labeled fatty acids was split evenly between oxidation (production of (3)H(2)O) and esterification (incorporation into tissue lipids, mainly TG). Triglycerides 255-257 lipoprotein lipase Mus musculus 97-100 11311126-10 2001 These findings indicated that NEFAs as lipolytic products of LPL-mediated triacylglycerol hydrolysis markedly affect UCP-3 expression and that increased LPL activities occurring during fasting in skeletal muscle contribute to the induction of UCP-3 expression by promoting the increased uptake of NEFAs. Triglycerides 74-89 lipoprotein lipase Mus musculus 61-64 10865833-8 2000 Furthermore, lipoprotein lipase activity was lower than in normal mice, suggesting impaired lipolysis was involved in the increased plasma triglyceride levels under insulin-resistant conditions. Triglycerides 139-151 lipoprotein lipase Mus musculus 13-31 11062730-7 2000 Elevated blood levels of triglyceride and non-esterified fatty acid were observed in mice bearing EL-4, associated with the impaired plasma LPL activity. Triglycerides 25-37 lipoprotein lipase Mus musculus 140-143 10634811-8 2000 These results indicate that oxVLDL induces endogenous TG synthesis predominantly through particle uptake via the scavenger receptor and much less via the extracellular lipoprotein lipase (LPL)-mediated hydrolysis of TG, as is the case for native VLDL. Triglycerides 216-218 lipoprotein lipase Mus musculus 168-186 10744772-5 2000 Reduced LPL in both plasma and vessel wall (LPL(+/-)E(-/-)) was associated with increased TG and increased total cholesterol (TC) compared with LPL(+/+)E(-/-) sibs. Triglycerides 90-92 lipoprotein lipase Mus musculus 8-11 10744772-5 2000 Reduced LPL in both plasma and vessel wall (LPL(+/-)E(-/-)) was associated with increased TG and increased total cholesterol (TC) compared with LPL(+/+)E(-/-) sibs. Triglycerides 90-92 lipoprotein lipase Mus musculus 44-47 10744772-5 2000 Reduced LPL in both plasma and vessel wall (LPL(+/-)E(-/-)) was associated with increased TG and increased total cholesterol (TC) compared with LPL(+/+)E(-/-) sibs. Triglycerides 90-92 lipoprotein lipase Mus musculus 44-47 10744772-8 2000 In contrast, transgenic mice with increased plasma LPL but with no increase in LPL expression in macrophages, and thus the vessel wall, had decreased TG and TC and significantly decreased lesion areas compared with LPL(+/+)E(-/-) mice. Triglycerides 150-152 lipoprotein lipase Mus musculus 51-54 10634811-8 2000 These results indicate that oxVLDL induces endogenous TG synthesis predominantly through particle uptake via the scavenger receptor and much less via the extracellular lipoprotein lipase (LPL)-mediated hydrolysis of TG, as is the case for native VLDL. Triglycerides 216-218 lipoprotein lipase Mus musculus 188-191 10634811-12 2000 Thus, from these studies it can be concluded that on oxidation, VLDL becomes less efficient in inducing TG accumulation in J774 cells as a consequence of a defect in apoC2 as an activator for the LPL-mediated extracellular lipolysis. Triglycerides 104-106 lipoprotein lipase Mus musculus 196-199 10588944-12 1999 LpL overexpression reduced plasma triglyceride, but not cholesterol, in male mice on WTD. Triglycerides 34-46 lipoprotein lipase Mus musculus 0-3 10484615-1 1999 Lipoprotein lipase (LPL) is known to play a crucial role in lipoprotein metabolism by hydrolyzing triglycerides; however its role in atherogenesis has yet to be determined. Triglycerides 98-111 lipoprotein lipase Mus musculus 0-18 10484615-1 1999 Lipoprotein lipase (LPL) is known to play a crucial role in lipoprotein metabolism by hydrolyzing triglycerides; however its role in atherogenesis has yet to be determined. Triglycerides 98-111 lipoprotein lipase Mus musculus 20-23 10484615-4 1999 On a normal chow diet, LPL/APOEKO mice showed marked suppression of the plasma triglyceride levels compared with APOEKO mice (54 vs. 182 mg/dl), but no significant changes in plasma cholesterol and apoB levels. Triglycerides 79-91 lipoprotein lipase Mus musculus 23-26 10484615-5 1999 Non-high density lipoproteins (HDL) from LPL/APOEKO mice had lower triglyceride content, a smaller size, and a more positive charge compared with those from APOEKO mice. Triglycerides 67-79 lipoprotein lipase Mus musculus 41-44 10077655-0 1999 Induced mutant mouse lines that express lipoprotein lipase in cardiac muscle, but not in skeletal muscle and adipose tissue, have normal plasma triglyceride and high-density lipoprotein-cholesterol levels. Triglycerides 144-156 lipoprotein lipase Mus musculus 40-58 10206963-5 1999 However, VLDL-triglyceride hydrolysis by exogenous LPL was considerably slower in transgenic compared with control mice, with the apparent Vmax of the reaction decreasing proportionately to human apoA-II expression. Triglycerides 14-26 lipoprotein lipase Mus musculus 51-54 10077655-1 1999 The tissue-specific expression of lipoprotein lipase (LPL) in adipose tissue (AT), skeletal muscle (SM), and cardiac muscle (CM) is rate-limiting for the uptake of triglyceride (TG)-derived free fatty acids and decisive in the regulation of energy balance and lipoprotein metabolism. Triglycerides 164-176 lipoprotein lipase Mus musculus 34-52 10077655-1 1999 The tissue-specific expression of lipoprotein lipase (LPL) in adipose tissue (AT), skeletal muscle (SM), and cardiac muscle (CM) is rate-limiting for the uptake of triglyceride (TG)-derived free fatty acids and decisive in the regulation of energy balance and lipoprotein metabolism. Triglycerides 164-176 lipoprotein lipase Mus musculus 54-57 10077655-1 1999 The tissue-specific expression of lipoprotein lipase (LPL) in adipose tissue (AT), skeletal muscle (SM), and cardiac muscle (CM) is rate-limiting for the uptake of triglyceride (TG)-derived free fatty acids and decisive in the regulation of energy balance and lipoprotein metabolism. Triglycerides 178-180 lipoprotein lipase Mus musculus 34-52 10077655-1 1999 The tissue-specific expression of lipoprotein lipase (LPL) in adipose tissue (AT), skeletal muscle (SM), and cardiac muscle (CM) is rate-limiting for the uptake of triglyceride (TG)-derived free fatty acids and decisive in the regulation of energy balance and lipoprotein metabolism. Triglycerides 178-180 lipoprotein lipase Mus musculus 54-57 10077655-11 1999 From this genetic model of LPL deficiency in SM and AT, it can be concluded that CM-specific LPL expression is a major determinant in the regulation of plasma TG and HDL-cholesterol levels. Triglycerides 159-161 lipoprotein lipase Mus musculus 27-30 9727057-8 1998 Adult mice expressing LPL exclusively in liver had slower VLDL turnover than wild-type mice, but greater VLDL mass clearance, increased VLDL triglyceride production, and three- to fourfold more plasma ketones. Triglycerides 141-153 lipoprotein lipase Mus musculus 22-25 9892249-1 1999 The present study was conducted to determine if direct injections of plasmid pMCKhLPL DNA would lead to sufficient overexpression of lipoprotein lipase (LPL) to reduce plasma triglycerides in mice. Triglycerides 175-188 lipoprotein lipase Mus musculus 133-151 9892249-1 1999 The present study was conducted to determine if direct injections of plasmid pMCKhLPL DNA would lead to sufficient overexpression of lipoprotein lipase (LPL) to reduce plasma triglycerides in mice. Triglycerides 175-188 lipoprotein lipase Mus musculus 82-85 9811888-1 1998 Lipoprotein lipase (LPL) is the central enzyme in plasma triglyceride hydrolysis. Triglycerides 57-69 lipoprotein lipase Mus musculus 0-18 9811888-1 1998 Lipoprotein lipase (LPL) is the central enzyme in plasma triglyceride hydrolysis. Triglycerides 57-69 lipoprotein lipase Mus musculus 20-23 9811888-8 1998 On the heterozygote LPL knock-out background (LPL1) background, plasma triglyceride levels were lowered 22 and 33% in the two transgenic lines. Triglycerides 71-83 lipoprotein lipase Mus musculus 20-23 9727057-9 1998 In summary, it appears that liver LPL shunts circulating triglycerides to the liver, which results in a futile cycle of enhanced VLDL production and increased ketone production, and subsequently spares glucose. Triglycerides 57-70 lipoprotein lipase Mus musculus 34-37 9414485-1 1998 Lipoprotein lipase (LPL) is important in the process of triglyceride storage in adipose tissue. Triglycerides 56-68 lipoprotein lipase Mus musculus 0-18 9741698-7 1998 However, when the amount of apoE-deficient VLDL/CMR was reduced to an equivalent level as in wild-type mice, LPL hydrolyzed 94% of VLDL/CMR triglycerides. Triglycerides 140-153 lipoprotein lipase Mus musculus 109-112 9800066-1 1998 The authors previously demonstrated that the gene for human lipoprotein lipase (hLPL), an enzyme crucial to the breakdown of triglyceride (TG)-rich dietary fats, corrects the hypertriglyceridemia in lipoprotein lipase (LPL)-deficient knockout mice after adenoviral (Ad)-mediated LPL gene transfer. Triglycerides 125-137 lipoprotein lipase Mus musculus 219-222 9800066-1 1998 The authors previously demonstrated that the gene for human lipoprotein lipase (hLPL), an enzyme crucial to the breakdown of triglyceride (TG)-rich dietary fats, corrects the hypertriglyceridemia in lipoprotein lipase (LPL)-deficient knockout mice after adenoviral (Ad)-mediated LPL gene transfer. Triglycerides 139-141 lipoprotein lipase Mus musculus 219-222 9800066-11 1998 Therefore, Ad-mediated overexpression of hepatic LPL was found to significantly decrease plasma TG levels unrelated to primary LPL deficiency. Triglycerides 96-98 lipoprotein lipase Mus musculus 49-52 9541510-5 1998 Furthermore, lipoprotein lipase activity was lower than in normal mice, suggesting impaired lipolysis to be involved in the increase in plasma triglyceride levels under insulin-resistant conditions. Triglycerides 143-155 lipoprotein lipase Mus musculus 13-31 9414485-1 1998 Lipoprotein lipase (LPL) is important in the process of triglyceride storage in adipose tissue. Triglycerides 56-68 lipoprotein lipase Mus musculus 20-23 9396715-0 1997 Nascent very-low-density lipoprotein triacylglycerol hydrolysis by lipoprotein lipase is inhibited by apolipoprotein E in a dose-dependent manner. Triglycerides 37-52 lipoprotein lipase Mus musculus 67-85 9409224-1 1997 Humans homozygous or heterozygous for mutations in the lipoprotein lipase (LPL) gene demonstrate significant disturbances in plasma lipoproteins, including raised triglyceride (TG) and reduced HDL cholesterol levels. Triglycerides 163-175 lipoprotein lipase Mus musculus 55-73 9409224-1 1997 Humans homozygous or heterozygous for mutations in the lipoprotein lipase (LPL) gene demonstrate significant disturbances in plasma lipoproteins, including raised triglyceride (TG) and reduced HDL cholesterol levels. Triglycerides 163-175 lipoprotein lipase Mus musculus 75-78 9409224-1 1997 Humans homozygous or heterozygous for mutations in the lipoprotein lipase (LPL) gene demonstrate significant disturbances in plasma lipoproteins, including raised triglyceride (TG) and reduced HDL cholesterol levels. Triglycerides 177-179 lipoprotein lipase Mus musculus 55-73 9409224-1 1997 Humans homozygous or heterozygous for mutations in the lipoprotein lipase (LPL) gene demonstrate significant disturbances in plasma lipoproteins, including raised triglyceride (TG) and reduced HDL cholesterol levels. Triglycerides 177-179 lipoprotein lipase Mus musculus 75-78 7759497-0 1995 COOH-terminal disruption of lipoprotein lipase in mice is lethal in homozygotes, but heterozygotes have elevated triglycerides and impaired enzyme activity. Triglycerides 113-126 lipoprotein lipase Mus musculus 28-46 9382958-5 1997 Overexpression of LPL resulted in marked reductions in total plasma cholesterol (TC; 48%, 43%, 25%) and triglycerides (TTg; 63%, 40%, 70%, p < 0.01) in apoE-/-, LDLr-/-, and wild-type (WT) mice, respectively. Triglycerides 104-117 lipoprotein lipase Mus musculus 18-21 9239412-11 1997 We postulate that fatty acids derived from macrophage LPL-catalyzed hydrolysis of triglycerides and phospholipids provide energy for macrophages in areas that have limited amounts of ambient glucose, and during periods of intense metabolic activity. Triglycerides 82-95 lipoprotein lipase Mus musculus 54-57 8824281-2 1996 Hepatic lipase (HL) and lipoprotein lipase (LPL) are key enzymes involved in the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins. Triglycerides 95-108 lipoprotein lipase Mus musculus 24-42 8824281-2 1996 Hepatic lipase (HL) and lipoprotein lipase (LPL) are key enzymes involved in the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins. Triglycerides 95-108 lipoprotein lipase Mus musculus 44-47 8663292-1 1996 Lipoprotein lipase (LPL), the major enzyme responsible for the hydrolysis of plasma triglycerides, promotes binding and catabolism of triglyceride-rich lipoproteins by various cultured cells. Triglycerides 84-97 lipoprotein lipase Mus musculus 0-18 8675619-12 1995 Heterozygous LPL knockout mice survive to adulthood and have mild hypertriglyceridemia, with 1.5-2-fold elevated triglyceride levels compared with controls in both the fed and fasted states on chow, Western-type, or 10% sucrose diets. Triglycerides 71-83 lipoprotein lipase Mus musculus 13-16 8675619-14 1995 In summary, total LPL deficiency in the mouse prevents triglyceride removal from plasma, causing death in the neonatal period, and expression of LPL in a single tissue alleviates this problem. Triglycerides 55-67 lipoprotein lipase Mus musculus 18-21 7598704-6 1995 Results suggest that the overexpression of LPL does not induce obesity by enhancing the hydrolysis of triglycerides in adipose tissue. Triglycerides 102-115 lipoprotein lipase Mus musculus 43-46 9396715-1 1997 In the present study it was investigated whether apolipoprotein (apoE) can inhibit the lipoprotein lipase (LPL)-mediated hydrolysis of very-low-density-lipoprotein (VLDL) triacylglycerols (TAGs). Triglycerides 171-187 lipoprotein lipase Mus musculus 87-105 9396715-1 1997 In the present study it was investigated whether apolipoprotein (apoE) can inhibit the lipoprotein lipase (LPL)-mediated hydrolysis of very-low-density-lipoprotein (VLDL) triacylglycerols (TAGs). Triglycerides 171-187 lipoprotein lipase Mus musculus 107-110 9202040-0 1997 Induced mutant mice expressing lipoprotein lipase exclusively in muscle have subnormal triglycerides yet reduced high density lipoprotein cholesterol levels in plasma. Triglycerides 87-100 lipoprotein lipase Mus musculus 31-49 9202256-8 1997 These data suggest that decreased PPARgamma expression following endotoxin or TNF treatment may contribute to the hyperlipidemia due to decreased expression of LPL, which would impair triglyceride clearance. Triglycerides 184-196 lipoprotein lipase Mus musculus 160-163 8864964-3 1996 The presence of enlarged triglyceride-rich particles with prolonged residence time in plasma implied defective lipolysis, but in vitro these particles were good substrates for purified lipoprotein lipase (LPL). Triglycerides 25-37 lipoprotein lipase Mus musculus 185-203 8864964-3 1996 The presence of enlarged triglyceride-rich particles with prolonged residence time in plasma implied defective lipolysis, but in vitro these particles were good substrates for purified lipoprotein lipase (LPL). Triglycerides 25-37 lipoprotein lipase Mus musculus 205-208 8732771-1 1996 Although it has been known for over 50 years that lipoprotein lipase (LPL) hydrolyzes triglyceride in chylomicrons, during the past half decade there has been a reinterest in the physiologic and pathophysiologic actions of this enzyme. Triglycerides 86-98 lipoprotein lipase Mus musculus 50-68 8732771-1 1996 Although it has been known for over 50 years that lipoprotein lipase (LPL) hydrolyzes triglyceride in chylomicrons, during the past half decade there has been a reinterest in the physiologic and pathophysiologic actions of this enzyme. Triglycerides 86-98 lipoprotein lipase Mus musculus 70-73 7635990-1 1995 In extrahepatic tissues lipoprotein lipase (LPL) hydrolyzes triglycerides thereby generating FFA for tissue uptake and metabolism. Triglycerides 60-73 lipoprotein lipase Mus musculus 24-42 7635990-1 1995 In extrahepatic tissues lipoprotein lipase (LPL) hydrolyzes triglycerides thereby generating FFA for tissue uptake and metabolism. Triglycerides 60-73 lipoprotein lipase Mus musculus 44-47 7635990-4 1995 In proportion to the level of LPL overexpression, decreased plasma triglyceride levels, elevated FFA uptake by muscle tissue, weight loss, and premature death were observed in three independent transgenic mouse lines. Triglycerides 67-79 lipoprotein lipase Mus musculus 30-33 7635990-7 1995 Our experiments indicate that LPL is rate limiting for the supply of muscle tissue with triglyceride-derived FFA. Triglycerides 88-100 lipoprotein lipase Mus musculus 30-33 7759497-4 1995 Pups homozygous (-/-) for LPL deficiency died within 48 h of birth with extreme elevations of serum triglycerides (13,327 mg/dl) associated with essentially absent LPL enzyme activity in heart and carcass. Triglycerides 100-113 lipoprotein lipase Mus musculus 26-29 7759497-5 1995 Newborn heterozygous (+/-) LPL-deficient pups had lower LPL enzyme activity and higher triglycerides (370 versus 121 mg/dl) than wild type (+/+) littermates. Triglycerides 87-100 lipoprotein lipase Mus musculus 27-30 8157673-1 1994 Lipoprotein lipase (LPL) is a key enzyme required for the hydrolysis of triglyceride-rich particles. Triglycerides 72-84 lipoprotein lipase Mus musculus 0-18 8157673-1 1994 Lipoprotein lipase (LPL) is a key enzyme required for the hydrolysis of triglyceride-rich particles. Triglycerides 72-84 lipoprotein lipase Mus musculus 20-23 1748295-1 1991 The enzyme lipoprotein lipase (LPL) is responsible for the hydrolysis of triglycerides into free fatty acids and glycerol. Triglycerides 73-86 lipoprotein lipase Mus musculus 11-29 8509711-12 1993 Collectively, these experiments demonstrate that extracellular lipolysis of Sf 60-400 VLDL by LPL is required for cholesteryl ester and triglyceride accumulation in J774 macrophages. Triglycerides 136-148 lipoprotein lipase Mus musculus 94-97 8509711-13 1993 After interaction with cellular LPL, VLDL triglycerides are hydrolyzed. Triglycerides 42-55 lipoprotein lipase Mus musculus 32-35 8500514-4 1993 Lipoprotein lipase activity in skeletal muscle tissue (mLPL) has previously been found to be an important factor regulating the concentration of serum triglycerides. Triglycerides 151-164 lipoprotein lipase Mus musculus 55-59 8500514-7 1993 Basal mLPL was negatively correlated with serum triglycerides (r = -0.48, P < 0.05) and positively correlated with HDL-cholesterol (r = 0.58, P < 0.01). Triglycerides 48-61 lipoprotein lipase Mus musculus 6-10 1450177-7 1992 Suppression of LPL secretion preceded gross triglyceride accumulation, was reversible, and was not the result of a reduction in LPL mRNA. Triglycerides 44-56 lipoprotein lipase Mus musculus 15-18 1450177-9 1992 Inhibition of LPL secretion by tunicamycin in both peritoneal macrophages and J774.1 cells prevented a hypertriglyceridemic very low density lipoprotein-induced triglyceride accumulation, an effect that was counteracted by addition of exogenous LPL. Triglycerides 108-120 lipoprotein lipase Mus musculus 14-17 1450177-10 1992 The results suggest that 1) extracellular hydrolysis of lipoprotein triglyceride is a major factor in inducing foam cell formation and 2) LPL secretion may be regulated by cell energy needs, and when these needs are exceeded, LPL secretion is suppressed. Triglycerides 68-80 lipoprotein lipase Mus musculus 226-229 1748295-1 1991 The enzyme lipoprotein lipase (LPL) is responsible for the hydrolysis of triglycerides into free fatty acids and glycerol. Triglycerides 73-86 lipoprotein lipase Mus musculus 31-34 1765386-1 1991 The catabolism of triglycerides-rich lipoproteins and the subsequent uptake of free fatty acids by muscle and adipose tissue is dependent on the enzyme lipoprotein lipase (LPL). Triglycerides 18-31 lipoprotein lipase Mus musculus 152-170 1765386-1 1991 The catabolism of triglycerides-rich lipoproteins and the subsequent uptake of free fatty acids by muscle and adipose tissue is dependent on the enzyme lipoprotein lipase (LPL). Triglycerides 18-31 lipoprotein lipase Mus musculus 172-175 34977493-5 2021 Lipoprotein lipase (LPL) is an essential enzyme in the anabolism and catabolism of very low-density lipoprotein, chylomicrons, and triglyceride-rich lipoproteins. Triglycerides 131-143 lipoprotein lipase Mus musculus 0-18 2025878-5 1991 The increased LPL would provide an increased level of fatty acids for oxidation in the cachectic state and would account for the effect on plasma FFAs and triglycerides. Triglycerides 155-168 lipoprotein lipase Mus musculus 14-17 34890852-9 2022 Adipose tissue explant secretomics further reveals that Trib1_ASKO adipose tissue has decreased ANGPTL4 production, and we demonstrate an accompanying increase in LPL activity that likely underlies the triglyceride phenotype. Triglycerides 202-214 lipoprotein lipase Mus musculus 163-166 34977493-5 2021 Lipoprotein lipase (LPL) is an essential enzyme in the anabolism and catabolism of very low-density lipoprotein, chylomicrons, and triglyceride-rich lipoproteins. Triglycerides 131-143 lipoprotein lipase Mus musculus 20-23 2993897-2 1985 Among these changes, a hypertriglyceridaemic state is frequently evident, resulting from defective triglyceride clearance, caused by systemic suppression of the enzyme lipoprotein lipase (LPL). Triglycerides 99-111 lipoprotein lipase Mus musculus 168-186 34580885-8 2022 The dysregulated liver LPL expression and low plasma triglyceride levels in ZBTB20-deficient mice were normalized by inactivating hepatic LPL expression. Triglycerides 53-65 lipoprotein lipase Mus musculus 138-141 34474934-2 2021 Angiopoietin-like proteins 3 (ANGPTL3) and 4 (ANGPTL4) are critical regulators of TG metabolism that function by inhibiting the activity of lipoprotein lipase (LPL), which is responsible for hydrolyzing triglycerides in lipoproteins into free fatty acids. Triglycerides 82-84 lipoprotein lipase Mus musculus 140-158 34474934-2 2021 Angiopoietin-like proteins 3 (ANGPTL3) and 4 (ANGPTL4) are critical regulators of TG metabolism that function by inhibiting the activity of lipoprotein lipase (LPL), which is responsible for hydrolyzing triglycerides in lipoproteins into free fatty acids. Triglycerides 82-84 lipoprotein lipase Mus musculus 160-163 34474934-2 2021 Angiopoietin-like proteins 3 (ANGPTL3) and 4 (ANGPTL4) are critical regulators of TG metabolism that function by inhibiting the activity of lipoprotein lipase (LPL), which is responsible for hydrolyzing triglycerides in lipoproteins into free fatty acids. Triglycerides 203-216 lipoprotein lipase Mus musculus 140-158 34474934-2 2021 Angiopoietin-like proteins 3 (ANGPTL3) and 4 (ANGPTL4) are critical regulators of TG metabolism that function by inhibiting the activity of lipoprotein lipase (LPL), which is responsible for hydrolyzing triglycerides in lipoproteins into free fatty acids. Triglycerides 203-216 lipoprotein lipase Mus musculus 160-163 35229724-8 2022 Thus, GPIHBP1"s AD plays a crucial function in plasma triglyceride metabolism; it sheathes LPL"s basic patch on the abluminal surface of ECs, thereby preventing LPL-HSPG interactions and freeing GPIHBP1-LPL complexes to move across ECs to the capillary lumen. Triglycerides 54-66 lipoprotein lipase Mus musculus 91-94 35229724-8 2022 Thus, GPIHBP1"s AD plays a crucial function in plasma triglyceride metabolism; it sheathes LPL"s basic patch on the abluminal surface of ECs, thereby preventing LPL-HSPG interactions and freeing GPIHBP1-LPL complexes to move across ECs to the capillary lumen. Triglycerides 54-66 lipoprotein lipase Mus musculus 161-164 35229724-8 2022 Thus, GPIHBP1"s AD plays a crucial function in plasma triglyceride metabolism; it sheathes LPL"s basic patch on the abluminal surface of ECs, thereby preventing LPL-HSPG interactions and freeing GPIHBP1-LPL complexes to move across ECs to the capillary lumen. Triglycerides 54-66 lipoprotein lipase Mus musculus 203-206 2563260-1 1989 We report here a study of the developmental and genetic control of tissue-specific expression of lipoprotein lipase, the enzyme responsible for hydrolysis of triglycerides in chylomicrons and very low density lipoproteins. Triglycerides 158-171 lipoprotein lipase Mus musculus 97-115 3516405-15 1986 Our findings suggest that particulate triacylglycerol was hydrolyzed by lipoprotein lipase at the surface of macrophages, and that fatty acid and monoacylglycerol formed by lipolysis were transported directly into the cells to be reesterified. Triglycerides 38-53 lipoprotein lipase Mus musculus 72-90 34065318-7 2021 Furthermore, the TG lowering effect of hepatic deletion of SHP was caused by increased clearance of postprandial TG and accompanied with decreased plasma levels of ApoC1, an inhibitor of lipoprotein lipase activity. Triglycerides 17-19 lipoprotein lipase Mus musculus 187-205 35413480-6 2022 Our findings highlight involvement of PPARgamma and a crucial role of ANGPTL4 in mediating the diurnal oscillation of TG-derived FA-uptake by BAT, and imply that time of day is essential when targeting LPL activity in BAT to improve metabolic health. Triglycerides 118-120 lipoprotein lipase Mus musculus 202-205 2735404-8 1989 The findings indicate that lipoprotein lipase in heart is synthesized by myocytes, transferred across extracellular space along cell surfaces and across endothelial cells via vesicles or intracellular channels, and concentrated at the surface of luminal projections of endothelium where the enzyme hydrolyzes triacylglycerol of chylomicrons and very low-density lipoproteins. Triglycerides 309-324 lipoprotein lipase Mus musculus 27-45 2760964-1 1989 It was demonstrated by using lipoprotein lipase (LPL) inhibitor benzene boronic acid (BBA) that LPL played a major role in the accumulation of triglycerides (TG) in mouse peritoneal macrophages exposed to rabbit normal very low density lipoproteins (N-VLDL). Triglycerides 143-156 lipoprotein lipase Mus musculus 29-47 2760964-1 1989 It was demonstrated by using lipoprotein lipase (LPL) inhibitor benzene boronic acid (BBA) that LPL played a major role in the accumulation of triglycerides (TG) in mouse peritoneal macrophages exposed to rabbit normal very low density lipoproteins (N-VLDL). Triglycerides 143-156 lipoprotein lipase Mus musculus 49-52 2760964-1 1989 It was demonstrated by using lipoprotein lipase (LPL) inhibitor benzene boronic acid (BBA) that LPL played a major role in the accumulation of triglycerides (TG) in mouse peritoneal macrophages exposed to rabbit normal very low density lipoproteins (N-VLDL). Triglycerides 143-156 lipoprotein lipase Mus musculus 96-99 2760964-1 1989 It was demonstrated by using lipoprotein lipase (LPL) inhibitor benzene boronic acid (BBA) that LPL played a major role in the accumulation of triglycerides (TG) in mouse peritoneal macrophages exposed to rabbit normal very low density lipoproteins (N-VLDL). Triglycerides 158-160 lipoprotein lipase Mus musculus 29-47 2760964-1 1989 It was demonstrated by using lipoprotein lipase (LPL) inhibitor benzene boronic acid (BBA) that LPL played a major role in the accumulation of triglycerides (TG) in mouse peritoneal macrophages exposed to rabbit normal very low density lipoproteins (N-VLDL). Triglycerides 158-160 lipoprotein lipase Mus musculus 96-99 2993897-2 1985 Among these changes, a hypertriglyceridaemic state is frequently evident, resulting from defective triglyceride clearance, caused by systemic suppression of the enzyme lipoprotein lipase (LPL). Triglycerides 99-111 lipoprotein lipase Mus musculus 188-191 33846453-2 2021 Angiopoietin-like protein 4 (ANGPTL4) regulates plasma triglyceride levels by inhibiting lipoprotein lipase (LPL). Triglycerides 55-67 lipoprotein lipase Mus musculus 89-107 3905648-7 1985 The separation of ob17 cells by isopycnic centrifugation shows that lipoprotein lipase is present at high levels in early differentiating cells which are still devoid of late markers, ie glycerol-3-phosphate dehydrogenase and triglycerides. Triglycerides 226-239 lipoprotein lipase Mus musculus 68-86 7276825-2 1981 The mechanism by which endotoxin induces a deficiency in the activity of the key enzyme of triglyceride metabolism, lipoprotein lipase (LPL), has been studied. Triglycerides 91-103 lipoprotein lipase Mus musculus 136-139 6874679-10 1983 Accumulation of triglyceride occurred by uptake of intact VLDL particles, by uptake of a triglyceride-depleted particle produced by the action of LPL, and by the direct uptake of free fatty acids generated by the activity of LPL. Triglycerides 16-28 lipoprotein lipase Mus musculus 146-149 6874679-10 1983 Accumulation of triglyceride occurred by uptake of intact VLDL particles, by uptake of a triglyceride-depleted particle produced by the action of LPL, and by the direct uptake of free fatty acids generated by the activity of LPL. Triglycerides 16-28 lipoprotein lipase Mus musculus 225-228 6874679-10 1983 Accumulation of triglyceride occurred by uptake of intact VLDL particles, by uptake of a triglyceride-depleted particle produced by the action of LPL, and by the direct uptake of free fatty acids generated by the activity of LPL. Triglycerides 89-101 lipoprotein lipase Mus musculus 146-149 7276825-2 1981 The mechanism by which endotoxin induces a deficiency in the activity of the key enzyme of triglyceride metabolism, lipoprotein lipase (LPL), has been studied. Triglycerides 91-103 lipoprotein lipase Mus musculus 116-134 33846453-10 2021 These observations suggest that after chronic high-fat feeding LPL is no longer rate-limiting for triglyceride delivery to adipocytes. Triglycerides 98-110 lipoprotein lipase Mus musculus 63-66 33846453-2 2021 Angiopoietin-like protein 4 (ANGPTL4) regulates plasma triglyceride levels by inhibiting lipoprotein lipase (LPL). Triglycerides 55-67 lipoprotein lipase Mus musculus 109-112 31645434-0 2020 A lipoprotein lipase-GPI-anchored high-density lipoprotein-binding protein 1 fusion lowers triglycerides in mice: Implications for managing familial chylomicronemia syndrome. Triglycerides 91-104 lipoprotein lipase Mus musculus 2-20 32739175-1 2020 Lipoprotein lipase (LPL) plays a central role in hydrolyzing triglyceride and its deficiency leads to atherosclerosis. Triglycerides 61-73 lipoprotein lipase Mus musculus 0-18 32739175-1 2020 Lipoprotein lipase (LPL) plays a central role in hydrolyzing triglyceride and its deficiency leads to atherosclerosis. Triglycerides 61-73 lipoprotein lipase Mus musculus 20-23 32237906-4 2020 The elevated plasma triglyceride level was due to impaired LPL-mediated triglyceride clearance caused by a disrupted LPL secretion. Triglycerides 20-32 lipoprotein lipase Mus musculus 59-62 32237906-4 2020 The elevated plasma triglyceride level was due to impaired LPL-mediated triglyceride clearance caused by a disrupted LPL secretion. Triglycerides 20-32 lipoprotein lipase Mus musculus 117-120 32237906-4 2020 The elevated plasma triglyceride level was due to impaired LPL-mediated triglyceride clearance caused by a disrupted LPL secretion. Triglycerides 72-84 lipoprotein lipase Mus musculus 59-62 32690595-2 2020 5D2 has been used to measure LPL levels, block the triglyceride hydrolase activity of LPL, and prevent the propensity of concentrated LPL preparations to form homodimers. Triglycerides 51-63 lipoprotein lipase Mus musculus 86-89 32690595-2 2020 5D2 has been used to measure LPL levels, block the triglyceride hydrolase activity of LPL, and prevent the propensity of concentrated LPL preparations to form homodimers. Triglycerides 51-63 lipoprotein lipase Mus musculus 86-89 32730227-1 2020 The angiopoietin-like protein ANGPTL8 (A8) is one of three ANGPTLs (A8, A3, A4) that coordinate changes in triglyceride (TG) delivery to tissues by inhibiting lipoprotein lipase (LPL), an enzyme that hydrolyzes TG. Triglycerides 107-119 lipoprotein lipase Mus musculus 159-177 32730227-1 2020 The angiopoietin-like protein ANGPTL8 (A8) is one of three ANGPTLs (A8, A3, A4) that coordinate changes in triglyceride (TG) delivery to tissues by inhibiting lipoprotein lipase (LPL), an enzyme that hydrolyzes TG. Triglycerides 121-123 lipoprotein lipase Mus musculus 159-177 32730227-1 2020 The angiopoietin-like protein ANGPTL8 (A8) is one of three ANGPTLs (A8, A3, A4) that coordinate changes in triglyceride (TG) delivery to tissues by inhibiting lipoprotein lipase (LPL), an enzyme that hydrolyzes TG. Triglycerides 121-123 lipoprotein lipase Mus musculus 179-182 32730227-1 2020 The angiopoietin-like protein ANGPTL8 (A8) is one of three ANGPTLs (A8, A3, A4) that coordinate changes in triglyceride (TG) delivery to tissues by inhibiting lipoprotein lipase (LPL), an enzyme that hydrolyzes TG. Triglycerides 211-213 lipoprotein lipase Mus musculus 159-177 31645434-1 2020 Lipoprotein lipase (LPL) is central to triglyceride metabolism. Triglycerides 39-51 lipoprotein lipase Mus musculus 0-18 31645434-1 2020 Lipoprotein lipase (LPL) is central to triglyceride metabolism. Triglycerides 39-51 lipoprotein lipase Mus musculus 20-23 31645434-2 2020 Severely compromised LPL activity causes familial chylomicronemia syndrome (FCS), which is associated with very high plasma triglyceride levels and increased risk of life-threatening pancreatitis. Triglycerides 124-136 lipoprotein lipase Mus musculus 21-24 30408040-1 2018 GPIHBP1 is a protein localized at the endothelial cell surface that facilitates triglyceride (TG) lipolysis by binding lipoprotein lipase (LPL). Triglycerides 80-92 lipoprotein lipase Mus musculus 119-137 31996466-2 2020 We describe a strategy for lowering triglycerides (TGs) with an apolipoprotein C-II (apoC-II) mimetic peptide called D6PV that activates lipoprotein lipase (LPL), the main plasma TG-hydrolyzing enzyme, and antagonizes the TG-raising effect of apoC-III. Triglycerides 36-49 lipoprotein lipase Mus musculus 137-155 31996466-2 2020 We describe a strategy for lowering triglycerides (TGs) with an apolipoprotein C-II (apoC-II) mimetic peptide called D6PV that activates lipoprotein lipase (LPL), the main plasma TG-hydrolyzing enzyme, and antagonizes the TG-raising effect of apoC-III. Triglycerides 36-49 lipoprotein lipase Mus musculus 157-160 31996466-2 2020 We describe a strategy for lowering triglycerides (TGs) with an apolipoprotein C-II (apoC-II) mimetic peptide called D6PV that activates lipoprotein lipase (LPL), the main plasma TG-hydrolyzing enzyme, and antagonizes the TG-raising effect of apoC-III. Triglycerides 51-54 lipoprotein lipase Mus musculus 137-155 31996466-2 2020 We describe a strategy for lowering triglycerides (TGs) with an apolipoprotein C-II (apoC-II) mimetic peptide called D6PV that activates lipoprotein lipase (LPL), the main plasma TG-hydrolyzing enzyme, and antagonizes the TG-raising effect of apoC-III. Triglycerides 51-54 lipoprotein lipase Mus musculus 157-160 31996466-2 2020 We describe a strategy for lowering triglycerides (TGs) with an apolipoprotein C-II (apoC-II) mimetic peptide called D6PV that activates lipoprotein lipase (LPL), the main plasma TG-hydrolyzing enzyme, and antagonizes the TG-raising effect of apoC-III. Triglycerides 51-53 lipoprotein lipase Mus musculus 137-155 31996466-2 2020 We describe a strategy for lowering triglycerides (TGs) with an apolipoprotein C-II (apoC-II) mimetic peptide called D6PV that activates lipoprotein lipase (LPL), the main plasma TG-hydrolyzing enzyme, and antagonizes the TG-raising effect of apoC-III. Triglycerides 51-53 lipoprotein lipase Mus musculus 157-160 31996466-2 2020 We describe a strategy for lowering triglycerides (TGs) with an apolipoprotein C-II (apoC-II) mimetic peptide called D6PV that activates lipoprotein lipase (LPL), the main plasma TG-hydrolyzing enzyme, and antagonizes the TG-raising effect of apoC-III. Triglycerides 179-181 lipoprotein lipase Mus musculus 137-155 30944669-1 2019 Angiopoietin-like 3 (ANGPTL3) is a regulator of plasma triglyceride (TRG) levels due to its inhibitory action on the activity of lipoprotein lipase (LPL). Triglycerides 55-67 lipoprotein lipase Mus musculus 129-147 30944669-1 2019 Angiopoietin-like 3 (ANGPTL3) is a regulator of plasma triglyceride (TRG) levels due to its inhibitory action on the activity of lipoprotein lipase (LPL). Triglycerides 55-67 lipoprotein lipase Mus musculus 149-152 30944669-1 2019 Angiopoietin-like 3 (ANGPTL3) is a regulator of plasma triglyceride (TRG) levels due to its inhibitory action on the activity of lipoprotein lipase (LPL). Triglycerides 69-72 lipoprotein lipase Mus musculus 129-147 30944669-1 2019 Angiopoietin-like 3 (ANGPTL3) is a regulator of plasma triglyceride (TRG) levels due to its inhibitory action on the activity of lipoprotein lipase (LPL). Triglycerides 69-72 lipoprotein lipase Mus musculus 149-152 30496565-4 2018 Moreover, the level of serum lipoprotein lipase (LPL), which plays an important role in fatty acid release from TG, was decreased significantly. Triglycerides 112-114 lipoprotein lipase Mus musculus 29-47 30496565-4 2018 Moreover, the level of serum lipoprotein lipase (LPL), which plays an important role in fatty acid release from TG, was decreased significantly. Triglycerides 112-114 lipoprotein lipase Mus musculus 49-52 31233750-1 2019 Lipoprotein lipase (LPL) is the rate-controlling enzyme for the accumulation of triacylglycerol into adipocytes, which acts by digesting it into glycerol and fatty acids. Triglycerides 80-95 lipoprotein lipase Mus musculus 0-18 31233750-1 2019 Lipoprotein lipase (LPL) is the rate-controlling enzyme for the accumulation of triacylglycerol into adipocytes, which acts by digesting it into glycerol and fatty acids. Triglycerides 80-95 lipoprotein lipase Mus musculus 20-23 31234537-1 2019 Lipoprotein lipase (LPL) hydrolyzes triglycerides in lipoprotein to supply fatty acids, and its deficiency leads to hypertriglyceridemia, thereby inducing metabolic syndrome (MetSyn). Triglycerides 36-49 lipoprotein lipase Mus musculus 0-18 31234537-1 2019 Lipoprotein lipase (LPL) hydrolyzes triglycerides in lipoprotein to supply fatty acids, and its deficiency leads to hypertriglyceridemia, thereby inducing metabolic syndrome (MetSyn). Triglycerides 36-49 lipoprotein lipase Mus musculus 20-23 29752428-2 2019 They inhibit the enzyme lipoprotein lipase, which plays a key role in the intravascular lipolysis of triglycerides present in some lipoprotein classes. Triglycerides 101-114 lipoprotein lipase Mus musculus 24-42 30598475-1 2019 Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1), the protein that shuttles LPL to the capillary lumen, is essential for plasma triglyceride metabolism. Triglycerides 170-182 lipoprotein lipase Mus musculus 118-121 30408040-1 2018 GPIHBP1 is a protein localized at the endothelial cell surface that facilitates triglyceride (TG) lipolysis by binding lipoprotein lipase (LPL). Triglycerides 80-92 lipoprotein lipase Mus musculus 139-142 30408040-1 2018 GPIHBP1 is a protein localized at the endothelial cell surface that facilitates triglyceride (TG) lipolysis by binding lipoprotein lipase (LPL). Triglycerides 94-96 lipoprotein lipase Mus musculus 119-137 30408040-1 2018 GPIHBP1 is a protein localized at the endothelial cell surface that facilitates triglyceride (TG) lipolysis by binding lipoprotein lipase (LPL). Triglycerides 94-96 lipoprotein lipase Mus musculus 139-142 29563332-2 2018 Angiopoietin-like protein 4 (ANGPTL4), a protein that inhibits lipoprotein lipase (LPL), controls fatty acid (FA) uptake in adipose and oxidative tissues and regulates circulating triacylglycerol-rich (TAG-rich) lipoproteins. Triglycerides 180-195 lipoprotein lipase Mus musculus 63-81 30232292-1 2018 BACKGROUND: Lipoprotein lipase (LPL) plays an important role in triglyceride metabolism. Triglycerides 64-76 lipoprotein lipase Mus musculus 12-30 30232292-1 2018 BACKGROUND: Lipoprotein lipase (LPL) plays an important role in triglyceride metabolism. Triglycerides 64-76 lipoprotein lipase Mus musculus 32-35 29738435-2 2018 CREBH governs triglyceride metabolism in the liver, which mediates the changes in gene expression governing fatty acid oxidation, ketogenesis, and apolipoproteins related to lipoprotein lipase (LPL) activation. Triglycerides 14-26 lipoprotein lipase Mus musculus 194-197 29627378-2 2018 This process is mediated by the lipoprotein lipase (LPL), an enzyme that catalyzed the hydrolysis of triglyceride (TAG) in glycerol and fatty acids (FA), which are burned to generate heat. Triglycerides 101-113 lipoprotein lipase Mus musculus 32-50 29627378-2 2018 This process is mediated by the lipoprotein lipase (LPL), an enzyme that catalyzed the hydrolysis of triglyceride (TAG) in glycerol and fatty acids (FA), which are burned to generate heat. Triglycerides 101-113 lipoprotein lipase Mus musculus 52-55 30021841-1 2018 Lipoprotein lipase (LPL) catalyzes the breakdown of circulating triglycerides in muscle and fat. Triglycerides 64-77 lipoprotein lipase Mus musculus 0-18 30021841-1 2018 Lipoprotein lipase (LPL) catalyzes the breakdown of circulating triglycerides in muscle and fat. Triglycerides 64-77 lipoprotein lipase Mus musculus 20-23 29502266-1 2018 AIMS/HYPOTHESIS: Angiopoietin-like 4 (ANGPTL4) is an important regulator of triacylglycerol metabolism, carrying out this role by inhibiting the enzymes lipoprotein lipase and pancreatic lipase. Triglycerides 76-91 lipoprotein lipase Mus musculus 153-171 29563332-2 2018 Angiopoietin-like protein 4 (ANGPTL4), a protein that inhibits lipoprotein lipase (LPL), controls fatty acid (FA) uptake in adipose and oxidative tissues and regulates circulating triacylglycerol-rich (TAG-rich) lipoproteins. Triglycerides 180-195 lipoprotein lipase Mus musculus 83-86 29371243-2 2018 Lipoprotein lipase (LpL), the rate-limiting enzyme in blood triglyceride catabolism, is expressed by macrophages in atherosclerotic plaques. Triglycerides 60-72 lipoprotein lipase Mus musculus 0-18 29371243-2 2018 Lipoprotein lipase (LpL), the rate-limiting enzyme in blood triglyceride catabolism, is expressed by macrophages in atherosclerotic plaques. Triglycerides 60-72 lipoprotein lipase Mus musculus 20-23 28694296-0 2017 Apolipoprotein C-III inhibits triglyceride hydrolysis by GPIHBP1-bound LPL. Triglycerides 30-42 lipoprotein lipase Mus musculus 71-74 29304082-1 2018 Excessive circulating triglycerides due to reduction or loss of lipoprotein lipase activity contribute to hypertriglyceridemia and increased risk for pancreatitis. Triglycerides 22-35 lipoprotein lipase Mus musculus 64-82 29304082-3 2018 Synthesized in multiple tissues including striated muscle and adipose tissue, lipoprotein lipase is trafficked to blood vessel endothelial cells where it is anchored at the plasma membrane and hydrolyzes triglycerides into free fatty acids. Triglycerides 204-217 lipoprotein lipase Mus musculus 78-96 29304082-7 2018 Human lipoprotein lipase infected mice had significantly lower blood triglycerides compared to mCherry controls and were comparable to wild-type blood triglyceride levels. Triglycerides 69-82 lipoprotein lipase Mus musculus 6-24 29304082-7 2018 Human lipoprotein lipase infected mice had significantly lower blood triglycerides compared to mCherry controls and were comparable to wild-type blood triglyceride levels. Triglycerides 69-81 lipoprotein lipase Mus musculus 6-24 28733267-1 2017 Angiopoietin-like 4 (ANGPTL4) raises plasma triglyceride levels by inhibiting lipoprotein lipase. Triglycerides 44-56 lipoprotein lipase Mus musculus 78-96 29449313-3 2018 In wild-type mice, cold exposure increases LPL-mediated processing of triglyceride-rich lipoproteins (TRLs) in brown adipose tissue (BAT), providing fuel for thermogenesis and leading to lower plasma triglyceride levels. Triglycerides 70-82 lipoprotein lipase Mus musculus 43-46 29299589-9 2018 The hypolipidemic effect occurred partly due to the regulation of hepatic lipase (HL) and lipoprotein lipase (LPL) in serum and liver to markedly decrease TG. Triglycerides 155-157 lipoprotein lipase Mus musculus 90-108 29299589-9 2018 The hypolipidemic effect occurred partly due to the regulation of hepatic lipase (HL) and lipoprotein lipase (LPL) in serum and liver to markedly decrease TG. Triglycerides 155-157 lipoprotein lipase Mus musculus 110-113 28710138-3 2017 Ex vivo studies with hypothalamus-derived astrocytes showed that LPL expression is upregulated by oleic acid, whereas it is decreased in response to palmitic acid or triglycerides. Triglycerides 166-179 lipoprotein lipase Mus musculus 65-68 28694296-5 2017 However, the triglycerides in apoC-III-enriched TRLs were hydrolyzed more slowly by free LPL, and the inhibitory effect of apoC-III on triglyceride lipolysis was exaggerated when LPL was bound to GPIHBP1 on the surface of agarose beads. Triglycerides 13-26 lipoprotein lipase Mus musculus 89-92 28694296-5 2017 However, the triglycerides in apoC-III-enriched TRLs were hydrolyzed more slowly by free LPL, and the inhibitory effect of apoC-III on triglyceride lipolysis was exaggerated when LPL was bound to GPIHBP1 on the surface of agarose beads. Triglycerides 13-26 lipoprotein lipase Mus musculus 179-182 28694296-5 2017 However, the triglycerides in apoC-III-enriched TRLs were hydrolyzed more slowly by free LPL, and the inhibitory effect of apoC-III on triglyceride lipolysis was exaggerated when LPL was bound to GPIHBP1 on the surface of agarose beads. Triglycerides 13-25 lipoprotein lipase Mus musculus 89-92 28694296-5 2017 However, the triglycerides in apoC-III-enriched TRLs were hydrolyzed more slowly by free LPL, and the inhibitory effect of apoC-III on triglyceride lipolysis was exaggerated when LPL was bound to GPIHBP1 on the surface of agarose beads. Triglycerides 13-25 lipoprotein lipase Mus musculus 179-182 28694296-6 2017 Also, recombinant apoC-III reduced triglyceride hydrolysis by free LPL only modestly, but the inhibitory effect was greater when the LPL was bound to GPIHBP1. Triglycerides 35-47 lipoprotein lipase Mus musculus 67-70 28694296-7 2017 A mutant apoC-III associated with low plasma triglyceride levels (p.A23T) displayed a reduced capacity to inhibit free and GPIHBP1-bound LPL. Triglycerides 45-57 lipoprotein lipase Mus musculus 137-140 28694296-8 2017 Our results show that apoC-III potently inhibits triglyceride hydrolysis when LPL is bound to GPIHBP1. Triglycerides 49-61 lipoprotein lipase Mus musculus 78-81 28456865-2 2017 It has been shown that neuronal lipoprotein lipase (LPL) participates in the control of energy balance by hydrolysing lipid particles enriched in triacylglycerols. Triglycerides 146-162 lipoprotein lipase Mus musculus 32-50 28456865-2 2017 It has been shown that neuronal lipoprotein lipase (LPL) participates in the control of energy balance by hydrolysing lipid particles enriched in triacylglycerols. Triglycerides 146-162 lipoprotein lipase Mus musculus 52-55 28412693-1 2017 Angiopoietin-like 4 (ANGPTL4) regulates plasma triglyceride levels by inhibiting LPL. Triglycerides 47-59 lipoprotein lipase Mus musculus 81-84 28413163-1 2017 Angiopoietin-like (ANGPTL)3 and ANGPTL8 are secreted proteins and inhibitors of LPL-mediated plasma triglyceride (TG) clearance. Triglycerides 100-112 lipoprotein lipase Mus musculus 80-83 28413163-1 2017 Angiopoietin-like (ANGPTL)3 and ANGPTL8 are secreted proteins and inhibitors of LPL-mediated plasma triglyceride (TG) clearance. Triglycerides 114-116 lipoprotein lipase Mus musculus 80-83 27913180-2 2017 Lipoprotein lipase (LPL) is an enzyme that is responsible for the metabolism of core triglycerides of very-low density lipoproteins (VLDL) and chylomicrons in the vasculature. Triglycerides 85-98 lipoprotein lipase Mus musculus 0-18 27913180-2 2017 Lipoprotein lipase (LPL) is an enzyme that is responsible for the metabolism of core triglycerides of very-low density lipoproteins (VLDL) and chylomicrons in the vasculature. Triglycerides 85-98 lipoprotein lipase Mus musculus 20-23 27417587-1 2016 OBJECTIVE: Liver-enriched transcription factor cAMP-responsive element-binding protein H (CREBH) regulates plasma triglyceride clearance by inducing lipoprotein lipase cofactors, such as apolipoprotein A-IV (apoA-IV), apoA-V, and apoC-II. Triglycerides 114-126 lipoprotein lipase Mus musculus 149-167 27417587-6 2016 We showed that CREBH deletion in Ldlr(-/-) mice increased very low-density lipoprotein-associated triglyceride and cholesterol levels, consistent with the impairment of lipoprotein lipase-mediated triglyceride clearance in these mice. Triglycerides 197-209 lipoprotein lipase Mus musculus 169-187 26271253-7 2015 The absence of EP4 in mice compromised the activation of lipoprotein lipase (LPL), the key enzyme responsible for trafficking of plasma triglycerides into peripheral tissues. Triglycerides 136-149 lipoprotein lipase Mus musculus 57-75 26271253-7 2015 The absence of EP4 in mice compromised the activation of lipoprotein lipase (LPL), the key enzyme responsible for trafficking of plasma triglycerides into peripheral tissues. Triglycerides 136-149 lipoprotein lipase Mus musculus 77-80 27034464-1 2016 LPL hydrolyzes triglycerides in triglyceride-rich lipoproteins along the capillaries of heart, skeletal muscle, and adipose tissue. Triglycerides 15-28 lipoprotein lipase Mus musculus 0-3