PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9765271-13 1998 Interestingly, this region of chromosome 8 contains a cluster of three other genes important for fatty acid homeostasis, lipoprotein lipase, the mitochondrial uncoupling protein 1 (UCP1) and sterol regulatory element-binding protein 1. Fatty Acids 97-107 lipoprotein lipase Mus musculus 121-139 10488074-2 1999 Lipoprotein lipase (LPL) provides tissues with fatty acids, which have complex effects on glucose utilization and insulin secretion. Fatty Acids 47-58 lipoprotein lipase Mus musculus 0-18 10488074-2 1999 Lipoprotein lipase (LPL) provides tissues with fatty acids, which have complex effects on glucose utilization and insulin secretion. Fatty Acids 47-58 lipoprotein lipase Mus musculus 20-23 9294198-0 1997 Lipoprotein lipase controls fatty acid entry into adipose tissue, but fat mass is preserved by endogenous synthesis in mice deficient in adipose tissue lipoprotein lipase. Fatty Acids 28-38 lipoprotein lipase Mus musculus 0-18 9051314-10 1997 LPL activity in white and brown fat (expressed as nmol fatty acids released h-1 mg-1 acetone powder) was unaltered 60 min following an acute injection of ethanol (2.5 g kg-1, i.p.) Fatty Acids 55-66 lipoprotein lipase Mus musculus 0-3 9239412-2 1997 To determine whether fatty acids released from lipoproteins by macrophage lipoprotein lipase (LPL) could substitute for glucose as a source of energy for phagocytosis, we cultured peritoneal macrophages from normal and LPL knockout (LPL-KO) mice that had been rescued from neonatal demise by expression of human LPL via the muscle creatine kinase promoter. Fatty Acids 21-32 lipoprotein lipase Mus musculus 74-92 9239412-2 1997 To determine whether fatty acids released from lipoproteins by macrophage lipoprotein lipase (LPL) could substitute for glucose as a source of energy for phagocytosis, we cultured peritoneal macrophages from normal and LPL knockout (LPL-KO) mice that had been rescued from neonatal demise by expression of human LPL via the muscle creatine kinase promoter. Fatty Acids 21-32 lipoprotein lipase Mus musculus 94-97 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. Fatty Acids 18-29 lipoprotein lipase Mus musculus 54-57 8670068-0 1996 Fatty acids regulate the expression of lipoprotein lipase gene and activity in preadipose and adipose cells. Fatty Acids 0-11 lipoprotein lipase Mus musculus 39-57 6252272-18 1980 In comparison with previously described cells from an established cell line which undergo adipose conversion (3T3 cells), the cells described in the present work, like adipocytes, showed more metabolic activity in pathways for fatty acid incorporation from exogenous lipid sources (lipoprotein lipase activity) than from de novo synthesis. Fatty Acids 227-237 lipoprotein lipase Mus musculus 282-300 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. Fatty Acids 54-65 lipoprotein lipase Mus musculus 14-17 34803493-0 2021 Targeted Inhibition of LPL/FABP4/CPT1 fatty acid metabolic axis can effectively prevent the progression of nonalcoholic steatohepatitis to liver cancer. Fatty Acids 38-48 lipoprotein lipase Mus musculus 23-26 34803493-7 2021 Results: We found that upregulation of the LPL/FABP4/CPT1 molecular axis, as a fatty acid metabolic reprogramming process, occurred specifically during the NASH phase. Fatty Acids 79-89 lipoprotein lipase Mus musculus 43-46 6377200-3 1984 By impairing the activity of cell surface lipoprotein lipase, this mediator acts to inhibit the uptake of fatty acid, and ultimately the accumulation of lipid by the adipocyte. Fatty Acids 106-116 lipoprotein lipase Mus musculus 42-60 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. Fatty Acids 158-169 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. Fatty Acids 158-169 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). Fatty Acids 75-86 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). Fatty Acids 75-86 lipoprotein lipase Mus musculus 20-23 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. Fatty Acids 88-98 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. Fatty Acids 88-98 lipoprotein lipase Mus musculus 49-52 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. Fatty Acids 108-118 lipoprotein lipase Mus musculus 194-197 28608812-6 2017 Using a mouse model lacking lipoprotein lipase (LPL), a master regulator of plasma lipid turnover specifically in adipocytes, we show that impaired fatty acid flux leads to reduced amounts of dietary essential fatty acids while there was a profound increase in de novo produced fatty acids in both bone marrow and cortical bone. Fatty Acids 148-158 lipoprotein lipase Mus musculus 28-46 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. Fatty Acids 136-147 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. Fatty Acids 136-147 lipoprotein lipase Mus musculus 52-55 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. Fatty Acids 98-108 lipoprotein lipase Mus musculus 63-81 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. Fatty Acids 98-108 lipoprotein lipase Mus musculus 83-86 28608812-6 2017 Using a mouse model lacking lipoprotein lipase (LPL), a master regulator of plasma lipid turnover specifically in adipocytes, we show that impaired fatty acid flux leads to reduced amounts of dietary essential fatty acids while there was a profound increase in de novo produced fatty acids in both bone marrow and cortical bone. Fatty Acids 148-158 lipoprotein lipase Mus musculus 48-51 28608812-6 2017 Using a mouse model lacking lipoprotein lipase (LPL), a master regulator of plasma lipid turnover specifically in adipocytes, we show that impaired fatty acid flux leads to reduced amounts of dietary essential fatty acids while there was a profound increase in de novo produced fatty acids in both bone marrow and cortical bone. Fatty Acids 210-221 lipoprotein lipase Mus musculus 28-46 28608812-6 2017 Using a mouse model lacking lipoprotein lipase (LPL), a master regulator of plasma lipid turnover specifically in adipocytes, we show that impaired fatty acid flux leads to reduced amounts of dietary essential fatty acids while there was a profound increase in de novo produced fatty acids in both bone marrow and cortical bone. Fatty Acids 210-221 lipoprotein lipase Mus musculus 48-51 28608812-8 2017 These results identify LPL as an important regulator of fatty acid transport to skeletal compartments and demonstrate an intricate functional link between systemic and skeletal fatty acid and glucose metabolism. Fatty Acids 56-66 lipoprotein lipase Mus musculus 23-26 28608812-8 2017 These results identify LPL as an important regulator of fatty acid transport to skeletal compartments and demonstrate an intricate functional link between systemic and skeletal fatty acid and glucose metabolism. Fatty Acids 177-187 lipoprotein lipase Mus musculus 23-26 27665576-9 2017 The induction of LPL activity by fasting in the core transgenic mice activated PPARalpha downstream target genes that are involved in fatty acid beta-oxidation. Fatty Acids 134-144 lipoprotein lipase Mus musculus 17-20 24986598-3 2014 Selective silencing of ATM LPL decreased foam cell formation in visceral adipose tissue of obese mice, consistent with a reduced supply of fatty acids from VLDL hydrolysis. Fatty Acids 139-150 lipoprotein lipase Mus musculus 27-30 24986598-4 2014 Unexpectedly, silencing LPL also decreased the expression of genes involved in fatty acid uptake (CD36) and esterification in ATMs. Fatty Acids 79-89 lipoprotein lipase Mus musculus 24-27 24747115-12 2014 Even low levels of replacement of SAT by n-3 FA effectively reduce arterial lipid deposition by decreasing aortic LpL, macrophages and pro-inflammatory markers. Fatty Acids 34-37 lipoprotein lipase Mus musculus 114-117 24722352-10 2014 Resveratrol significantly decreases mRNA expression of Lpl, Scd1, Ppar-gamma, Acc1, and Fas related to fatty acids synthesis, adipogenesis and lipogenesis, which may be driven by increased Fiaf expression. Fatty Acids 103-114 lipoprotein lipase Mus musculus 55-58 23228690-2 2013 Lipoprotein lipase (LPL) is the master regulator of fatty acid uptake from triglyceride-rich lipoproteins. Fatty Acids 52-62 lipoprotein lipase Mus musculus 0-18 23253599-9 2013 These results were associated with up-regulation of PPAR-alpha, LPL, HSL and CPT-1, which are related to lipolysis and fatty acid oxidation. Fatty Acids 119-129 lipoprotein lipase Mus musculus 64-67 23542081-1 2013 Adipose fat storage is thought to require uptake of circulating triglyceride (TG)-derived fatty acids via lipoprotein lipase (LpL). Fatty Acids 90-101 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). Fatty Acids 90-101 lipoprotein lipase Mus musculus 126-129 23228690-2 2013 Lipoprotein lipase (LPL) is the master regulator of fatty acid uptake from triglyceride-rich lipoproteins. Fatty Acids 52-62 lipoprotein lipase Mus musculus 20-23 23228690-3 2013 In addition to LPL-mediated fatty acid uptake, adipocytes are able to synthesize fatty acids from non-lipid precursor, a process called de novo lipogenesis (DNL). Fatty Acids 28-38 lipoprotein lipase Mus musculus 15-18 19339774-1 2009 BACKGROUND/AIMS: To delineate the hypotriglyceridemic effect of conjugated linoleic acid (CLA) in mice, the effect of this fatty acid on lipoprotein lipase (LPL) and apolipoprotein C-III (ApoCIII) mRNA accumulation in muscle, adipose and liver tissue was studied. Fatty Acids 123-133 lipoprotein lipase Mus musculus 137-155 22562834-10 2012 Thus, overexpression of Lpl facilitates muscle fatty acid utilization and contributes to fat overload. Fatty Acids 47-57 lipoprotein lipase Mus musculus 24-27 21059267-11 2010 CONCLUSIONS: This study demonstrates that apoC-II and LPL mRNAs correlate temporally and geographically with surfactant lipid synthesis in preparation for birth and suggests that fatty acid recruitment from the circulation by apoC-II-activated LPL is regionally modulated by apoC-II secretion. Fatty Acids 179-189 lipoprotein lipase Mus musculus 54-57 21059267-11 2010 CONCLUSIONS: This study demonstrates that apoC-II and LPL mRNAs correlate temporally and geographically with surfactant lipid synthesis in preparation for birth and suggests that fatty acid recruitment from the circulation by apoC-II-activated LPL is regionally modulated by apoC-II secretion. Fatty Acids 179-189 lipoprotein lipase Mus musculus 244-247 20024897-2 2010 The expression levels of genes involved in lipid metabolism such as fatty-acid-binding protein 4 and lipoprotein lipase were significantly downregulated following treatment with platycodin D. Fatty Acids 68-78 lipoprotein lipase Mus musculus 95-119 20080985-8 2010 In addition, the expression of PPARgamma downstream target genes involved in fatty acid synthesis - the lipoprotein lipase (Lpl) and aP2 involved in adipogenesis - was more inhibited by TRalpha1PV than by TRbeta1PV. Fatty Acids 77-87 lipoprotein lipase Mus musculus 104-122 20080985-8 2010 In addition, the expression of PPARgamma downstream target genes involved in fatty acid synthesis - the lipoprotein lipase (Lpl) and aP2 involved in adipogenesis - was more inhibited by TRalpha1PV than by TRbeta1PV. Fatty Acids 77-87 lipoprotein lipase Mus musculus 124-127 18647880-1 2008 Fatty acids (FAs) are acquired from free FA associated with albumin and lipoprotein triglyceride that is hydrolyzed by lipoprotein lipase (LpL). Fatty Acids 0-11 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). Fatty Acids 0-11 lipoprotein lipase Mus musculus 139-142 18647880-1 2008 Fatty acids (FAs) are acquired from free FA associated with albumin and lipoprotein triglyceride that is hydrolyzed by lipoprotein lipase (LpL). Fatty Acids 13-16 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). Fatty Acids 13-16 lipoprotein lipase Mus musculus 139-142 18647880-4 2008 The aim of this study was to examine the importance of LpL-derived FAs in hypertensive hypertrophied hearts. Fatty Acids 67-70 lipoprotein lipase Mus musculus 55-58 17971230-1 2007 BACKGROUND: A major portion of available fatty acids for adipocyte uptake is derived from lipoprotein lipase (LPL)-mediated hydrolysis of circulating lipoprotein particles. Fatty Acids 41-52 lipoprotein lipase Mus musculus 90-108 17189607-3 2007 One possible pathway is mediated by LPL, an enzyme that primarily hydrolyzes plasma triglyceride into fatty acids. Fatty Acids 102-113 lipoprotein lipase Mus musculus 36-39 17350593-7 2007 In conclusion, NO-1886 ameliorated and induced regression of experimental steatohepatitis via increasing endogenous LPL activation resulting in suppression on pro-inflammatory factors and reduction of hepatic fatty acids. Fatty Acids 209-220 lipoprotein lipase Mus musculus 116-119 15919836-10 2005 Despite normal hepatic TG secretion, the activity of lipoprotein lipase in epididymal fat was enhanced by the high-fat diet in the transgenic mice in a setting of decreased re-esterification and increased in situ fatty acid oxidation. Fatty Acids 213-223 lipoprotein lipase Mus musculus 53-71 17139480-5 2006 Loss of cardiac LpL forces the heart to increase its uptake of glucose, reduce fatty acid oxidation, and eventually leads to cardiac dysfunction. Fatty Acids 79-89 lipoprotein lipase Mus musculus 16-19 17139480-6 2006 In contrast, cardiomyocyte specific overexpression of an anchored form of LpL leads to excess lipid uptake, induction of fatty acid oxidation genes, and dilated cardiomyopathy. Fatty Acids 121-131 lipoprotein lipase Mus musculus 74-77 15028738-2 2004 The heart acquires fatty acids associated with albumin or derived from lipoprotein lipase (LpL)-mediated hydrolysis of lipoprotein triglyceride (TG). Fatty Acids 19-30 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). Fatty Acids 19-30 lipoprotein lipase Mus musculus 91-94 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. Fatty Acids 113-124 lipoprotein lipase Mus musculus 0-18 15013626-8 2004 In summary, these data show that the availability of fatty acids, resulting from the catabolism of VLDL by LPL, is required to promote the phenotypical differentiation of neuroblastoma cells. Fatty Acids 53-64 lipoprotein lipase Mus musculus 107-110 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. Fatty Acids 151-162 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. Fatty Acids 151-162 lipoprotein lipase Mus musculus 20-23 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. Fatty Acids 164-167 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. Fatty Acids 164-167 lipoprotein lipase Mus musculus 20-23 14685668-7 2003 LPL-mediated fatty acid and lipoprotein uptake is not sufficient to harm muscle tissue. Fatty Acids 13-23 lipoprotein lipase Mus musculus 0-3 12501246-1 2003 Lipoprotein lipase (LPL) is a key enzyme involved in the metabolism of lipoproteins, providing tissues like adipose tissue or skeletal muscle with fatty acids. Fatty Acids 147-158 lipoprotein lipase Mus musculus 0-18 12501246-1 2003 Lipoprotein lipase (LPL) is a key enzyme involved in the metabolism of lipoproteins, providing tissues like adipose tissue or skeletal muscle with fatty acids. Fatty Acids 147-158 lipoprotein lipase Mus musculus 20-23 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. Fatty Acids 113-124 lipoprotein lipase Mus musculus 20-23 11440913-3 2001 This heparin-releasable LPL pool remained constant over a variety of experimental conditions, including workload and fatty acid concentrations, making the mouse heart a suitable model to study chylomicron catabolism. Fatty Acids 117-127 lipoprotein lipase Mus musculus 24-27 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. Fatty Acids 131-142 lipoprotein lipase Mus musculus 105-108 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). Fatty Acids 122-133 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). Fatty Acids 122-133 lipoprotein lipase Mus musculus 97-100 11440913-7 2001 These results suggest that fatty acids produced from lipoprotein hydrolysis by the action of LPL and fatty acids from a fatty acid-albumin complex do not enter a common metabolic pool in the heart. Fatty Acids 27-38 lipoprotein lipase Mus musculus 93-96 11440913-7 2001 These results suggest that fatty acids produced from lipoprotein hydrolysis by the action of LPL and fatty acids from a fatty acid-albumin complex do not enter a common metabolic pool in the heart. Fatty Acids 27-37 lipoprotein lipase Mus musculus 93-96 11246888-0 2001 Direct regulatory effect of fatty acids on macrophage lipoprotein lipase: potential role of PPARs. Fatty Acids 28-39 lipoprotein lipase Mus musculus 54-72 11246888-11 2001 All FAs, with the exception of EPA and OA, increased extra- and intracellular LPL immunoreactive mass and activity. Fatty Acids 4-7 lipoprotein lipase Mus musculus 78-81 11257467-5 2001 The experimental fatty acids at low concentrations (<30 micromol/L) moderately increased intracellular and HR-LPL activity. Fatty Acids 17-28 lipoprotein lipase Mus musculus 113-116