PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 18779653-1 2008 We investigated the mechanism of spontaneous cholesterol efflux induced by acyl-coenzyme A:cholesterol acyltransferase (ACAT) inhibition, and how an alteration of cholesterol metabolism in macrophages impacts on that in HepG2 cells. Cholesterol 45-56 carboxylesterase 1 Homo sapiens 75-118 18779653-6 2008 The findings reported here provide new insight into mechanisms of spontaneous cholesterol efflux, and suggest that ACAT inhibition may stimulate cholesterol-catabolic (cytochrome P450) pathway in lesion-macrophages, in contrast, suppress it in hepatocyte via FXR induced by biliary cholesterol (BC). Cholesterol 78-89 carboxylesterase 1 Homo sapiens 115-119 18779653-1 2008 We investigated the mechanism of spontaneous cholesterol efflux induced by acyl-coenzyme A:cholesterol acyltransferase (ACAT) inhibition, and how an alteration of cholesterol metabolism in macrophages impacts on that in HepG2 cells. Cholesterol 45-56 carboxylesterase 1 Homo sapiens 120-124 18779653-6 2008 The findings reported here provide new insight into mechanisms of spontaneous cholesterol efflux, and suggest that ACAT inhibition may stimulate cholesterol-catabolic (cytochrome P450) pathway in lesion-macrophages, in contrast, suppress it in hepatocyte via FXR induced by biliary cholesterol (BC). Cholesterol 145-156 carboxylesterase 1 Homo sapiens 115-119 18779653-6 2008 The findings reported here provide new insight into mechanisms of spontaneous cholesterol efflux, and suggest that ACAT inhibition may stimulate cholesterol-catabolic (cytochrome P450) pathway in lesion-macrophages, in contrast, suppress it in hepatocyte via FXR induced by biliary cholesterol (BC). Cholesterol 145-156 carboxylesterase 1 Homo sapiens 115-119 18779653-1 2008 We investigated the mechanism of spontaneous cholesterol efflux induced by acyl-coenzyme A:cholesterol acyltransferase (ACAT) inhibition, and how an alteration of cholesterol metabolism in macrophages impacts on that in HepG2 cells. Cholesterol 91-102 carboxylesterase 1 Homo sapiens 120-124 16962139-2 2006 It has been implicated in a variety of endogenous cholesterol metabolism pathways including the following apparently disparate reactions: cholesterol ester hydrolysis (CEH), fatty acyl Coenzyme A hydrolysis (FACoAH), acyl-Coenzyme A:cholesterol acyltransfer (ACAT), and fatty acyl ethyl ester synthesis (FAEES). Cholesterol 50-61 carboxylesterase 1 Homo sapiens 168-171 18078940-7 2008 Since esterification of cholesterol is catalyzed by intestinal ACAT, and is a rate-limiting step in cholesterol absorption, it was concluded that the varying effects of CLA, LN, LA and CLN on blood cholesterol were mediated, at least in part, by their inhibition on intestinal ACAT activity. Cholesterol 24-35 carboxylesterase 1 Homo sapiens 63-67 18078940-7 2008 Since esterification of cholesterol is catalyzed by intestinal ACAT, and is a rate-limiting step in cholesterol absorption, it was concluded that the varying effects of CLA, LN, LA and CLN on blood cholesterol were mediated, at least in part, by their inhibition on intestinal ACAT activity. Cholesterol 24-35 carboxylesterase 1 Homo sapiens 277-281 18000807-0 2008 Androgen-mediated cholesterol metabolism in LNCaP and PC-3 cell lines is regulated through two different isoforms of acyl-coenzyme A:Cholesterol Acyltransferase (ACAT). Cholesterol 18-29 carboxylesterase 1 Homo sapiens 117-160 17950700-1 2007 Acyl-coenzyme A:cholesterol acyltransferase (ACAT) catalyzes the synthesis of cholesteryl esters from cholesterol and long-chain fatty acids. Cholesterol 16-27 carboxylesterase 1 Homo sapiens 45-49 17950700-2 2007 The two ACAT enzymes, ACAT1 and ACAT2, lack sterol regulatory elements in their promoters and have not been thought to be transcriptionally regulated by cellular cholesterol. Cholesterol 162-173 carboxylesterase 1 Homo sapiens 8-12 16971496-0 2007 Stable overexpression of human macrophage cholesteryl ester hydrolase results in enhanced free cholesterol efflux from human THP1 macrophages. Cholesterol 95-106 carboxylesterase 1 Homo sapiens 42-69 16971496-2 2007 Since extracellular cholesterol acceptor-mediated cholesterol efflux is the only recognized mechanism of cholesterol removal from foam cells and this process is rate limited at the level of intracellular cholesterol ester hydrolysis, a reaction catalyzed by neutral cholesteryl ester hydrolase (CEH), we examined the hypothesis that CEH overexpression in the human macrophage monocyte/macrophage cell line THP1 results in increased cholesterol efflux, as well as decreased cellular cholesterol ester accumulation. Cholesterol 20-31 carboxylesterase 1 Homo sapiens 266-293 16971496-2 2007 Since extracellular cholesterol acceptor-mediated cholesterol efflux is the only recognized mechanism of cholesterol removal from foam cells and this process is rate limited at the level of intracellular cholesterol ester hydrolysis, a reaction catalyzed by neutral cholesteryl ester hydrolase (CEH), we examined the hypothesis that CEH overexpression in the human macrophage monocyte/macrophage cell line THP1 results in increased cholesterol efflux, as well as decreased cellular cholesterol ester accumulation. Cholesterol 20-31 carboxylesterase 1 Homo sapiens 295-298 16971496-2 2007 Since extracellular cholesterol acceptor-mediated cholesterol efflux is the only recognized mechanism of cholesterol removal from foam cells and this process is rate limited at the level of intracellular cholesterol ester hydrolysis, a reaction catalyzed by neutral cholesteryl ester hydrolase (CEH), we examined the hypothesis that CEH overexpression in the human macrophage monocyte/macrophage cell line THP1 results in increased cholesterol efflux, as well as decreased cellular cholesterol ester accumulation. Cholesterol 20-31 carboxylesterase 1 Homo sapiens 333-336 16971496-2 2007 Since extracellular cholesterol acceptor-mediated cholesterol efflux is the only recognized mechanism of cholesterol removal from foam cells and this process is rate limited at the level of intracellular cholesterol ester hydrolysis, a reaction catalyzed by neutral cholesteryl ester hydrolase (CEH), we examined the hypothesis that CEH overexpression in the human macrophage monocyte/macrophage cell line THP1 results in increased cholesterol efflux, as well as decreased cellular cholesterol ester accumulation. Cholesterol 50-61 carboxylesterase 1 Homo sapiens 266-293 16971496-2 2007 Since extracellular cholesterol acceptor-mediated cholesterol efflux is the only recognized mechanism of cholesterol removal from foam cells and this process is rate limited at the level of intracellular cholesterol ester hydrolysis, a reaction catalyzed by neutral cholesteryl ester hydrolase (CEH), we examined the hypothesis that CEH overexpression in the human macrophage monocyte/macrophage cell line THP1 results in increased cholesterol efflux, as well as decreased cellular cholesterol ester accumulation. Cholesterol 50-61 carboxylesterase 1 Homo sapiens 295-298 16971496-2 2007 Since extracellular cholesterol acceptor-mediated cholesterol efflux is the only recognized mechanism of cholesterol removal from foam cells and this process is rate limited at the level of intracellular cholesterol ester hydrolysis, a reaction catalyzed by neutral cholesteryl ester hydrolase (CEH), we examined the hypothesis that CEH overexpression in the human macrophage monocyte/macrophage cell line THP1 results in increased cholesterol efflux, as well as decreased cellular cholesterol ester accumulation. Cholesterol 50-61 carboxylesterase 1 Homo sapiens 333-336 16971496-2 2007 Since extracellular cholesterol acceptor-mediated cholesterol efflux is the only recognized mechanism of cholesterol removal from foam cells and this process is rate limited at the level of intracellular cholesterol ester hydrolysis, a reaction catalyzed by neutral cholesteryl ester hydrolase (CEH), we examined the hypothesis that CEH overexpression in the human macrophage monocyte/macrophage cell line THP1 results in increased cholesterol efflux, as well as decreased cellular cholesterol ester accumulation. Cholesterol 50-61 carboxylesterase 1 Homo sapiens 266-293 16971496-2 2007 Since extracellular cholesterol acceptor-mediated cholesterol efflux is the only recognized mechanism of cholesterol removal from foam cells and this process is rate limited at the level of intracellular cholesterol ester hydrolysis, a reaction catalyzed by neutral cholesteryl ester hydrolase (CEH), we examined the hypothesis that CEH overexpression in the human macrophage monocyte/macrophage cell line THP1 results in increased cholesterol efflux, as well as decreased cellular cholesterol ester accumulation. Cholesterol 50-61 carboxylesterase 1 Homo sapiens 295-298 16971496-2 2007 Since extracellular cholesterol acceptor-mediated cholesterol efflux is the only recognized mechanism of cholesterol removal from foam cells and this process is rate limited at the level of intracellular cholesterol ester hydrolysis, a reaction catalyzed by neutral cholesteryl ester hydrolase (CEH), we examined the hypothesis that CEH overexpression in the human macrophage monocyte/macrophage cell line THP1 results in increased cholesterol efflux, as well as decreased cellular cholesterol ester accumulation. Cholesterol 50-61 carboxylesterase 1 Homo sapiens 333-336 16971496-2 2007 Since extracellular cholesterol acceptor-mediated cholesterol efflux is the only recognized mechanism of cholesterol removal from foam cells and this process is rate limited at the level of intracellular cholesterol ester hydrolysis, a reaction catalyzed by neutral cholesteryl ester hydrolase (CEH), we examined the hypothesis that CEH overexpression in the human macrophage monocyte/macrophage cell line THP1 results in increased cholesterol efflux, as well as decreased cellular cholesterol ester accumulation. Cholesterol 50-61 carboxylesterase 1 Homo sapiens 266-293 16971496-2 2007 Since extracellular cholesterol acceptor-mediated cholesterol efflux is the only recognized mechanism of cholesterol removal from foam cells and this process is rate limited at the level of intracellular cholesterol ester hydrolysis, a reaction catalyzed by neutral cholesteryl ester hydrolase (CEH), we examined the hypothesis that CEH overexpression in the human macrophage monocyte/macrophage cell line THP1 results in increased cholesterol efflux, as well as decreased cellular cholesterol ester accumulation. Cholesterol 50-61 carboxylesterase 1 Homo sapiens 295-298 16971496-2 2007 Since extracellular cholesterol acceptor-mediated cholesterol efflux is the only recognized mechanism of cholesterol removal from foam cells and this process is rate limited at the level of intracellular cholesterol ester hydrolysis, a reaction catalyzed by neutral cholesteryl ester hydrolase (CEH), we examined the hypothesis that CEH overexpression in the human macrophage monocyte/macrophage cell line THP1 results in increased cholesterol efflux, as well as decreased cellular cholesterol ester accumulation. Cholesterol 50-61 carboxylesterase 1 Homo sapiens 333-336 16971496-5 2007 Efflux of free or unesterified cholesterol by acetylated LDL-loaded THP1-CEH cells to ApoA-I by an ABCA1-dependent pathway or to HDL by an ABCG1-dependent pathway was significantly higher than that in THP1-WT cells. Cholesterol 31-42 carboxylesterase 1 Homo sapiens 73-76 16971496-6 2007 In addition, THP1-CEH cells accumulated significantly lower amount of esterified cholesterol. Cholesterol 81-92 carboxylesterase 1 Homo sapiens 18-21 16971496-7 2007 CEH overexpression, therefore, not only enhances cholesterol efflux but also reduces cellular accumulation of cholesteryl esters. Cholesterol 49-60 carboxylesterase 1 Homo sapiens 0-3 17123760-1 2007 Acyl-coenzyme A: cholesterol acyltransferase (ACAT) esterifies free cholesterol in the liver and the intestine. Cholesterol 17-28 carboxylesterase 1 Homo sapiens 46-50 16962139-2 2006 It has been implicated in a variety of endogenous cholesterol metabolism pathways including the following apparently disparate reactions: cholesterol ester hydrolysis (CEH), fatty acyl Coenzyme A hydrolysis (FACoAH), acyl-Coenzyme A:cholesterol acyltransfer (ACAT), and fatty acyl ethyl ester synthesis (FAEES). Cholesterol 50-61 carboxylesterase 1 Homo sapiens 259-263 16554527-1 2006 BACKGROUND: The enzyme acyl-coenzyme A:cholesterol acyltransferase (ACAT) esterifies cholesterol in a variety of tissues. Cholesterol 39-50 carboxylesterase 1 Homo sapiens 68-72 16832167-2 2006 RECENT FINDINGS: ACAT inhibitors decrease the intracellular conversion of free cholesterol into cholesteryl ester in a number of tissues, including intestine, liver and macrophages. Cholesterol 79-90 carboxylesterase 1 Homo sapiens 17-21 16503866-1 2005 Acyl-coenzyme A: cholesterol acyltransferase (ACAT) is an intracellular enzyme that catalyzes the formation of cholesterol esters from cholesterol and fatty acyl-coenzyme A. Cholesterol 17-28 carboxylesterase 1 Homo sapiens 46-50 16753029-3 2006 Excess cellular cholesterol is converted to cholesteryl esters by the enzyme acyl-coenzyme A:cholesterol acyltransferase (ACAT) 1 or is removed from a cell by cellular cholesterol efflux at the plasma membrane. Cholesterol 16-27 carboxylesterase 1 Homo sapiens 77-129 16753029-4 2006 A close relationship between the ACAT substrate pool and the cholesterol efflux pool is proposed. Cholesterol 61-72 carboxylesterase 1 Homo sapiens 33-37 16495773-2 2006 SMP-797 showed inhibitory effects on acyl-coenzyme A: cholesterol acyltransferase (ACAT) activities in various microsomes and in human cell lines, and hypocholesterolemic effects in rabbits fed a cholesterol-rich diet and hamsters fed a normal diet. Cholesterol 54-65 carboxylesterase 1 Homo sapiens 83-87 16503866-2 2005 Animal experiments showed that ACAT inhibitors reduce plasma cholesterol levels by suppressing absorption of dietary cholesterol and by suppressing the assembly and secretion of apolipoprotein B-containing lipoproteins such as very low density lipoprotein in liver and chylomicron in intestine. Cholesterol 61-72 carboxylesterase 1 Homo sapiens 31-35 16503866-2 2005 Animal experiments showed that ACAT inhibitors reduce plasma cholesterol levels by suppressing absorption of dietary cholesterol and by suppressing the assembly and secretion of apolipoprotein B-containing lipoproteins such as very low density lipoprotein in liver and chylomicron in intestine. Cholesterol 117-128 carboxylesterase 1 Homo sapiens 31-35 16081098-2 2005 We present and analyze crystal structures of hCE1 in complexes with the cholesterol-lowering drug mevastatin, the breast cancer drug tamoxifen, the fatty acyl ethyl ester (FAEE) analogue ethyl acetate, and the novel hCE1 inhibitor benzil. Cholesterol 72-83 carboxylesterase 1 Homo sapiens 45-49 16131527-0 2005 Human liver cholesteryl ester hydrolase: cloning, molecular characterization, and role in cellular cholesterol homeostasis. Cholesterol 99-110 carboxylesterase 1 Homo sapiens 12-39 16024911-6 2005 However, CEH had 2.5-fold higher activity when mixed droplets were used as substrate in an in vitro assay, consistent with the reported higher cholesterol efflux from cells containing mixed isotropic droplets. Cholesterol 143-154 carboxylesterase 1 Homo sapiens 9-12 15533865-12 2004 This ACAT inhibitor also caused a mild increase in LDL cholesterol. Cholesterol 55-66 carboxylesterase 1 Homo sapiens 5-9 15164335-8 2004 Hepatic ACAT activity but not the intestinal ACAT activity was associated with hepatic cholesterol concentration and percent cholesterol absorption. Cholesterol 87-98 carboxylesterase 1 Homo sapiens 8-12 15317807-2 2004 The extent of cholesterol esterification by the ER-resident protein, acyl-coenzyme A:cholesterol acyl-transferase (ACAT), has become the standard method for monitoring cholesterol transport to the ER and is assumed to reflect the regulatory pool of ER cholesterol. Cholesterol 14-25 carboxylesterase 1 Homo sapiens 69-113 15317807-2 2004 The extent of cholesterol esterification by the ER-resident protein, acyl-coenzyme A:cholesterol acyl-transferase (ACAT), has become the standard method for monitoring cholesterol transport to the ER and is assumed to reflect the regulatory pool of ER cholesterol. Cholesterol 14-25 carboxylesterase 1 Homo sapiens 115-119 15317807-2 2004 The extent of cholesterol esterification by the ER-resident protein, acyl-coenzyme A:cholesterol acyl-transferase (ACAT), has become the standard method for monitoring cholesterol transport to the ER and is assumed to reflect the regulatory pool of ER cholesterol. Cholesterol 85-96 carboxylesterase 1 Homo sapiens 115-119 15317807-2 2004 The extent of cholesterol esterification by the ER-resident protein, acyl-coenzyme A:cholesterol acyl-transferase (ACAT), has become the standard method for monitoring cholesterol transport to the ER and is assumed to reflect the regulatory pool of ER cholesterol. Cholesterol 85-96 carboxylesterase 1 Homo sapiens 115-119 15317807-9 2004 Therefore, cholesterol esterification by the ER-resident protein ACAT is dissociable from cholesterol transport to the cholesterol homeostatic machinery in the ER. Cholesterol 11-22 carboxylesterase 1 Homo sapiens 65-69 15164335-8 2004 Hepatic ACAT activity but not the intestinal ACAT activity was associated with hepatic cholesterol concentration and percent cholesterol absorption. Cholesterol 125-136 carboxylesterase 1 Homo sapiens 8-12 12837853-8 2003 These data establish the possibility that increased CE hydrolysis, mediated by CEH up-regulation, could represent an important mechanism to reduce the cholesterol burden of foam cells. Cholesterol 151-162 carboxylesterase 1 Homo sapiens 79-82 12725862-1 2003 Human carboxylesterase 1 (hCE1) is a broad-spectrum bioscavenger that plays important roles in narcotic metabolism, clinical prodrug activation, and the processing of fatty acid and cholesterol derivatives. Cholesterol 182-193 carboxylesterase 1 Homo sapiens 26-30 12725862-1 2003 Human carboxylesterase 1 (hCE1) is a broad-spectrum bioscavenger that plays important roles in narcotic metabolism, clinical prodrug activation, and the processing of fatty acid and cholesterol derivatives. Cholesterol 182-193 carboxylesterase 1 Homo sapiens 6-24 12773168-6 2003 hCE1 has also been reported to contain cholesteryl ester hydrolase, fatty acyl-CoA hydrolase and acyl-CoA:cholesterol acyltransferase activities, and thus appears to be involved in cholesterol metabolism. Cholesterol 106-117 carboxylesterase 1 Homo sapiens 0-4 12725862-5 2003 Further, we use our structure to identify tacrine derivatives that act as low-micromolar inhibitors of hCE1 and may provide new avenues for treating narcotic abuse and cholesterol-related diseases. Cholesterol 168-179 carboxylesterase 1 Homo sapiens 103-107 12437499-3 2002 Excess cholesterol is stored as cholesteryl ester through an esterification process regulated in part by acyl coenzyme A:cholesterol acyltransferase (ACAT). Cholesterol 7-18 carboxylesterase 1 Homo sapiens 105-148 12533546-0 2003 Cholesterol is superior to 7-ketocholesterol or 7 alpha-hydroxycholesterol as an allosteric activator for acyl-coenzyme A:cholesterol acyltransferase 1. Cholesterol 0-11 carboxylesterase 1 Homo sapiens 106-149 12533546-1 2003 We compared the abilities of cholesterol versus various oxysterols as substrate and/or as activator for the enzyme acyl-coenzyme A:cholesterol acyltransferase (ACAT), by monitoring the activity of purified human ACAT1 in response to sterols solubilized in mixed micelles or in reconstituted vesicles. Cholesterol 29-40 carboxylesterase 1 Homo sapiens 115-158 12437499-3 2002 Excess cholesterol is stored as cholesteryl ester through an esterification process regulated in part by acyl coenzyme A:cholesterol acyltransferase (ACAT). Cholesterol 7-18 carboxylesterase 1 Homo sapiens 150-154 12437499-4 2002 ACAT is found in many tissue types which require the storage of cholesterol. Cholesterol 64-75 carboxylesterase 1 Homo sapiens 0-4 11557507-8 2001 More specifically, LDLR expression, ACAT activity, and CEH activity appeared responsive to an increase in cholesterol degradation after increased CYP7A1 expression. Cholesterol 106-117 carboxylesterase 1 Homo sapiens 36-40 12049990-8 2002 Moreover, researchers are currently investigating the development of drugs directed at molecular targets, including cholesterol esterification and accumulation in macrophage foam cells (e.g., inhibiting acyl-coenzyme A : cholesterol acyltransferase), degradation of atherosclerotic plaque (e.g., decreasing the expression of matrix metalloproteinases), and reverse cholesterol transport (e.g., stimulating ATP-binding cassette transporter A1). Cholesterol 116-127 carboxylesterase 1 Homo sapiens 203-248 11684695-1 2002 Acyl-coenzyme A:cholesterol acyltransferase (ACAT) plays important roles in cellular cholesterol homeostasis and in the early stages of atherosclerosis. Cholesterol 16-27 carboxylesterase 1 Homo sapiens 45-49 11579092-7 2001 Cholesterol trafficking to acyl-coenzyme A:cholesterol acyltransferase (ACAT) was also defective in ASM knockout macrophages. Cholesterol 0-11 carboxylesterase 1 Homo sapiens 27-70 11579092-7 2001 Cholesterol trafficking to acyl-coenzyme A:cholesterol acyltransferase (ACAT) was also defective in ASM knockout macrophages. Cholesterol 0-11 carboxylesterase 1 Homo sapiens 72-76 11888294-1 2002 Acyl-coenzyme A:cholesterol acyltransferase (ACAT) is an enzyme involved in cellular cholesterol homeostasis and atherosclerosis. Cholesterol 16-27 carboxylesterase 1 Homo sapiens 45-49 11772425-4 2002 ACAT is present in a variety of tissues and is responsible for catalyzing the conversion of free cholesterol to the more readily stored cholesteryl esters. Cholesterol 97-108 carboxylesterase 1 Homo sapiens 0-4 11772425-6 2002 Partial ACAT inhibition with specific agents has resulted in lesion regression and decreased progression, whereas complete ACAT inhibition via genetic alterations has led to an exacerbation of cholesterol deposition in tissues in animal models. Cholesterol 193-204 carboxylesterase 1 Homo sapiens 123-127 11557507-8 2001 More specifically, LDLR expression, ACAT activity, and CEH activity appeared responsive to an increase in cholesterol degradation after increased CYP7A1 expression. Cholesterol 106-117 carboxylesterase 1 Homo sapiens 55-58 10903474-2 2000 Once inside the enterocytes, cholesterol is esterified by the action of acyl-coenzyme A:cholesterol acyltransferase (ACAT), assembled into chylomicrons, and secreted into the lymph. Cholesterol 29-40 carboxylesterase 1 Homo sapiens 72-115 11584272-4 2001 Acyl-coenzyme A:cholesterol acyltransferase (ACAT), the enzyme that catalyses the formation of cholesteryl esters, modulates the generation of Abeta through the tight control of the equilibrium between free cholesterol and cholesteryl esters. Cholesterol 16-27 carboxylesterase 1 Homo sapiens 45-49 11409902-1 2001 Cholesteryl ester hydrolase (CEH) is responsible for hydrolysis of stored cholesterol esters in macrophage foam cells and release of free cholesterol for high-density lipoprotein-mediated efflux. Cholesterol 74-85 carboxylesterase 1 Homo sapiens 0-27 11409902-1 2001 Cholesteryl ester hydrolase (CEH) is responsible for hydrolysis of stored cholesterol esters in macrophage foam cells and release of free cholesterol for high-density lipoprotein-mediated efflux. Cholesterol 74-85 carboxylesterase 1 Homo sapiens 29-32 11409902-6 2001 Analogous to other genes involved in macrophage cholesterol homeostasis, human CEH may also be regulated by PPAR. Cholesterol 48-59 carboxylesterase 1 Homo sapiens 79-82 11294643-1 2001 Fatty acyl CoA and cholesterol are the substrates for cholesteryl ester synthesis by acyl coenzyme A:cholesterol acyltransferase (ACAT). Cholesterol 19-30 carboxylesterase 1 Homo sapiens 85-128 11177212-7 2000 If the ACAT is associated with cholesterol absorption, the part of mechanisms by which CLA decreases serum cholesterol may involve down-regulation of intestinal ACAT activity. Cholesterol 31-42 carboxylesterase 1 Homo sapiens 7-11 10903474-2 2000 Once inside the enterocytes, cholesterol is esterified by the action of acyl-coenzyme A:cholesterol acyltransferase (ACAT), assembled into chylomicrons, and secreted into the lymph. Cholesterol 29-40 carboxylesterase 1 Homo sapiens 117-121 9242919-1 1997 Due to its presumed role in regulating cellular cholesterol homeostasis, and in various pathophysiological conditions, acyl-coenzyme A:cholesterol acyltransferase (ACAT) has attracted much attention. Cholesterol 48-59 carboxylesterase 1 Homo sapiens 119-162 11015575-5 2000 The full-length cDNA was sequenced and found to exhibit 76% homology (at the nucleotide and conceptually translated protein level) to hepatic CEH, an enzyme shown to be involved in hepatic cholesterol homeostasis and regulated by cholesterol at the transcription level via sterol response elements in the proximal promoter. Cholesterol 189-200 carboxylesterase 1 Homo sapiens 142-145 11015575-9 2000 Overexpression of human macrophage CEH resulted in an impairment of upregulation of low-density lipoprotein (LDL) receptor mRNA in Chinese hamster ovary (CHO-K1) cells grown in cholesterol-deficient environment. Cholesterol 177-188 carboxylesterase 1 Homo sapiens 35-38 10406948-10 1999 Inhibition of lysosomal hydrolysis with chloroquine abolished the effect measured on ACAT activity in the presence of LDL, suggesting that CE of LDL, but not free cholesterol, maintains cell cholesterol homeostasis. Cholesterol 191-202 carboxylesterase 1 Homo sapiens 85-89 9714140-8 1998 Cholesterol of exogenous origin has been shown to pass via the cell membrane before its esterification by ACAT. Cholesterol 0-11 carboxylesterase 1 Homo sapiens 106-110 9714140-9 1998 We postulate that this is not the case for endogenous cholesterol, which may have direct access to ACAT. Cholesterol 54-65 carboxylesterase 1 Homo sapiens 99-103 9610773-9 1998 Two other genes involved in cholesterol absorption and chylomicron secretion, namely acyl coenzyme A:cholesterol acyltransferase (ACAT) and microsomal triglyceride transfer protein (MTP) were also examined for segregation and similarly excluded. Cholesterol 28-39 carboxylesterase 1 Homo sapiens 130-134 9500571-4 1998 The subsequent esterification of [3H]cholesterol was reduced greater than 90% by each ACAT inhibitor. Cholesterol 37-48 carboxylesterase 1 Homo sapiens 86-90 9500571-5 1998 Similar results were obtained in cells in which ACAT activity was induced by preincubation either with 25-hydroxycholesterol and mevalonic acid or with CEase and bile salt mixed-micelles containing 100 micromol/L cholesterol. Cholesterol 113-124 carboxylesterase 1 Homo sapiens 48-52 9211065-1 1997 The conversion of cholesterol to an esterified storage form by the enzyme acyl-coenzyme A: cholesterol acyltransferase, is a critical component of sterol and membrane homeostasis and represents a significant step in atherogenesis. Cholesterol 18-29 carboxylesterase 1 Homo sapiens 74-118 9148923-2 1997 The rationale was that the acyl-coenzyme A:cholesterol acyltransferase (ACAT) in homogenates should have access only to cholesterol associated with the (rough) ER membrane fragments in which it resides. Cholesterol 43-54 carboxylesterase 1 Homo sapiens 72-76 9020103-8 1997 However, significant activity was detected from strains expressing human ACAT when cholesterol was equilibrated with the microsomal membranes. Cholesterol 83-94 carboxylesterase 1 Homo sapiens 73-77 9020103-9 1997 The human enzyme in yeast utilized cholesterol as the preferred sterol and was sensitive to competitive (S58035) and non-competitive (DuP 128) ACAT inhibitors. Cholesterol 35-46 carboxylesterase 1 Homo sapiens 143-147 9242919-1 1997 Due to its presumed role in regulating cellular cholesterol homeostasis, and in various pathophysiological conditions, acyl-coenzyme A:cholesterol acyltransferase (ACAT) has attracted much attention. Cholesterol 48-59 carboxylesterase 1 Homo sapiens 164-168 9242919-4 1997 In addition, we present a working model linking the presumed allosteric property of ACAT with cholesterol trafficking into and out of the endoplasmic reticulum. Cholesterol 94-105 carboxylesterase 1 Homo sapiens 84-88 8960784-0 1996 Effect of exogenous cholesterol and dithiothreitol on the activity of human liver microsomal acyl-coenzyme A:cholesterol acyltransferase (ACAT). Cholesterol 20-31 carboxylesterase 1 Homo sapiens 93-136 8960784-0 1996 Effect of exogenous cholesterol and dithiothreitol on the activity of human liver microsomal acyl-coenzyme A:cholesterol acyltransferase (ACAT). Cholesterol 20-31 carboxylesterase 1 Homo sapiens 138-142 8960784-4 1996 Experiments with [3H]cholesterol and [14C]oleoyl-CoA indicated the time course of equilibration of exogenous with endogenous cholesterol as ACAT substrates, and showed that ACAT activity could be accurately measured using [3H]cholesterol/Tween 80, providing that the concentration of endogenous microsomal cholesterol was also determined. Cholesterol 125-136 carboxylesterase 1 Homo sapiens 140-144 8960784-4 1996 Experiments with [3H]cholesterol and [14C]oleoyl-CoA indicated the time course of equilibration of exogenous with endogenous cholesterol as ACAT substrates, and showed that ACAT activity could be accurately measured using [3H]cholesterol/Tween 80, providing that the concentration of endogenous microsomal cholesterol was also determined. Cholesterol 125-136 carboxylesterase 1 Homo sapiens 173-177 8960784-4 1996 Experiments with [3H]cholesterol and [14C]oleoyl-CoA indicated the time course of equilibration of exogenous with endogenous cholesterol as ACAT substrates, and showed that ACAT activity could be accurately measured using [3H]cholesterol/Tween 80, providing that the concentration of endogenous microsomal cholesterol was also determined. Cholesterol 125-136 carboxylesterase 1 Homo sapiens 140-144 8960784-1 1996 Acyl-coenzyme A:cholesterol acyltransferase (ACAT) is the intracellular enzyme responsible for the esterification of cholesterol with long-chain fatty acyl-CoA derivatives and has been implicated in atherosclerosis and gallstone disease. Cholesterol 16-27 carboxylesterase 1 Homo sapiens 45-49 8960784-4 1996 Experiments with [3H]cholesterol and [14C]oleoyl-CoA indicated the time course of equilibration of exogenous with endogenous cholesterol as ACAT substrates, and showed that ACAT activity could be accurately measured using [3H]cholesterol/Tween 80, providing that the concentration of endogenous microsomal cholesterol was also determined. Cholesterol 125-136 carboxylesterase 1 Homo sapiens 173-177 8960784-5 1996 Pre-incubation of liver microsomes for 90 min in the presence of 2 mmol/l DTT and exogenous cholesterol/Tween 80 resulted in a 60% reduction in ACAT activity, compared with the corresponding activity when DTT was omitted. Cholesterol 92-103 carboxylesterase 1 Homo sapiens 144-148 8960784-6 1996 If microsomes were pre-incubated with DTT prior to the pre-incubation with exogenous cholesterol/Tween 80, an 85-90% reduction in ACAT activity occurred. Cholesterol 85-96 carboxylesterase 1 Homo sapiens 130-134 8960784-8 1996 These results indicate that the supply of cholesterol to the enzyme active site is an important factor in ACAT assays in vitro and that DTT has a major effect on this process, suggesting that these factors may be important in controlling ACAT activity in vivo. Cholesterol 42-53 carboxylesterase 1 Homo sapiens 106-110 8960784-8 1996 These results indicate that the supply of cholesterol to the enzyme active site is an important factor in ACAT assays in vitro and that DTT has a major effect on this process, suggesting that these factors may be important in controlling ACAT activity in vivo. Cholesterol 42-53 carboxylesterase 1 Homo sapiens 238-242 8960784-2 1996 The effects of exogenous cholesterol and dithiothreitol (DTT) on the ACAT activity of human liver microsomes have been determined. Cholesterol 25-36 carboxylesterase 1 Homo sapiens 69-73 8960784-4 1996 Experiments with [3H]cholesterol and [14C]oleoyl-CoA indicated the time course of equilibration of exogenous with endogenous cholesterol as ACAT substrates, and showed that ACAT activity could be accurately measured using [3H]cholesterol/Tween 80, providing that the concentration of endogenous microsomal cholesterol was also determined. Cholesterol 21-32 carboxylesterase 1 Homo sapiens 173-177 8960784-4 1996 Experiments with [3H]cholesterol and [14C]oleoyl-CoA indicated the time course of equilibration of exogenous with endogenous cholesterol as ACAT substrates, and showed that ACAT activity could be accurately measured using [3H]cholesterol/Tween 80, providing that the concentration of endogenous microsomal cholesterol was also determined. Cholesterol 125-136 carboxylesterase 1 Homo sapiens 140-144 8960784-4 1996 Experiments with [3H]cholesterol and [14C]oleoyl-CoA indicated the time course of equilibration of exogenous with endogenous cholesterol as ACAT substrates, and showed that ACAT activity could be accurately measured using [3H]cholesterol/Tween 80, providing that the concentration of endogenous microsomal cholesterol was also determined. Cholesterol 125-136 carboxylesterase 1 Homo sapiens 173-177 8543556-5 1995 In this study, we investigated the effect of cholesterol-feeding, which induces an increase in triglyceride and cholesteryl ester of the liver as a consequence of the induction of both intestinal and hepatic ACAT activities, on the secretion of VLDL. Cholesterol 45-56 carboxylesterase 1 Homo sapiens 208-212 8652654-3 1996 When HepG2 cells were loaded with cholesterol and 25-hydroxycholesterol, both the whole-cell ACAT activity and the microsomal ACAT activity were increased by 85.1% and 41.3%. Cholesterol 34-45 carboxylesterase 1 Homo sapiens 126-130 8652654-4 1996 In contrast, cholesterol depletion of HepG2 cells with compactin, a 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitor, resulted in a decrease in both the whole-cell and the microsomal ACAT activity by 46.4% and 58.3%. Cholesterol 13-24 carboxylesterase 1 Homo sapiens 192-196 8652654-7 1996 These results indicate that cholesterol-induced up-regulation of ACAT activity in HepG2 cells does not occur at the level of transcription, but rather at a posttranscriptional level. Cholesterol 28-39 carboxylesterase 1 Homo sapiens 65-69 8937522-8 1996 The activated transfer machinery appears to involve the Golgi apparatus and diverts cholesterol from the shuttle between acylcoenzyme A: cholesterol acyltransferase and neutral cholesteryl ester hydrolase (cholesteryl ester cycle). Cholesterol 84-95 carboxylesterase 1 Homo sapiens 177-204 8652654-3 1996 When HepG2 cells were loaded with cholesterol and 25-hydroxycholesterol, both the whole-cell ACAT activity and the microsomal ACAT activity were increased by 85.1% and 41.3%. Cholesterol 34-45 carboxylesterase 1 Homo sapiens 93-97 8608158-2 1996 IL1 enhanced cholesterol esterification by [14C]oleic acid and acyl-coenzyme A cholesterol acyl transferase activity in a dose-dependent manner. Cholesterol 13-24 carboxylesterase 1 Homo sapiens 63-107 8645354-4 1996 The presence of modified lipoprotein, or of 25-hydroxycholesterol, markedly increased cholesterol esterification in these cells and these effects were potently inhibited by the presence of the ACAT inhibitor, 447C88. Cholesterol 54-65 carboxylesterase 1 Homo sapiens 193-197 7493995-10 1995 This finding, along with earlier studies, suggests that cholesterol concentration in the endoplasmic reticulum may be the major determinant for regulating ACAT activity in the intact cells. Cholesterol 56-67 carboxylesterase 1 Homo sapiens 155-159 8407899-2 1993 Intracellularly, an essential element in forming cholesterol ester from cholesterol is the enzyme acyl-coenzyme A:cholesterol acyltransferase (ACAT). Cholesterol 49-60 carboxylesterase 1 Homo sapiens 98-141 7822296-1 1995 Acyl-coenzyme A:cholesterol acyltransferase (ACAT) is an intracellular enzyme that catalyzes the conjugation of long chain fatty acid and cholesterol to form cholesteryl esters. Cholesterol 16-27 carboxylesterase 1 Homo sapiens 45-49 8049197-9 1994 This is evidence that the mRNA of ACAT/carboxylesterase is induced by cholesterol loading. Cholesterol 70-81 carboxylesterase 1 Homo sapiens 34-38 8049197-10 1994 It is concluded from the data presented that ACAT/carboxylesterase is relevant for cellular cholesterol esterification in vivo. Cholesterol 92-103 carboxylesterase 1 Homo sapiens 45-49 7507110-5 1994 This reaction also stimulated the mobilization of cell surface-associated [3H]cholesterol and its utilization in the synthesis of [3H]cholesteryl esters via acyl coenzyme-A cholesterol acyltransferase (ACAT). Cholesterol 78-89 carboxylesterase 1 Homo sapiens 157-200 7507110-5 1994 This reaction also stimulated the mobilization of cell surface-associated [3H]cholesterol and its utilization in the synthesis of [3H]cholesteryl esters via acyl coenzyme-A cholesterol acyltransferase (ACAT). Cholesterol 78-89 carboxylesterase 1 Homo sapiens 202-206 8197480-1 1994 Acyl coenzyme A:cholesterol acyltransferase (ACAT) is an intracellular enzyme that catalyzes the formation of cholesterol esters from cholesterol and long-chain fatty acyl-coenzyme A. Cholesterol 16-27 carboxylesterase 1 Homo sapiens 45-49 7756263-0 1995 Role of bile salt-dependent cholesteryl ester hydrolase in the uptake of micellar cholesterol by intestinal cells. Cholesterol 82-93 carboxylesterase 1 Homo sapiens 28-55 7756263-1 1995 The bile salt-dependent cholesteryl ester hydrolase (CEH; EC 3.1.1.13) has been proposed to promote the intestinal absorption of both the free and esterified (FC, CE) forms of dietary cholesterol. Cholesterol 184-195 carboxylesterase 1 Homo sapiens 24-51 7756263-1 1995 The bile salt-dependent cholesteryl ester hydrolase (CEH; EC 3.1.1.13) has been proposed to promote the intestinal absorption of both the free and esterified (FC, CE) forms of dietary cholesterol. Cholesterol 184-195 carboxylesterase 1 Homo sapiens 53-56 7756263-4 1995 To test the ability of CEH to promote micellar cholesterol uptake in a CaCo2 system under more physiological conditions, an in vitro model was developed. Cholesterol 47-58 carboxylesterase 1 Homo sapiens 23-26 7756263-7 1995 The uptake of cholesterol that was derived from micellar CE was significantly increased 5-10-fold (p < 0.001) in Tr vs control cells as a result of the hydrolysis of the CE by the CEH and subsequent uptake of the liberated free cholesterol. Cholesterol 14-25 carboxylesterase 1 Homo sapiens 183-186 7822296-14 1995 Using this system, we have shown that cholesterol itself can serve as an ACAT activator in vitro, in addition to its role as an ACAT substrate. Cholesterol 38-49 carboxylesterase 1 Homo sapiens 73-77 7822296-14 1995 Using this system, we have shown that cholesterol itself can serve as an ACAT activator in vitro, in addition to its role as an ACAT substrate. Cholesterol 38-49 carboxylesterase 1 Homo sapiens 128-132 7822296-15 1995 The current work provides the experimental basis to hypothesize that, inside mammalian cells, cholesterol itself may serve as a physiological regulator of ACAT. Cholesterol 94-105 carboxylesterase 1 Homo sapiens 155-159 8577825-6 1995 Another area of development is that of acyl coenzyme A cholesterol acyltransferase inhibitors, i.e., drugs interfering with cholesterol esterification in tissues, particularly in the arterial wall; the major problem with these seems to be that of poor tolerability and of lack of definitive proof of plasma cholesterol reduction in humans. Cholesterol 124-135 carboxylesterase 1 Homo sapiens 39-82 8407899-2 1993 Intracellularly, an essential element in forming cholesterol ester from cholesterol is the enzyme acyl-coenzyme A:cholesterol acyltransferase (ACAT). Cholesterol 49-60 carboxylesterase 1 Homo sapiens 143-147 1418688-2 1992 When cholesterol and linoleic acid were used as the substrates, PEG-modified CEH synthesized cholesterol linoleate only in water-immiscible organic solvents. Cholesterol 5-16 carboxylesterase 1 Homo sapiens 77-80 8496932-3 1993 In order to further define the structural features necessary for potent inhibition of acyl-coenzyme A:cholesterol acyltransferase (ACAT) in vitro and cholesterol lowering in vivo, systematic study of bioisosteric replacements for the amide bond in our previously identified series of fatty acid anilide ACAT inhibitors was undertaken. Cholesterol 102-113 carboxylesterase 1 Homo sapiens 131-135 8434560-5 1993 Inhibition of acyl-coenzyme A:cholesterol acyltransferase (ACAT) may block intestinal cholesterol absorption and reduce synthesis of very-low-density lipoprotein (VLDL), while simultaneously enriching high-density lipoprotein (HDL) cholesterol. Cholesterol 30-41 carboxylesterase 1 Homo sapiens 59-63 8434560-5 1993 Inhibition of acyl-coenzyme A:cholesterol acyltransferase (ACAT) may block intestinal cholesterol absorption and reduce synthesis of very-low-density lipoprotein (VLDL), while simultaneously enriching high-density lipoprotein (HDL) cholesterol. Cholesterol 86-97 carboxylesterase 1 Homo sapiens 14-57 8434560-5 1993 Inhibition of acyl-coenzyme A:cholesterol acyltransferase (ACAT) may block intestinal cholesterol absorption and reduce synthesis of very-low-density lipoprotein (VLDL), while simultaneously enriching high-density lipoprotein (HDL) cholesterol. Cholesterol 86-97 carboxylesterase 1 Homo sapiens 59-63 8394386-6 1993 ACAT and acidic CE hydrolase activities were increased and neutral CE hydrolase activity was decreased, indicating that these enzymes are regulated by intracellular cholesterol enrichment. Cholesterol 165-176 carboxylesterase 1 Homo sapiens 0-4 8394386-6 1993 ACAT and acidic CE hydrolase activities were increased and neutral CE hydrolase activity was decreased, indicating that these enzymes are regulated by intracellular cholesterol enrichment. Cholesterol 165-176 carboxylesterase 1 Homo sapiens 16-28 8394386-6 1993 ACAT and acidic CE hydrolase activities were increased and neutral CE hydrolase activity was decreased, indicating that these enzymes are regulated by intracellular cholesterol enrichment. Cholesterol 165-176 carboxylesterase 1 Homo sapiens 67-79 2066675-6 1991 The capacity to esterify cholesterol, judged by the activity of acyl coenzyme A:cholesterol acyltransferase (ACAT), was similar in gallstone and gallstone-free patients (5.4 +/- 0.4 vs. 6.7 +/- 1.1 pmol/min per mg protein). Cholesterol 25-36 carboxylesterase 1 Homo sapiens 64-107 1736037-1 1992 Acyl-coenzyme A:cholesterol acyltransferase (ACAT) catalyzes the esterification of cholesterol in human mononuclear cells (MNC). Cholesterol 16-27 carboxylesterase 1 Homo sapiens 45-49 1639221-8 1992 ACAT is regulated mainly by the level of its substrate cholesterol. Cholesterol 55-66 carboxylesterase 1 Homo sapiens 0-4 2066675-6 1991 The capacity to esterify cholesterol, judged by the activity of acyl coenzyme A:cholesterol acyltransferase (ACAT), was similar in gallstone and gallstone-free patients (5.4 +/- 0.4 vs. 6.7 +/- 1.1 pmol/min per mg protein). Cholesterol 25-36 carboxylesterase 1 Homo sapiens 109-113 2066675-7 1991 In the presence of exogenous cholesterol, ACAT activity increased by more than fourfold in both groups. Cholesterol 29-40 carboxylesterase 1 Homo sapiens 42-46 34153284-3 2021 It has been proposed that Ces1d/CES1 might also catalyze cholesteryl ester (CE) hydrolysis in the liver and be responsible for the hydrolysis of high-density lipoprotein (HDL)-derived CE, thus contributing to the final step in the reverse cholesterol transport (RCT) pathway, where cholesterol is secreted from the liver into bile and feces, either directly or after conversion to water-soluble bile salts. Cholesterol 282-293 carboxylesterase 1 Homo sapiens 32-36 2086698-9 1990 These changes in ACAT activity in livers of patients with cholesterol gallstones are consistent with the known increase in the amount of free cholesterol secreted in the bile of these patients. Cholesterol 58-69 carboxylesterase 1 Homo sapiens 17-21 34234263-1 2021 A recent genome-wide copy number variations (CNVs) scan identified a 16q12.2 deletion that included the carboxylesterase 1 (CES1) gene, which is important in the metabolism of fatty acids and cholesterol. Cholesterol 192-203 carboxylesterase 1 Homo sapiens 104-122 34234263-1 2021 A recent genome-wide copy number variations (CNVs) scan identified a 16q12.2 deletion that included the carboxylesterase 1 (CES1) gene, which is important in the metabolism of fatty acids and cholesterol. Cholesterol 192-203 carboxylesterase 1 Homo sapiens 124-128 2199133-0 1990 Effects of the ACAT inhibitor CL 277,082 on cholesterol metabolism in humans. Cholesterol 44-55 carboxylesterase 1 Homo sapiens 15-19 34436484-0 2021 Acyl-Coenzyme A: Cholesterol Acyltransferase (ACAT) in Cholesterol Metabolism: From Its Discovery to Clinical Trials and the Genomics Era. Cholesterol 55-66 carboxylesterase 1 Homo sapiens 0-44 34436484-0 2021 Acyl-Coenzyme A: Cholesterol Acyltransferase (ACAT) in Cholesterol Metabolism: From Its Discovery to Clinical Trials and the Genomics Era. Cholesterol 55-66 carboxylesterase 1 Homo sapiens 46-50 34436484-1 2021 The purification and cloning of the acyl-coenzyme A: cholesterol acyltransferase (ACAT) enzymes and the sterol O-acyltransferase (SOAT) genes has opened new areas of interest in cholesterol metabolism given their profound effects on foam cell biology and intestinal lipid absorption. Cholesterol 178-189 carboxylesterase 1 Homo sapiens 36-80 34436484-1 2021 The purification and cloning of the acyl-coenzyme A: cholesterol acyltransferase (ACAT) enzymes and the sterol O-acyltransferase (SOAT) genes has opened new areas of interest in cholesterol metabolism given their profound effects on foam cell biology and intestinal lipid absorption. Cholesterol 178-189 carboxylesterase 1 Homo sapiens 82-86 34153284-3 2021 It has been proposed that Ces1d/CES1 might also catalyze cholesteryl ester (CE) hydrolysis in the liver and be responsible for the hydrolysis of high-density lipoprotein (HDL)-derived CE, thus contributing to the final step in the reverse cholesterol transport (RCT) pathway, where cholesterol is secreted from the liver into bile and feces, either directly or after conversion to water-soluble bile salts. Cholesterol 239-250 carboxylesterase 1 Homo sapiens 32-36 2575465-1 1989 The effect of ex vivo ischaemia at 37 degrees C on the activities of human hepatic acyl-CoA:cholesterol acyltransferase (ACAT), acyl-CoA hydrolase and carboxylesterase and on the microsomal cholesterol and total phospholipid concentrations was determined in liver tissue from two patients. Cholesterol 92-103 carboxylesterase 1 Homo sapiens 121-125 35013861-5 2022 RESULT: In this study, we found medicinal plants and their bioactive components suppress foam cell formation in a variety of ways; some inhibit cholesterol transporter and lectin-like oxidized low-density lipoprotein receptor-1 upregulation, while others inhibit the function of acyl CoA: cholesterol acyltransferase activity, and neutral cholesteryl ester hydrolase activity. Cholesterol 144-155 carboxylesterase 1 Homo sapiens 339-366 2760547-9 1989 This finding indicates that hepatic ACAT in humans can also utilize exogenous cholesterol as substrate. Cholesterol 78-89 carboxylesterase 1 Homo sapiens 36-40 2760547-7 1989 The enhanced ACAT activity obtained by freezing was at least partly explained by a transfer of unesterified cholesterol to the microsomal fraction and possibly also by making the substrate(s) more available to the enzyme. Cholesterol 108-119 carboxylesterase 1 Homo sapiens 13-17 2760547-10 1989 Addition of cholesterol to frozen microsomes prepared from unfrozen liver tissue increased the ACAT activity two- to threefold, whereas addition of cholesterol to microsomes prepared from frozen liver tissue did not further increase the enzyme activity. Cholesterol 12-23 carboxylesterase 1 Homo sapiens 95-99 3244018-5 1988 Exogenous cholesterol in the liposomes was absolutely necessary for providing ACAT activity, but not for incorporation of the ACAT enzyme into the vesicle bilayer. Cholesterol 10-21 carboxylesterase 1 Homo sapiens 78-82 4006035-4 1985 Upon reacting with CEH 6-pyrenylhexanoic acid and free cholesterol are formed. Cholesterol 55-66 carboxylesterase 1 Homo sapiens 19-22 2990593-1 1985 Acyl coenzyme A : cholesterol acyltransferase (ACAT), the enzyme catalyzing the hepatic cholesterol esterification, could be involved in the modified availability of cholesterol detectable in proliferating systems. Cholesterol 18-29 carboxylesterase 1 Homo sapiens 47-51 2853367-10 1988 In addition, the regulation of cholesteryl ester hydrolase, as well as of other enzymes involved the metabolism of cholesterol, seems to involve post-translational modifications (e.g., phosphorylation). Cholesterol 115-126 carboxylesterase 1 Homo sapiens 31-58 6651782-1 1983 Membranes prepared from cultured fibroblasts were assayed for acyl-coenzyme A: cholesterol acyltransferase (ACAT) by a method that relied exclusively on the cholesterol already present on the membranes as the sterol substrate. Cholesterol 79-90 carboxylesterase 1 Homo sapiens 108-112 6651782-0 1983 The effects of low-density lipoprotein and cholesterol on acyl-coenzyme A: cholesterol acyltransferase activity in membranes from cultured human fibroblasts. Cholesterol 43-54 carboxylesterase 1 Homo sapiens 58-102 6651782-5 1983 In contrast with these effects of LDL, incubation of the cells with non-esterified cholesterol produced a prolonged increase in ACAT activity and an increase in the activity observed after equilibration. Cholesterol 83-94 carboxylesterase 1 Homo sapiens 128-132 6405661-3 1983 However, when rat serum cholesterol was determined, CEH-2 yielded a value significantly lower when compared to the four other CEH. Cholesterol 24-35 carboxylesterase 1 Homo sapiens 52-55 7421586-2 1980 The enzyme, acyl-coenzyme A:cholesterol acyltransferase (ACAT), is responsible for the intracellular esterification of cholesterol. Cholesterol 28-39 carboxylesterase 1 Homo sapiens 57-61 7421586-5 1980 Using labeled oleoyl CoA and the endogenous cholesterol as reactants, ACAT was detected in fresh samples of human liver obtained from patients undergoing staging laparotomy for Hodgkin"s disease. Cholesterol 44-55 carboxylesterase 1 Homo sapiens 70-74 971353-1 1976 Cholesteryl ester hydrolase activity was measured in the microsomal and supernatant fractions of the aorta of atherosclerosis-susceptible White Carneau and atherosclerosis-resistant Show Racer pigeons while on their normal cholesterol-free diets. Cholesterol 223-234 carboxylesterase 1 Homo sapiens 0-27 477221-2 1979 In the presence of CoA and ATP, human liver microsomes catalyse the incorporation of [14C]oleate or [14C]cholesterol into cholesteryl oleate, thus demonstrating the presence of acyl-coenzyme A-cholesterol acyltransferase (cholesterol acyltransferase) in human liver. Cholesterol 105-116 carboxylesterase 1 Homo sapiens 177-220 29321244-2 2018 We recently reported that silencing expression of carboxylesterase 1 (CES1) in human THP-1 macrophages [CES1KD (THP-1 cells with CES1 expression knocked down) macrophages] reduced cholesterol uptake and decreased expression of CD36 and scavenger receptor-A in cells loaded with acetylated low-density lipoprotein (acLDL). Cholesterol 180-191 carboxylesterase 1 Homo sapiens 50-68 32466188-2 2020 Since the carboxylesterase gene family plays a crucial role in xenobiotic metabolism and lipid/cholesterol homeostasis, we hypothesize that genetic variants in carboxylesterase genes may influence clinical outcomes for prostate cancer patients. Cholesterol 95-106 carboxylesterase 1 Homo sapiens 10-26 32466188-2 2020 Since the carboxylesterase gene family plays a crucial role in xenobiotic metabolism and lipid/cholesterol homeostasis, we hypothesize that genetic variants in carboxylesterase genes may influence clinical outcomes for prostate cancer patients. Cholesterol 95-106 carboxylesterase 1 Homo sapiens 160-176 32258948-5 2020 Human CES1 also reduced hepatic-free cholesterol levels and induced low-density lipoprotein receptor. Cholesterol 37-48 carboxylesterase 1 Homo sapiens 6-10 30901224-7 2019 Furthermore, dysregulation of CPS1, ASL, and ARG1, key enzymes involved in urea cycle, together with Annexin A6 and CES1, major proteins in regulating cholesterol homeostasis and fatty acid ester metabolism, was verified using immunohistochemical staining. Cholesterol 151-162 carboxylesterase 1 Homo sapiens 116-120 29247837-8 2018 PAF activated cholesterol ester hydrolases (CEH), enzymes that released cholesterol from stores of cholesterol esters. Cholesterol 14-25 carboxylesterase 1 Homo sapiens 44-47 29321244-2 2018 We recently reported that silencing expression of carboxylesterase 1 (CES1) in human THP-1 macrophages [CES1KD (THP-1 cells with CES1 expression knocked down) macrophages] reduced cholesterol uptake and decreased expression of CD36 and scavenger receptor-A in cells loaded with acetylated low-density lipoprotein (acLDL). Cholesterol 180-191 carboxylesterase 1 Homo sapiens 70-74 29050765-8 2017 Also, MARCO and COLEC12, affecting phagocytosis, and CES1, associated with an increase in free cholesterol, were down-regulated. Cholesterol 95-106 carboxylesterase 1 Homo sapiens 53-57 29321244-2 2018 We recently reported that silencing expression of carboxylesterase 1 (CES1) in human THP-1 macrophages [CES1KD (THP-1 cells with CES1 expression knocked down) macrophages] reduced cholesterol uptake and decreased expression of CD36 and scavenger receptor-A in cells loaded with acetylated low-density lipoprotein (acLDL). Cholesterol 180-191 carboxylesterase 1 Homo sapiens 104-108 29321244-10 2018 These results are consistent with a model in which abrogation of CES1 function attenuates the CYP27A1-LXRalpha-ABCA1 signaling axis by depleting endogenous ligands for the nuclear receptors PPARgamma, RAR, and/or RXR that regulate cholesterol homeostasis. Cholesterol 231-242 carboxylesterase 1 Homo sapiens 65-69 24051439-2 2013 The assay is based on Allain"s method of spectrophotometric determination of cholesterol by means of cholesterol oxidase, peroxidase, but using 3,5-dichloro-dihydroxybenzenesulfonic acid (DHBS) as phenolic chromogen and human serum as a source of substrate for the CEH as a novelty. Cholesterol 77-88 carboxylesterase 1 Homo sapiens 265-268 28349866-3 2017 Given the central role of hepatic cholesteryl ester hydrolase (CEH) in the intrahepatic hydrolysis of CE and subsequent removal of the resulting free cholesterol (FC), in this work, we applied galactose-functionalized polyamidoamine (PAMAM) dendrimer generation 5 (Gal-G5) for hepatocyte-specific delivery of CEH expression vector. Cholesterol 150-161 carboxylesterase 1 Homo sapiens 34-61 28349866-3 2017 Given the central role of hepatic cholesteryl ester hydrolase (CEH) in the intrahepatic hydrolysis of CE and subsequent removal of the resulting free cholesterol (FC), in this work, we applied galactose-functionalized polyamidoamine (PAMAM) dendrimer generation 5 (Gal-G5) for hepatocyte-specific delivery of CEH expression vector. Cholesterol 150-161 carboxylesterase 1 Homo sapiens 63-66 29911769-1 2017 Carboxylesterase 1 (CE1) is an important serine hydrolase in mammals, which involved in the hydrolysis of a variety of compounds (endogenous substrates like cholesterol and xenobiotic compounds like ester-contain drugs and pesticides). Cholesterol 157-168 carboxylesterase 1 Homo sapiens 0-18 29911769-1 2017 Carboxylesterase 1 (CE1) is an important serine hydrolase in mammals, which involved in the hydrolysis of a variety of compounds (endogenous substrates like cholesterol and xenobiotic compounds like ester-contain drugs and pesticides). Cholesterol 157-168 carboxylesterase 1 Homo sapiens 20-23 23744992-3 2013 Earlier, we demonstrated that overexpression of human CE hydrolase (Gene symbol CES1) increased bile acid synthesis in human hepatocytes and enhanced reverse cholesterol transport in mice. Cholesterol 158-169 carboxylesterase 1 Homo sapiens 80-84 24512105-10 2014 The enzyme encoded by CES1 is a major liver enzyme that typically catalyzes the decomposition of ester into alcohol and carboxylic acid and is involved in drug or xenobiotics, fatty acid, and cholesterol metabolisms. Cholesterol 192-203 carboxylesterase 1 Homo sapiens 22-26 24028971-3 2013 Acyl-coenzyme A:cholesterol acyltransferase (ACAT) is a key enzyme in cellular cholesterol metabolism. Cholesterol 16-27 carboxylesterase 1 Homo sapiens 45-49 21081832-7 2011 The mRNA levels of CES1 were positively correlated with various measures of adiposity, particularly those estimated by CT in the three depots; they were also positively correlated with plasma LDL-cholesterol levels in omental fat. Cholesterol 196-207 carboxylesterase 1 Homo sapiens 19-23 22262001-0 2012 Early steps in reverse cholesterol transport: cholesteryl ester hydrolase and other hydrolases. Cholesterol 23-34 carboxylesterase 1 Homo sapiens 47-74 23468884-1 2013 CONTEXT AND AIMS: Carboxylesterase 1 (CES1) appears to play an important role in the control of the metabolism of triglycerides and cholesterol in adipocytes and other cell types including hepatocytes. Cholesterol 132-143 carboxylesterase 1 Homo sapiens 18-36 23468884-1 2013 CONTEXT AND AIMS: Carboxylesterase 1 (CES1) appears to play an important role in the control of the metabolism of triglycerides and cholesterol in adipocytes and other cell types including hepatocytes. Cholesterol 132-143 carboxylesterase 1 Homo sapiens 38-42 20947831-5 2010 METHODS AND RESULTS: We compared the expression of NCEH1, LIPE, and cholesterol ester hydrolase (CES1) in human monocyte-derived macrophages (HMMs) and examined the effects of inhibition or overexpression of each enzyme in the cholesterol trafficking. Cholesterol 68-79 carboxylesterase 1 Homo sapiens 97-101 19878739-4 2010 CEH, therefore, regulates the process of reverse cholesterol transport and ultimate elimination of cholesterol from the body. Cholesterol 49-60 carboxylesterase 1 Homo sapiens 0-3 20530478-5 2010 CES1 is an endogenous liver protein involved in processing of triglycerides and cholesterol. Cholesterol 80-91 carboxylesterase 1 Homo sapiens 0-4 19878739-4 2010 CEH, therefore, regulates the process of reverse cholesterol transport and ultimate elimination of cholesterol from the body. Cholesterol 99-110 carboxylesterase 1 Homo sapiens 0-3 18762277-2 2008 Hence, CEH has an important regulatory role in macrophage reverse cholesterol transport (RCT). Cholesterol 66-77 carboxylesterase 1 Homo sapiens 7-10 19293413-1 2009 CONTEXT: Inhibition of acyl coenzyme A:cholesterol acyltransferase (ACAT), an intracellular enzyme involved in cholesterol accumulation, with pactimibe was developed to assist in the prevention of cardiovascular disease. Cholesterol 39-50 carboxylesterase 1 Homo sapiens 68-72 20403742-1 2009 Carboxylesterases (CES) are responsible for the detoxification of a wide range of drugs and xenobiotics, and may contribute to cholesterol, fatty acid and lung surfactant metabolism. Cholesterol 127-138 carboxylesterase 1 Homo sapiens 0-17 19062296-3 2009 In addition, carboxylesterases are involved in lipid homeostasis, including cholesterol metabolism and transport with a proposed role in the development of atherosclerosis. Cholesterol 76-87 carboxylesterase 1 Homo sapiens 13-30 18762277-1 2008 Cholesteryl esters are hydrolyzed by cholesteryl ester hydrolase (CEH) yielding free cholesterol for export from macrophages. Cholesterol 85-96 carboxylesterase 1 Homo sapiens 37-64 18762277-1 2008 Cholesteryl esters are hydrolyzed by cholesteryl ester hydrolase (CEH) yielding free cholesterol for export from macrophages. Cholesterol 85-96 carboxylesterase 1 Homo sapiens 66-69