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Carboxylesterase 1

Carboxylesterase, REH
This gene encodes a member of the carboxylesterase large family. The family members are responsible for the hydrolysis or transesterification of various xenobiotics, such as cocaine and heroin, and endogenous substrates with ester, thioester, or amide bonds. They may participate in fatty acyl and cholesterol ester metabolism, and may play a role in the blood-brain barrier system. This enzyme is the major liver enzyme and functions in liver drug clearance. Mutations of this gene cause carboxylesterase 1 deficiency. Three transcript variants encoding three different isoforms have been found for this gene. [provided by RefSeq, Jun 2010] (from NCBI)
Top mentioned proteins: ESI, ACID, CAN, acetylcholinesterase, HAD
Papers using Carboxylesterase antibodies
Gene set enrichment analysis: A knowledge-based approach for interpreting genome-wide expression profiles.
Jeang K. T., In PLoS ONE, 2004
... Total RNA was isolated from biological replicates of E/R-silenced REH (n = 3) and AT-2 (n = 3) cells obtained from independent KD experiments by Trizol reagent (Life Technologies, Carlsbad, CA) ...
Papers on Carboxylesterase
Prognostic impact of carboxylesterase 1 gene variants in patients with congestive heart failure treated with angiotensin-converting enzyme inhibitors.
Hansen et al., Aalborg, Denmark. In Pharmacogenet Genomics, 12 Feb 2016
OBJECTIVE: Most angiotensin-converting enzyme inhibitors (ACEIs) are prodrugs activated by carboxylesterase 1 (CES1).
Gambogic acid potentiates clopidogrel-induced apoptosis and attenuates irinotecan-induced apoptosis through down-regulating human carboxylesterase 1 and -2.
Yang et al., Nanjing, China. In Xenobiotica, 10 Feb 2016
In this study, we report that gambogic acid (GA), a promising anticancer agent, potentiates clopidogrel-induced apoptosis and attenuates CPT-11-induced apoptosis by down-regulating human carboxylesterase (CES) 1 and -2 via ERK and p38 MAPK pathway activation, which provides a molecular explanation linking the effect of drug combination directly to the decreased capacity of hydrolytic biotransformation.
ω-Imidazolyl- and ω-Tetrazolylalkylcarbamates as Inhibitors of Fatty Acid Amide Hydrolase: Biological Activity and in vitro Metabolic Stability.
Lehr et al., Münster, Germany. In Chemmedchem, 06 Feb 2016
With the aid of esterase inhibitors it was shown that in porcine plasma, carboxylesterase-like enzymes and paraoxonase are involved in carbamate cleavage.
Highly sensitive and selective detection of human carboxylesterase 1 activity by liquid chromatography with fluorescence detection.
Yang et al., Dalian, China. In J Chromatogr B Analyt Technol Biomed Life Sci, 01 Feb 2016
Human carboxylesterases 1 (hCE1), one of the most important human drug metabolizing enzymes, catalyzes the hydrolysis of a large number of structurally diverse of endogenous and exogenous substrates.
Selective production of 1-monocaprin by porcine liver carboxylesterase-catalyzed esterification: Its enzyme kinetics and catalytic performance.
Chang et al., Seoul, South Korea. In Enzyme Microb Technol, 31 Jan 2016
Porcine liver carboxylesterase (PLE) belongs to carboxylesterase family (EC
Arylacetamide Deacetylase Is Responsible for Activation of Prasugrel in Human and Dog.
Nakajima et al., Kanazawa, Japan. In Drug Metab Dispos, 30 Jan 2016
It is efficiently hydrolyzed in the intestine after oral administration, and the enzyme responsible for the hydrolysis in human was demonstrated to be carboxylesterase (CES) 2. Prasugrel hydrolase activity is detected in dog intestine where CES enzymes are absent, so this prompted us to investigate the involvement of enzyme(s) other than CES.
Differential Mechanisms of Tenofovir and Tenofovir Disoproxil Fumarate Cellular Transport and Implications for Topical Pre-exposure Prophylaxis.
Herold et al., United States. In Antimicrob Agents Chemother, 28 Jan 2016
The carboxylesterase inhibitor bis-nitrophenyl phosphate reduced TDF uptake, suggesting saturability of intracellular carboxylesterases.
Effects of chlorpyrifos on enzymatic systems of Cydia pomonella (Lepidoptera: Tortricidae) adults.
Montagna et al., Neuquén, Argentina. In Insect Sci, 25 Jan 2016
The FP displayed higher carboxylesterase (CarE) and 7-ethoxycoumarine O-deethylase (ECOD) activities than LSS.
Synthesis and evaluation of atorvastatin esters as prodrugs metabolically activated by human carboxylesterases.
Hosokawa et al., Chiba, Japan. In Bioorg Med Chem Lett, 19 Jan 2016
We discovered that they underwent metabolic activation specifically by the human carboxylesterase 1 (CES1) isozyme.
Alkyl 2-arylhydrazinylidene-3-oxo-3-polyfluoroalkylpropionates as new effective and selective inhibitors of carboxylesterase.
Chupakhin et al., Moscow, Russia. In Dokl Biochem Biophys, Nov 2015
A series of alkyl 2-Arylhydrazinylidene-3-oxo-3-polyfluoroalkylpropionates was synthesized and their inhibitory activity with respect to porcine liver carboxylesterase (CaE, EC,
Notum deacylates Wnt proteins to suppress signalling activity.
Vincent et al., Potters Bar, United Kingdom. In Nature, Apr 2015
Kinetic and mass spectrometric analyses of human proteins show that Notum is a carboxylesterase that removes an essential palmitoleate moiety from Wnt proteins and thus constitutes the first known extracellular protein deacylase.
Metabolomics identifies an inflammatory cascade involved in dioxin- and diet-induced steatohepatitis.
Gonzalez et al., Bethesda, United States. In Cell Metab, 2012
Serum metabolomics identified azelaic acid monoesters as significantly increased metabolites after TCDD treatment, due to downregulation of hepatic carboxylesterase 3 (CES3, also known as triglyceride hydrolase) expression in an arylhydrocarbon receptor (AhR)-dependent manner in mice.
Identification of a novel intracellular cholesteryl ester hydrolase (carboxylesterase 3) in human macrophages: compensatory increase in its expression after carboxylesterase 1 silencing.
Ghosh et al., Richmond, United States. In Am J Physiol Cell Physiol, 2012
This study provides the first evidence of functional compensation whereby increased expression of CES3 restores intracellular cholesteryl ester hydrolytic activity and free cholesterol efflux in CES1-deficient cells.
Carboxylesterase 1 polymorphism impairs oseltamivir bioactivation in humans.
Niemi et al., Helsinki, Finland. In Clin Pharmacol Ther, 2012
Genetic variability in Carboxylesterase 1 affects the pharmacokinetics of oseltamivir and indicate that CES1 plays an important role in the bioactivation of oseltamivir in humans.
Examination of the carboxylesterase phenotype in human liver.
Xie et al., United States. In Arch Biochem Biophys, 2012
tested the hypothesis that an individual's CES phenotype can be characterized by reporter substrates/probes that interrogate native CES1 and CES2 activities in liver and immunoblotting methods
A discriminative analytical method for detection of CES1A1 and CES1A2/CES1A3 genetic variants.
Markowitz et al., Gainesville, United States. In Pharmacogenet Genomics, 2012
The comparison of the genotyping results between this novel assay and those previously reported methods highlighted the necessity of applying the discriminative genotyping assay in pharmacogenetic studies involving CES1 gene.
Depot-specific expression of lipolytic genes in human adipose tissues--association among CES1 expression, triglyceride lipase activity and adiposity.
Ishibashi et al., Tochigi, Japan. In J Atheroscler Thromb, 2010
High mRNA levels of CES1 is associated with adiposity and lipolysis, thereby contributing to the development of obesity-associated phenotypes.
Loss of TGH/Ces3 in mice decreases blood lipids, improves glucose tolerance, and increases energy expenditure.
Lehner et al., Edmonton, Canada. In Cell Metab, 2010
Here we show that ablation of carboxylesterase 3 (Ces3)/triacylglycerol hydrolase (TGH) expression in mice (Tgh(-/-)) results in decreased plasma triacylglycerol, apolipoprotein B, and fatty acid levels in both fasted and fed states.
Enzyme-catalyzed activation of anticancer prodrugs.
Vermeulen et al., Amsterdam, Netherlands. In Pharmacol Rev, 2004
The following endogenous enzymes are discussed: aldehyde oxidase, amino acid oxidase, cytochrome P450 reductase, DT-diaphorase, cytochrome P450, tyrosinase, thymidylate synthase, thymidine phosphorylase, glutathione S-transferase, deoxycytidine kinase, carboxylesterase, alkaline phosphatase, beta-glucuronidase and cysteine conjugate beta-lyase.
Modulation of irinotecan metabolism by ketoconazole.
Sparreboom et al., Rotterdam, Netherlands. In J Clin Oncol, 2002
RESULTS: With ketoconazole coadministration, the relative formation of APC was reduced by 87% (P =.002), whereas the relative exposure to the carboxylesterase-mediated SN-38 as expected on the basis of dose (area under the plasma concentration-time curve normalized to dose) was increased by 109% (P =.004).
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