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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
Inhibition behavior of fructus psoraleae's ingredients towards human carboxylesterase 1 (hCES1).
Fang et al., Shenyang, China. In Xenobiotica, 11 Dec 2015
The present study aims to determine the inhibition of human carboxylesterase 1 (CES1) by FP's major ingredients, including neobavaisoflavone, corylifolinin, coryfolin, psoralidin, corylin and bavachinin.
Human Intestinal Raf Kinase Inhibitor Protein, RKIP, Catalyzes Prasugrel as a Bioactivation Hydrolase.
Atsushi et al., Novara, Italy. In Drug Metab Dispos, 11 Dec 2015
UNASSIGNED: Prasugrel is a thienopyridine antiplatelet prodrug that undergoes rapid hydrolysis in vivo to a thiolactone metabolite by human carboxylesterase-2 (hCE2) during gastrointestinal absorption.
An in vitro screening with emerging contaminants reveals inhibition of carboxylesterase activity in aquatic organisms.
Sanchez-Hernandez et al., Barcelona, Spain. In Aquat Toxicol, 04 Dec 2015
Herein, an in vitro enzyme trial was performed to explore sensitivity of carboxylesterase (CE) activity of aquatic organisms to fourteen PPCPs.
The activity of detoxifying enzymes in the infective juveniles of Heterorhabditis bacteriophora strains: Purification and characterization of two acetylcholinesterases.
Ghanem et al., Cairo, Egypt. In Comp Biochem Physiol C Toxicol Pharmacol, 03 Dec 2015
UNASSIGNED: The infectivity and detoxifying enzyme activities including glutathione-S-transferase (GST), acetylcholinesterase (AChE) and carboxylesterase (CaE) are investigated in the infective juveniles (IJs) of six different strains of Heterorhabditis bacteriophora as a biocontrol agent against insect pests.
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.
A comprehensive review of UDP-glucuronosyltransferase and esterases for drug development.
Nakajima et al., Nagoya, Japan. In Drug Metab Pharmacokinet, Feb 2015
In the field of esterases, it is becoming clear that enzymes other than carboxylesterase are involved in drug hydrolysis.
Quantitative Proteomics Analysis of the Hepatitis C Virus Replicon High-Permissive and Low-Permissive Cell Lines.
Peng et al., Beijing, China. In Plos One, Dec 2014
The differential expression of Glutathione S-transferase P (GSTP1), Ubiquitin carboxyl-terminal hydrolase isozyme L1 (UCHL1), carboxylesterase 1 (CES1), vimentin, Proteasome activator complex subunit1 (PSME1), and Cathepsin B (CTSB) were verified by western blot.
Pharmacokinetic drug interactions with clopidogrel: updated review and risk management in combination therapy.
Zhou et al., Hangzhou, China. In Ther Clin Risk Manag, Dec 2014
The mechanism of the DDIs with clopidogrel involves modulating CYP enzymes (eg, CYP2B6, CYP2C8, CYP2C19, and CYP3A4), paraoxonase-1, hepatic carboxylesterase 1, P-glycoprotein, and organic anion transporter family member 1B1.
Chromatographic and electrophoretic strategies for the chiral separation and quantification of d- and l-threo methylphenidate in biological matrices.
Pond et al., Johnson City, United States. In Biomed Chromatogr, Nov 2014
Furthermore, it was deduced that the stereoselective cleavage of MPH to produce ritalinic acid (RA) by human carboxylesterase results in a higher oral bioavailability of the d-threo enantiomer.
Mesenchymal stem cells as cellular vehicles for prodrug gene therapy against tumors.
de Waziers et al., Paris, France. In Biochimie, Oct 2014
This review will summarize the current knowledge about MSCs engineered to express different suicide genes (cytosine deaminase, thymidine kinase, carboxylesterase, cytochrome P450) to elicit a significant antitumor response against brain tumors, ovarian, hepatocellular, pancreatic, renal or medullary thyroid carcinomas, breast or prostate cancer and pulmonary metastases.
The pharmacogenetics of carboxylesterases: CES1 and CES2 genetic variants and their clinical effect.
Paré et al., In Drug Metabol Drug Interact, 2013
Human carboxylesterase 1 (CES1) and carboxylesterase 2 (CES2) are serine esterases responsible for the hydrolysis of ester and amide bonds present in a number of pharmaceutical products.
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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