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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.
Supplier
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
Effects of toxicologically relevant xenobiotics and the lipid-derived electrophile 4-hydroxynonenal on macrophage cholesterol efflux: silencing carboxylesterase 1 has paradoxical effects on cholesterol uptake and efflux.
New
Crow et al., United States. In Chem Res Toxicol, 20 Nov 2014
Carboxylesterase 1 (CES1), proposed to hydrolyze CEs, is inactivated by oxon metabolites of organophosphorus pesticides and by the lipid electrophile 4-hydroxynonenal (HNE).
Design of Enzymatically Cleavable Prodrugs of a Potent Platinum-Containing Anticancer Agent.
New
Bierbach et al., Winston-Salem, United States. In Chemistry, 10 Nov 2014
Two distinct pathways by which the target compounds undergo effective ester hydrolysis, the proposed activating step, have been confirmed: platinum-assisted, self-immolative ester cleavage in a low-chloride environment (LC-ESMS, NMR spectroscopy) and enzymatic cleavage by human carboxylesterase-2 (hCES-2) (LC-ESMS).
A highly selective long-wavelength fluorescent probe for the detection of human carboxylesterase 2 and its biomedical applications.
New
Yang et al., Dalian, China. In Chem Commun (camb), 10 Nov 2014
UNLABELLED: A highly selective long-wavelength fluorescent probe TCFB has been developed for the detection of hCE2.
Preclinical activity of nanoliposomal irinotecan is governed by tumor deposition and intratumor pro-drug conversion.
New
Fitzgerald et al., Merrimack, United States. In Cancer Res, 01 Nov 2014
We identified tumor permeability and carboxylesterase activity needed for pro-drug activation as critical factors in achieving longer duration of SN-38 in tumors.
Mesenchymal stem cells as cellular vehicles for prodrug gene therapy against tumors.
Review
New
de Waziers et al., Paris, France. In Biochimie, Jul 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.
Hepatic carboxylesterase 1 is induced by glucose and regulates postprandial glucose levels.
New
Zhang et al., Baghdad, Iraq. In Plos One, Dec 2013
Carboxylesterase 1 (CES1) is an enzyme that hydrolyzes triglycerides and cholesterol esters, and is important for lipid metabolism.
Vinyl acetate monomer (VAM) genotoxicity profile: relevance for carcinogenicity.
Review
New
Albertini, Burlington, United States. In Crit Rev Toxicol, Sep 2013
It is also DNA reactive and mutagenic, but only after its carboxylesterase mediated conversion to acetaldehyde (AA), a metabolic reaction that also produces acetic acid and protons.
Therapeutic targeting of CPT-11 induced diarrhea: a case for prophylaxis.
Review
New
Mani et al., United States. In Curr Drug Targets, Jun 2013
Covered topics include schedule/dose modification, intestinal alkalization, structural/chemical modification, genetic testing, anti-diarrheal therapies, transporter (ABCB1, ABCC2, BCRP2) inhibitors, enzyme (β-glucuronidase, UGT1A1, CYP3A4, carboxylesterase, COX-2) inducers and inhibitors, probiotics, antibiotics, adsorbing agents, cytokine and growth factor activators and inhibitors and other miscellaneous agents.
Investigation binding patterns of human carboxylesterase I (hCES I) with broad substrates by MD simulations.
Review
Li et al., Dalian, China. In Curr Top Med Chem, 2012
Human carboxylesterase I (hCES 1) plays an important role in the metabolism and activation of prodrugs, such as, the hydrolysis of a variety of drugs of prodrugs featuring an ester, amide or carbamate function.
[Progress in the structure and function of human carboxylesterase 1].
Review
Lü et al., Changsha, China. In Sheng Wu Gong Cheng Xue Bao, 2012
Human carboxylesterase 1 (HCE1), belonging to a multigene serine hydrolase family, is a major liver carboxylesterase responsible for the hydrolysis and metabolism of various xenobiotics.
Metabolomics identifies an inflammatory cascade involved in dioxin- and diet-induced steatohepatitis.
Impact
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
Impact
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.
Review
Impact
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.
Impact
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).
Pathophysiology and therapy of irinotecan-induced delayed-onset diarrhea in patients with advanced colorectal cancer: a prospective assessment.
Impact
Cvitkovic et al., Villejuif, France. In J Clin Oncol, 1998
Before treatment, and if late diarrhea occurred, patients underwent colon mucosal biopsies for CPT-11 and topoisomerase I levels; intestinal transit time; fecalogram; fat and protein excretion; alpha1-antitrypsin clearance; D-xylose test; blood levels for vasoactive intestinal polypeptide, glucagon, gastrin, somatostatin, prostaglandin E2, and carboxylesterase; CPT-11/SN-38 and SN-38 glucuronide pharmacokinetics; and stool cultures.
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