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Alterations in methylation of CpG sites of specific genes (HDAC4, RAX2, APOA5 and CES1 loci) may contribute to childhood obesity.
The results showed that there was a significant association between CES1 S75N (rs2307240) and the outcome of clopidogrel therapy. Moreover, the frequency of the T allele of rs2307240 in acute coronary syndrome patients (MAF = 0.22) was more than four times higher than that in the general public
Study utilized humanized mouse model expressing WT (control), G143E and catalytically dead S221A variants of human CES1 in the liver in the absence of endogenous expression of the mouse orthologous gene shows that compared to wild-type CES1, expression of the CES1G143E confers resistance to development of high-fat diet induced hepatic steatosis and leads to improved metabolic profile.
Which selectively amplified CES1A1 and, if present, also CES1A2.
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.
Anordrin is predominantly catalyzed by CES1 and CES2 to generate the main active metabolite, anordiol.
genetic association and pharmacogenomic studies in population in Finland: Data suggest that 2 SNPs in CES1 (rs12443580, rs8192935) are associated with variations in expression of CES1 (in whole blood samples but not in liver); these CES1 SNPs do not affect pharmacokinetics or pharmacodynamics of clopidogrel, an inhibitor of platelet aggregation. A missense mutation in CES1 (rs71647871) impairs hydrolysis of clopidogrel.
The frequencies of SNVs with a potential functional impact were below 0.02 suggesting limited pharmacogenetic potential for CES1 genotyping.
none of the selected variations of CES1 had a clinically relevant impact on the metabolism of enalapril
Study revealed that several nsSNPs significantly impaired CES1 activity on the metabolism of the CES1 substrates enalapril, clopidogrel, and sacubitril.
Suggest a primary metabolic role for CES1 in the capacity of skin/keratinocytes to mediated biotransformation of penta-ethyl ester prodrug of DTPA.
These data suggest that infants younger than 3 weeks of age would exhibit significantly lower CES1- and CES2-dependent metabolic clearance compared with older individuals.
The intestinal transport of oseltamivir, a hCE1 substrate, could be evaluated in subclone #78 cell monolayers.
An association was identified with a genetic variation in CES1 and early-onset capecitabine-related toxicity.
Reduced CES1 expression/activity could promote development of METH-PAH.
These data suggest that CES1 genetic variants and gender are important contributing factors to variability in dabigatran etexilate activation in humans.
some functional CES1 genetic variants (for example, G143E) may impair ACE inhibitor activation, and consequently affect therapeutic outcomes of ACEI prodrugs.
HNF4alpha regulated CES1 expression by directly binding to the proximal promoter of CES1.
We conclude that the -816A>C variant is not associated with interindividual variability in CES1 expression and activity or therapeutic response to ACEI prodrugs
Our study identified CYP2C19*3 and CES1 rs8192950 as genetic polymorphisms related to recurrent ischemic events in patients with extracranial or intracranial occlusive disease, demonstrating the important roles of CYP2C19 and CES1 in patients treated with clopidogrel
Data suggest that substrate specificity of porcine liver esterase extends to the plasticizers di-(2-ethylhexyl) trimellitates.
One novel isoform termed alternative pig liver esterase (APLE) was found to hydrolyze methyl-(2R,4E)-5-chloro-2-isopropyl-4-pentenoate in a highly stereoselective manner (E>200).
The objective of this study is to explore the mechanisms that regulate TGH expression in porcine adipocyte and its role in fasting-induced and Isoproterenol-stimulated lipolysis in porcine primary adipocytes.
Carboxylesterase distribution in minipig skin in similar to that in human skin.
PMPMEase was purified to apparent homogeneity from porcine liver supernatant.
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.
acyl coenzyme A:cholesterol acyltransferase
, acyl-coenzyme A:cholesterol acyltransferase
, brain carboxylesterase hBr1
, carboxylesterase 1 (monocyte/macrophage serine esterase 1)
, carboxylesterase 2 (liver)
, cholesteryl ester hydrolase
, cocaine carboxylesterase
, human monocyte/macrophage serine esterase 1
, liver carboxylesterase 1
, methylumbelliferyl-acetate deacetylase 1
, monocyte/macrophage serine esterase
, retinyl ester hydrolase
, serine esterase 1
, triacylglycerol hydrolase
, carboxylesterase D1
, carboxylesterase 1
, alternative pig liver esterase
, liver carboxylesterase
, prenylated methylated protein methyl esterase