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Validated All-in-One™ qPCR Primer for BCHE(NM_000055.3) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
Mutant alleles at the BCHE locus are responsible for suxamethonium sensitivity. Homozygous persons sustain prolonged apnea after administration of the muscle relaxant suxamethonium in connection with surgical anesthesia. The activity of pseudocholinesterase in the serum is low and its substrate behavior is atypical. In the absence of the relaxant, the homozygote is at no known disadvantage. [provided by RefSeq].
Gene References into function
- Mutations associated with prolonged neuromuscular block during anesthesia.
- Butyrylcholinesterase K variant on chromosome 3 q is associated with Type II diabetes in white Caucasian subjects.
- can hydrolyze acetylcholine in the normal and Alzheimer brain.
- Engineering of a monomeric and low-glycosylated form
- Human butyrylcholinesterase is reversibly inhibited by tetraethylammonium ion.
- serum enzyme inhibited by antidepressants, fluoxetine, sertraline and amitriptyline, in a dose related manner
- BuChE-catalyzed hydrolysis of N-methylindoxyl acetate: analysis of volume changes upon reaction and hysteretic behavior. Hydrolysis by wild-type BuChE and peripheral site mutants (D70G, Y332A, D70G/Y332A) was found to follow Michaelis-Menten kinetics.
- There is a minor association between BChE-K and early-onset coronary artery disease, especially in the presence of the APOE-epsilon 4 allele
- Wild-type and A328W mutant expressed in Chinese hamster ovary cells have a 16-hour half-life in the circulation and protect mice from cocaine toxicity.
- Novel mutation and multiple mutations found in the human butyrylcholinesterase gene affect enzyme activity.
- Butyrylcholinesterase is a major regulator of attention especially in cholinergic deficiency states through its ability to hydrolyse acetylcholine.
- Data help to better define the etiology of low BChE activity and the role of the rather common K allele
- The distinct distribution of BuChE activity in neurons in the human thalamus is consistent with an important role for this enzyme in neurotransmission in the human nervous system.
- the structure of BChE is similar to a previously published theoretical model of this enzyme and to the structure of Torpedo acetylcholinesterase
- replacement of Ala277(Trp279) with Trp in human BChE does not affect the binding of E2020 to BChE
- Theoretical analysis of the oscillatory behaviour of the approach to the steady-state for BuChE led us to propose a model for the hysteresis of BuChE with Benzoylcholine.
- analysis of global dynamics of human butyrylcholinesterase in solvents
- BCHE K polymorphism is associated with Type 2 diabetes or with estimates of pancreatic beta cell function in large-scale Danish Caucasian populations.
- This study reports the first data on the relation of BCHE alleles to anthropometric characters.
- Both bambuterol and terbutaline inhibit BChE, but their affinities differ in human serum BChE variants.
- When genetically transferred into rats, accelerated cocaine metabolism.
- BChE-K variant and ApoE-epsilon 4 alleles act synergistically to increase the risk of late-onset Alzheimer's disease, particularly in age group <75 years in Tehran, Iran.
- compareison of theoretical results with those from previous work on mouse acetylcholinesterase and discussion of their implications for substrate binding and catalysis in BuChE.
- four new mutations, found in the exon 2 of the BCHE gene, in a sample from 3001 Brazilian blood donors.A table with the 58 non-usual variants of butyrylcholinesterase is also presented
- BuChE may play role in the phosphorylation of tau in Alzheimer disease
- The results suggest the involvement of BuChE in the pathophysiological process constituting the metabolic syndrome.
- Human plasma contains four esterases: butyrylcholinesterase, paraoxonase, acetylcholinesterase, and albumin.
- failure to observe increased [(11)C]BMP hydrolysis in vivo makes it less likely that incremental BuChE contributes importantly to acetylcholine hydrolysis in Alzheimer disease
- Effects of the oxyanion hole on the energy barriers provide valuable clues on how to rationally design BChE mutants with a higher catalytic activity for the hydrolysis of cocaine.
- pharmacokinetics of BuChE were evaluated in guinea pigs and in cynomolgus monkeys
- K allele of butyrylcholinesterase in diabetes mellitus, Type 2 may predispose to a higher risk of metabolic syndrome
- The hydrolysis of anilides and esters of choline appears to utilize the same catalytic site in BuChE.
- In Alzheimer's disease, BChE may have thus acquired an inverse role to that of AChE by adopting imperfect amphipathic characteristics of its C terminus
- These findings suggest that the Polyethyleneglycol conjugated (PEGylated) recombinant human acetylcholinesterase exhibits unaltered biodistribution and high bioavailability.
- Down-regulation of butyrylcholinesterase is associated with colorectal carcinoma
- H(2)O(2) is a major player in the regulation of the cholinergic signal via both acetylcholinesterase and BchE and this signal is severely affected in the epidermis of patients with active vitiligo
- We hypothesize that CSF BuChE varies inversely with BuChE in cortical amyloid plaques. Thus, low BuChE in a patient's CSF may predict extensive incorporation in neuritic plaques, increased neurotoxicity and greater central neurodegeneration.
- Levels are decreased in colonic adenocarcinomas.
- the 1615G --> A polymorphism BCHE genotype was independently associated with in-stent restenosis in a Japanese population
- calcium-activated BuchE as a major protective mechanism against suicide inhibition of acetylcholinesterase by organophosphates in this non-neuronal tissue
- frequencies of 4 alleles U, A, F, S in Iran of phenotypes of BChE was as follows: normal phenotype (UU) 95.5%, moderate sensitive to succinylcholine including UA,US,UF phenotypes was 3.9%, hypersensitive to succinylcholine (AA, AF, AS, FF, SS) was 0.58%.
- Alzheimer's disease risk was found affected by interaction between estrogen receptor-alpha and butyrylcholinesterase alleles.
- BChE polymorphisms do not constitute a major genetic risk factor for susceptibility to Alzheimer's disease: in a Sardinian population.
- Transgenic goats produced active rBChE in milk sufficient for prophylaxis of humans at risk for exposure to organophosphorus agents
- It was concluded that the active sites for esterase and aryl-acylamidase activities are identical, i.e. S198.
- Studied aging pathway for BCHE inhibited by different organophosphates.
- effects of three non synonymous BCHE mutations (G75R, E90D and /99M) on enzyme kinetic parameters obtained after the expression of the respective recombinant BChEs
- homozygosity, but not heterozygosity, for BCHE-K is a potential risk factor for the development of NFT pathology in young individuals implicating BCHE-K in the pathogenesis of early AD.
- Full-length monomeric recombinant BChE has been crystallized for the first time. A 2.8 A X-ray structure was solved in space group P42(1)2, with unit-cell parameters a = b = 156, c = 146 A.
- data suggest that the BCHE-K allele increases the risk of coronary artery disease in the population (with and without DM) in western parts of Iran, and its presence intensifies the risk of coronary artery disease in type 2 diabetics
- Serum BChE activity is associated with parameters of adiposity, the serum lipid profile and the degree of insulin resistance in type 2 diabetes .
- In our population the K variant of BChE is linked to the age of diagnosis of Alzheimer's disease, since AD patients with this allele presented with a later stage. BChE allelic frequencies in our population are higher than those previously reported.
- Mutations in the BCHE gene is associated with prolonged duration of action of mivacurium or succinylcholine during anaesthesia
- proline-rich peptides organize the 4 subunits of BChE into a 340 kDa tetramer, by interacting with the C-terminal BChE tetramerization domain
- Described denaturing HPLC method to be used for screening for the most common variants of BCHE.
- a direct association between the reduction of butyrylcholinesterase by the increase of homocysteine and an indirect effect by increase in oxidative stress
- 14-3-3 zeta protein and butyrylcholinesterase (BCHE) synergistic effects between polymorphisms in tau phosphorylation relate-genes may help in determining the risk profile for AD.
- Gene expression showed that only one of the newly identified mutations (G333C) altered BChE activity, leading to a decrease of about 80% in relation to the wild-type enzyme.
- Recombinant human butyrylcholinesterase interacts with beta-amyloid fibrils and can attenuate their formation and branching.
- Synergistic effect of apolipoprotein E epsilon4 and butyrylcholinesterase K-variant is associated with disease progression from mild cognitive impairment to Alzheimer's disease
- effects of tyramine, serotonin and benzalkonium on the esterase and aryl acylamidase activities of wild-type butyrylcholinesterase and its peripheral anionic site mutant, D70G, were investigated
- two new mutations of the BCHE gene in 346 Euro-Brazilians
- number of butyrylcholinesterase (BCHE)-K alleles was associated with increasing BuChE activity
- The long chain dicholine ester makes closer contact than the short chain ester between one of its carbonyl carbons and the catalytic Ser198, thus explaining why long-chain dicholine esters are hydrolyzed more rapidly by butyrylcholinesterase.
- Differences between the t peptides of Aacetylcholinesterase and butyrylcholinesterase are conserved among all vertebrates.
- elastic neutron scattering study of the molecular dynamics of native human butyrylcholinesterase and its "aged" soman-inhibited conjugate revealed a significant change in molecular flexibility on an angstrom-nanosecond scale as a function of temperature
