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Search Results: 1 - 10 of 48 matches for " Butyrylcholinesterase "
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Prevalence of Wild-Type Butyrylcholinesterase Genotype in Patients with Alzheimer’s Dementia  [PDF]
Beate Mueller, Georg Adler
World Journal of Neuroscience (WJNS) , 2015, DOI: 10.4236/wjns.2015.53019
Abstract: Approximately, two-thirds patients with Alzheimer’s disease (AD) are reported to have homozygous wild-type butyrylcholinesterase (BuChE) gene expression. It is associated with a higher rate of hydrolysis of acetylcholine, which ultimately leads to increase in the levels of BuChE in advanced stages of the disease. Rivastigmine, a dual inhibitor of acetylcholinesterase (AChE) and BuChE, might be of additional benefit in patients with AD with wild-type BuChE allele.
Determinación de valores de referencia de colinesterasa plasmática e intraeritrocitaria en ni?os de una población hospitalaria
Guerra,María B.; Cargnel,Elda G.; Osta,Viviana; Osinde,María E.; Schkair,Juan C.;
Archivos argentinos de pediatr?-a , 2005,
Abstract: introduction. plasmatic and intraerythrocytic cholinesterases are enzymes characterized by important interand intraindividual fluctuations, that are reflected in wide levels of normality. therefore, the interpretation of results becomes very difficult if basal values of the patient are not available. due to a shortage of data in the bibliography and, particularly at a national level, the objective of this investigation was to establish reference values for plasmatic and intraerythrocytic cholinesterases for the population who attended to the hospital de ni?os "dr. ricardo gutiérrez". population, material and methods. one hundred and fifty eight children and adolescents, who attended to the surgery service of the hospital de ni?os "dr. ricardo gutiérrez" were selected to perform programmed and elective surgical interventions. plasmatic cholinesterase was determined by knedel and bottger method that uses butyrylcholine as a substrate and acetylcholinesterase was determined by a kinetic method with acetylcholine as a substrate (ellman's method), with previous wash and lysate of erythrocytes. results. the median value for intraerythrocytic cholinesterase was 7,823 iu/l erythrocytes, with percentils 2.5th and 97.5th corresponding to activities of 6,056 and 10,320, respectively. the median value of plasmatic cholinesterase was 11,591 iu/l, with activities of 7,689 and 15,056 for percentiles 2.5th and 97.5th. no significant correlation was found with age or gender. conclusion. we consider essential to establish reference values in our population for a proper interpretation of acetylcholinesterase and plasma cholinesterase levels in case of exposure to poisons of drugs that might affect the activity of these enzymes or for the detection of atypical variants.
Significance of serum butyrylcholinesterase levels in oral cancer
Prabhu K,Naik D,Ray S,Vadiraj
Australasian Medical Journal , 2011,
Abstract: BackgroundOral squamous cell carcinoma (OSCC) is a relatively commonepithelial malignancy, and thus represents a significantpublic health problem. Early detection improves quality oflife for affected patients. Identification of molecularmarkers (or biomarkers) which can predict diseaseprogression is necessary for better management of thesedisorders. A correlation of cholinesterase withtumourigenesis, cell proliferation and cell differentiationhas been observed. Butyrylcholinesterase (BChE;pseudocholinesterase) has been shown to be a biochemicalmarker for cervical cancer which is also an epithelialmalignancy. In this study, we sought to estimate andcompare serum BChE levels in healthy controls and patientswith biopsy-proven oral squamous cell cancer (also anepithelial malignancy) before definitive therapy asradiotherapy or chemotherapy may alter the levels of BChEand may act as a confounding variable.MethodAfter obtaining consent from biopsy proven oral cancerpatients (n= 39) (before onset of any definitive treatment),and from age- and sex-matched healthy controls (n = 20),2ml of blood was collected. After clot formation sampleswere centrifuged, serum was collected for estimation ofBChE.ResultsPre-treatment serum BChE levels were significantly elevated(p < 0.0001) in oral cancer patients compared to that ofcontrols. BChE levels showed a significant increase (p =0.005) with advancing stage in oral cancer patients.ConclusionOur results show there could be a role for serum BChE indetermining the prognosis of oral cancer.
Knowledge, Attitudes, Practices and Biomonitoring of Farmers and Residents Exposed to Pesticides in Brazil
Juliana Oliveira Pasiani,Priscila Torres,Juciê Roniery Silva,Bruno Zago Diniz,Eloisa Dutra Caldas
International Journal of Environmental Research and Public Health , 2012, DOI: 10.3390/ijerph9093051
Abstract: In this study, the knowledge, attitudes and practices regarding pesticide use and the levels of exposure of farmers and residents to organophosphorous and/or carbamates pesticides were evaluated in two rural settings in Brazil. A questionnaire was completed by 112 farm workers aged ≥18 years. Almost all farmers acknowledged that pesticides were potentially harmful to their health (87.5%); however, over half rarely (48.2%) or never (7.2%) used personal protective devices (PPDs). An association was found ( p = 0.001) between the work regimen and the use of PPDs, with more frequent equipment use among hired laborers than those involved in family agriculture. A significant correlation ( p = 0.027) was found between the reporting of adverse symptoms and the use of backpack sprayers. Mean AChE activities of farmers (n = 64) and residents (n = 18) during the exposure and non-exposure periods were significantly lower than their control groups. Mean BChE activities of farmers and residents were significantly lower than their controls during the exposure period. Among the 60 farmers that had blood samples collected in both the exposure and non-exposure (baseline) periods, 10 (16.7%) had AChE depletion of over 30% during the exposure period compared with the baseline level. Six residents living on the same farms also presented this depletion. AChE was over 30% higher than the baseline level for 19 farmers (31.7%), indicating a reboot effect. Special education programs are needed in these regions to promote the safe use of pesticides in the field to decrease the risks from exposure to pesticides for farmers, and from secondary exposure to these compounds for their families.
Effect of Seven Newly Synthesized and Currently Available Oxime Cholinesterase Reactivators on Cyclosarin-Intoxicated Rats
Jana Zdarova Karasova,Jiri Kassa,Kamil Musilek,Miroslav Pohanka,Ladislav Novotny,Kamil Kuca
International Journal of Molecular Sciences , 2009, DOI: 10.3390/ijms10073065
Abstract: Seven new oxime-based acetylcholinesterase reactivators were compared with three currently available ones (obidoxime, trimedoxime, HI-6) for their ability to lessen cholinesterase inhibition in blood and brain of cyclosarin-treated rats. Oximes were given at doses of 5% their LD50 along with 21 mg/kg atropine five min before the LD50 of cyclosarin (120 ug/kg) was administered. Blood and brain samples were collected 30 minutes later. The greatest difference between acetylcholinesterase inhibition in blood of cyclosarin-treated rats was found after administration of HI-6 (40%), compared to 22% for trimedoxime and 6% for obidoxime. Only two of the seven newly synthesized oximes had any effect (K203 at 7%, K156 at 5%). Effective oximes against cyclosarin-inhibited plasma butyrylcholinesterase were HI-6 (42%), trimedoxime (11%), and K156 (4%). The oximes were less effective in brain than in blood, with reactivation values for HI-6 30% against acetylcholinesterase and 10% against butyrylcholinesterase. Values for newly synthesized oximes were less than 10% for K206, K269 and K203.
Effect of Several New and Currently Available Oxime Cholinesterase Reactivators on Tabun-intoxicated Rats
Jana Zdarova Karasova,Jiri Kassa,Young-Sik Jung,Kamil Musilek,Miroslav Pohanka,Kamil Kuca
International Journal of Molecular Sciences , 2008, DOI: 10.3390/ijms9112243
Abstract: The therapeutical efficacies of eleven oxime-based acetylcholinesterase reactivators were compared in an in vivo (rat model) study of treatment of intoxication caused by tabun. In this group there were some currently available oximes (obidoxime, trimedoxime and HI-6) and the rest were newly synthesized compounds. The best reactivation efficacy for acetylcholinesterase in blood (expressed as percent of reactivation) among the currently available oximes was observed after administration of trimedoxime (16%) and of the newly synthesized K127 (22432) (25%). The reactivation of butyrylcholinesterase in plasma was also studied; the best reactivators were trimedoxime, K117 (22435), and K127 (22432), with overall reactivation efficacies of approximately 30%. Partial protection of brain ChE against tabun inhibition was observed after administration of trimedoxime (acetylcholinesterase 20%; butyrylcholinesterase 30%) and obidoxime (acetylcholinesterase 12%; butyrylcholinesterase 16%).
Synthesis and biological evaluation of lycorine derivatives as dual inhibitors of human acetylcholinesterase and butyrylcholinesterase
Yue-Hu Wang, Qin-Li Wan, Cheng-Ding Gu, Huai-Rong Luo, Chun-Lin Long
Chemistry Central Journal , 2012, DOI: 10.1186/1752-153x-6-96
Abstract: A series of lycorine derivatives (1–10) were synthesized and evaluated for anti-cholinesterase activity. Result showed that the novel compound 2-O-tert-butyldimethylsilyl-1-O-(methylthio)methyllycorine (7) was a dual inhibitor of human acetylcholinesterase (hAChE) and butyrylcholinesterase (hBChE) with IC50 values of 11.40 ± 0.66 μM and 4.17 ± 0.29 μM, respectively. The structure-activity relationships indicated that (i) the 1-O-(methylthio)methyl substituent in lycorine was better than the 1-O-acetyl group for the inhibition of cholinesterase; (ii) the acylated or etherified derivatives of lycorine and lycorin-2-one were more potent against hBChE than hAChE; and (iii) the oxidation of lycorine at C-2 decreases the activity.Acylated or etherified derivatives of lycorine are potential dual inhibitors of hBChE and hAChE. Hence, further study on the modification of lycorine for ChE inhibition is necessary.Alzheimer’s disease (AD) is a neurologically degenerative disorder that affects more than 20 million people worldwide [1], and is the third-most costly disease after cardiovascular disease and cancer [2]. The neuropathological hallmarks of the disease include β-amyloid (Aβ) plaques, neurofibrillary tangles, and synaptic loss. Based on the cholinergic hypothesis, the symptoms of AD are the result of the reduction in brain acetylcholine (ACh) activity due to the catabolism of ACh by its principal hydrolytic enzyme acetylcholinesterase (AChE). AChE inhibition is the current approach for AD treatment. Tacrine, donepezil, rivastigmine, and galanthamine are all examples of typical AChE inhibitory drugs [3].Similar to AChE, butyrylcholinesterase (BChE) can also inactivate ACh. The reduction in ACh is usually accompanied by a decrease in AChE activity. By contrast, BChE in AD remains at normal levels or even elevated in the brain. BChE may be a significant contributor to the observed loss of ACh in AD [4]. Furthermore, BChE inhibition can lower Aβ peptide [5,6]. BChE is essen
In vitro Inhibition of Acetylcholinesterase, Butyrylxcholinesterase and Lipoxygenase by Crude Extract of Myricaria elegans Royle
Waqar Ahmad,Bashir Ahmad,Manzoor Ahmad,Zafar Iqbal
Journal of Biological Sciences , 2003,
Abstract: The 80% methanolic extract of Myricaria elegans Royle was investigated for in vitro acetylcholinesterase (ACHE), butyrylcholinesterase (BCHE) and lipoxygenase enzyme inhibition activities. The crude extract was found to have significant acetylcholinesterase inhibitory activity (74.8%) and remarkable butryrylcholinesterase inhibitory activity (96.0%). However, no activity was observed against the enzyme lipoxygenase (0.0%).
Hologram QSAR Models of 4-[(Diethylamino)methyl]-phenol Inhibitors of Acetyl/Butyrylcholinesterase Enzymes as Potential Anti-Alzheimer Agents
Simone Decembrino de Souza,Alessandra Mendon?a Teles de Souza,Ana Carolina Corrêa de Sousa,Ana Carolina Rennó Sodero,Lúcio Mendes Cabral,Magaly Gir?o Albuquerque,Helena Carla Castro,Carlos Rangel Rodrigues
Molecules , 2012, DOI: 10.3390/molecules17089529
Abstract: Hologram QSAR models were developed for a series of 36 inhibitors (29 training set and seven test set compounds) of acetyl/butyrylcholinesterase (AChE/BChE) enzymes, an attractive molecular target for Alzheimer’s disease (AD) treatment. The HQSAR models (N = 29) exhibited significant cross-validated (AChE, q2 = 0.787; BChE, q2 = 0. 904) and non-cross-validated (AChE, r2 = 0.965; BChE, r2 = 0.952) correlation coefficients. The models were used to predict the inhibitory potencies of the test set compounds, and agreement between the experimental and predicted values was verified, exhibiting a powerful predictive capability. Contribution maps show that structural fragments containing aromatic moieties and long side chains increase potency. Both the HQSAR models and the contribution maps should be useful for the further design of novel, structurally related cholinesterase inhibitors.
Thermostabilisation of human serum butyrylcholinesterase for detection of its inhibitors in water and biological fluids
Jaganathan, Lakshmanan;Boopathy, Rathanam;
Brazilian Archives of Biology and Technology , 1999, DOI: 10.1590/S1516-89131999000300012
Abstract: the ability of gelatine-trehalose to convert the normally fragile, dry human serum bche into a thermostable enzyme and its use in the detection of cholinesterase inhibitors in water and biological fluids is described. gelatine or trehalose alone is unable to protect the dry enzyme against exposure to high temperature, while a combination of gelatine and trehalose were able to protect the enzyme activity against prolonged exposure to temperature as high as +50°c. a method for rapid, simple and inexpensive means of screening for cholinesterase inhibitors such as carbamates and organophosphates in water, vegetables and human blood has been developed.
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