Relevant bibliographies by topics / Butyrylcholinesterase activity

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  2. Dissertations / Theses
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Academic literature on the topic 'Butyrylcholinesterase activity'

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Published: 18 May 2024

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Journal articles on the topic "Butyrylcholinesterase activity"

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Goliasch, Georg, Arvand Haschemi, Rodrig Marculescu, Georg Endler, Gerald Maurer, Oswald Wagner, Kurt Huber, Christine Mannhalter, and Alexander Niessner. "Butyrylcholinesterase Activity Predicts Long-Term Survival in Patients with Coronary Artery Disease." Clinical Chemistry 58, no. 6 (June 1, 2012): 1055–58. http://dx.doi.org/10.1373/clinchem.2011.175984.

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Abstract BACKGROUND Low serum butyrylcholinesterase activity was associated with all-cause and cardiovascular mortality in a community-based study; however, there are no data from investigations of the long-term effects of butyrylcholinesterase on mortality in patients with diagnosed coronary artery disease (CAD). We therefore assessed the effect of butyrylcholinesterase activity on the outcomes of patients with CAD. METHODS AND RESULTS We prospectively included 720 patients in our study: 293 patients with stable CAD and 427 patients with acute coronary syndrome. During a median follow-up of 11.3 years corresponding to 6469 overall person-years, 278 deaths (38.6%) were recorded. We detected a significant and independent protective effect of butyrylcholinesterase on all-cause mortality [adjusted hazard ratio (HR) for a 1-SD increase, 0.62; 95% CI, 0.54–0.71; P < 0.001] and cardiovascular mortality (adjusted HR, 0.64; 95% CI, 0.54–0.76; P < 0.001) in a Cox proportional hazards regression analysis. The 10-year survival rates were 42%, 74%, and 87% in the first, second, and third tertiles of butyrylcholinesterase activity. The presentation of CAD affected the effect of butyrylcholinesterase on mortality (P for interaction = 0.012), with a stronger association found in patients with stable CAD (adjusted HR, 0.56; 95% CI, 0.45–0.70; P < 0.001). CONCLUSIONS Our study demonstrates a strong inverse association between butyrylcholinesterase activity and long-term outcome in patients with known CAD. Because butyrylcholinesterase added predictive information after adjustment for established cardiovascular risk factors, additional underlying pathophysiological mechanisms and the potential applicability of butyrylcholinesterase activity for secondary risk prediction needs to be addressed in future studies.
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Abbott, C. A., M. I. MacKness, S. Kumar, A. O. Olukoga, C. Gordon, S. Arrol, D. Bhatnagar, A. J. M. Boulton, and P. N. Durrington. "Relationship between Serum Butyrylcholinesterase Activity, Hypertriglyceridaemia and Insulin Sensitivity in Diabetes Mellitus." Clinical Science 85, no. 1 (July 1, 1993): 77–81. http://dx.doi.org/10.1042/cs0850077.

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1. The activity of serum butyrylcholinesterase (‘pseudocholinesterase’, EC3.1.1.8) was investigated in 56 patients with type 1 diabetes mellitus, 51 patients with type 2 diabetes mellitus and 101 healthy control subjects. 2. Butyrylcholinesterase activity was significantly elevated in both type 1 (8.10 ± 3.35 units/ml) and type 2 (7.22 ± 1.95 units/ml) diabetes compared with the control subjects (4.23 ± 1.89 units/ml) (P <0.001). 3. In the patients with type 1 and type 2 diabetes, serum butyrylcholinesterase activity was correlated with log serum fasting triacylglycerol concentration (r = 0.41 and r = 0.43, respectively, P <0.001). In the type 2 population serum butyrylcholinesterase activity was also correlated with insulin sensitivity (r = −0.51, P <0.001). 4. Serum butyrylcholinesterase activity was unrelated to age, gender, serum γ-glutamyltranspeptidase activity, body mass index, or treatment for diabetes in both the diabetic populations. 5. In 37 non-diabetic patients with butyrylcholinesterase deficiency serum triacylglycerol levels were in the normal range. 6. These results are consistent with the view that butyrylcholinesterase may have a role in the altered lipoprotein metabolism in hypertriglyceridaemia associated with insulin insensitivity or insulin deficiency in diabetes mellitus.
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Mabrouk, Hajer, Haithem Mechria, Anouar Mechri, Houda Rahali, Wahiba Douki, Lotfi Gaha, and Mohamed Fadhel Najjar. "Butyrylcholinesterase activity in schizophrenic patients." Annales de biologie clinique 69, no. 6 (November 2011): 647–52. http://dx.doi.org/10.1684/abc.2011.0634.

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Suneetha, Lavanya M., Venkata Karunakar, Raj Gopal Reddy, and Sujai Suneetha. "Serum Butyrylcholinesterase Activity in Leprosy." International Journal of Leprosy and Other Mycobacterial Diseases 72, no. 3 (2004): 324. http://dx.doi.org/10.1489/0020-7349(2004)72<324:sbail>2.0.co;2.

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Kálmán, János, Anna Juhász, Zoltán Rakonczay, György Ábrahám, Krisztina Boda, Tibor Farkas, Botond Penke, and Zoltán Janka. "Serum butyrylcholinesterase activity in hyperlipidaemia." Atherosclerosis 173, no. 1 (March 2004): 145–46. http://dx.doi.org/10.1016/j.atherosclerosis.2003.12.002.

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Van Lith, H. A., and A. C. Beynen. "Dietary cholesterol lowers the activity of butyrylcholinesterase (EC3.1.1.8), but elevates that of esterase-1 (EC3.1.1.1) in plasma of rats." British Journal of Nutrition 70, no. 3 (November 1993): 721–26. http://dx.doi.org/10.1079/bjn19930167.

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The question addressed is whether an increased intake of cholesterol affects esterase-1 (EC3.1.1.1; ES-1) and butyrylcholinesterase (EC3.1.1.8) activity in plasma. Rats were fed on a purified diet either without or with cholesterol (10 g/kg) added at the expense of the carbohydrate source. Dietary cholesterol significantly decreased plasma butyrylcholinesterase activity, but raised plasma ES-1 activity. Evidence is discussed, suggesting that plasma butyrylcholinesterase is involved in plasma cholesterol metabolism, whereas esterase-1 is involved in intestinal cholesterol absorption.
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Darvesh, Sultan, Andrea M. LeBlanc, Ian R. Macdonald, George A. Reid, Virender Bhan, Robert J. Macaulay, and John D. Fisk. "Butyrylcholinesterase activity in multiple sclerosis neuropathology." Chemico-Biological Interactions 187, no. 1-3 (September 2010): 425–31. http://dx.doi.org/10.1016/j.cbi.2010.01.037.

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Kuhl, David E., Robert A. Koeppe, Scott E. Snyder, Satoshi Minoshima, Kirk A. Frey, and Michael R. Kilbourn. "Imaging butyrylcholinesterase activity in Alzheimer's disease." Annals of Neurology 60, no. 6 (December 2006): 746. http://dx.doi.org/10.1002/ana.21023.

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Vahdati-Mashhadian, Nasser, Mohammad K. Hassanzadeh, Javad Hosseini, and Ali A. Saffareshargh. "Ethnic differences in the frequency of distribution of serum cholinesterase activity in the Iranian population." Canadian Journal of Physiology and Pharmacology 82, no. 5 (May 1, 2004): 326–30. http://dx.doi.org/10.1139/y04-030.

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One thousand Iranians belonging to 5 different Iranian ethnic groups were tested for butyrylcholinesterase (BChE) activity and phenotype. The phenotype was measured as percent inhibition in the presence of dibucaine. It was found that the Iranian population had an extraordinarily high frequency of the atypical variant of butyrylcholinesterase. 70% to 80% of Iranians carried the atypical mutation (Asp70Gly) on one allele. This contrasts with European and American populations where only 4% carry the atypical allele. The atypical variant of butyrylcholinesterase is known to be associated with prolonged apnea after administration of the muscle relaxants succinylcholine and mivacurium, and is also thought to be associated with abnormal sensitivity to cocaine toxicity. This study demonstrates that the ethnic background of a person has an important role in a person's response to drugs.Key words: butyrylcholinesterase, dibucaine number, heterozygous genes, different Iranian ethnics, metabolic polymorphism.
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Kulesh, A. A., and V. V. Schestakov. "MELATONIN SECRETION AND SERUM BUTYRYLCHOLINESTERASE ACTIVITY AS A POTENTIAL BIOMARKERS OF COGNITIVE IMPAIRMENT IN ACUTE ISCHEMIC STROKE." National Journal of Neurology 2, no. 02 (November 30, 2012): 66–70. http://dx.doi.org/10.61788/njn.v2i12.08.

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The assessment of melatonin secretion in 25 men and serum butyrylcholinesterase level in 40 patients was performed in acute period of stroke. The interaction between these parameters and cognitive state was analyzed. The low levels of 6-sulfatoxymelatonin in daily urine and butyrylcholinesterase in blood were revealed. The 6-sulfatoxymelatonin level in daily urine < 4,0 ng/ml can be regarded as a potential biological marker of poststoke memory dysfunction. The serum butyrylcholinesterase level < 7,0 nmol/sec-l can be regarded as a potential biochemical marker of the multifunctional type of poststoke cognitive impairment.
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Dissertations / Theses on the topic "Butyrylcholinesterase activity"

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Xue, Liu. "HIGH-ACTIVITY MUTANTS OF HUMAN BUTYRYLCHOLINESTERASE FOR COCAINE ABUSE TREATMENT." UKnowledge, 2013. http://uknowledge.uky.edu/pharmacy_etds/40.

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Cocaine is a widely abused drug without an FDA-approved medication. It has been recognized as an ideal anti-cocaine medication to accelerate cocaine metabolism producing biologically inactive metabolites via a route similar to the primary cocaine-metabolizing pathway, i.e. butyrylcholinesterase (BChE)-catalyzed hydrolysis. However, the native BChE has a low catalytic activity against cocaine. We recently designed and discovered a set of BChE mutants with a high catalytic activity specifically for cocaine. An ideal, therapeutically valuable mutant of human BChE should have not only a significantly improved catalytic activity against cocaine, but also certain selectivity for cocaine over neurotransmitter acetylcholine (ACh) such that one would not expect systemic administration of the BChE mutant to interrupt cholinergic transmission. Through integrated computational-experimental studies, several BChE mutants were identified to have not only a considerably improved catalytic efficiency against cocaine, but also the desirable selectivity for cocaine over ACh. Representative BChE mutants have been confirmed to be potent in actual protection of mice from acute toxicity (convulsion and lethality) of a lethal dose of cocaine (180 mg/kg, LD100). Pretreatment with the BChE mutant (i.e. 1 min prior to cocaine administration) dose-dependently protected mice against cocaine-induced convulsions and lethality. The in vivo data reveal the primary factor, i.e. the relative catalytic efficiency, determining the efficacy in practical protection of mice from the acute cocaine toxicity and future direction for further improving the efficacy of the enzyme in the cocaine overdose treatment. For further characterization in animal models, we successfully developed high-efficiency stable cell lines efficiently expressing the BChE mutants by using a lentivirus-based repeated-transduction method. The large-scale protein production enabled us to further characterize the in vivo profiles of the BChE mutant concerning the biological half-life and potency in accelerating cocaine clearance. In particular, it has been demonstrated that the BChE mutant can rapidly metabolize cocaine and completely eliminate cocaine-induced hyperactivity in rodents, implying that the BChE mutant may be developed as a promising therapeutic agent for cocaine abuse treatment.
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Dutta, Susmita. "Biochemical and molecular studies on pesticide-exposed workers of tea gardens of North Bengal." Thesis, University of North Bengal, 2018. http://hdl.handle.net/123456789/2805.

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Debord, Jean. "Relation structure chimique-activité biologique pour quelques phosphoramides et benzamides." Poitiers, 1988. http://www.theses.fr/1988POIT2331.

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Les constantes d'inhibition reversible de la butylcholinesterase par une serie de 16 phosphoramides aliphatiques ont ete determinees par spectrophotometrie et par microcalorimetrie. L'activite des substituants amines augmente avec la lipophilie. L'inhibition irreversible de la butylcholinesterase par le thio-tepa et le methyl-parathion a ete etudiee en suivant l'hydrolyse d'une faible concentration de substrat en presence de l'inhibiteur
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Kaluzsná, Blanka. "Biologická aktivita obsahových látek rostlin XXIII. Alkaloidy Corydalis cava (L.) SCHWEIGG. et KOERTE a jejich účinek na acetylcholinesterasu a butyrylcholinesterasu." Master's thesis, 2013. http://www.nusl.cz/ntk/nusl-329799.

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Charles University in Prague, Faculty of Pharmacy in Hradec Králové Department of Pharmaceutical Botany and Ecology Candidate: Bc. Blanka Kaluzsná Supervisor: Prof. RNDr. Lubomír Opletal, CSc. Title of Diploma Thesis: Biological activity of plant metabolites XXIII. alkaloids of Corydalis cava (l.) Schweigg. & Körte and their effect on acetylcholinesterase and butyrylcholinesterase An ether extract which contained tertiary basic alkaloids was prepared from the dry bulb of Corydalis cava (L.) SCHWEIGG. & KÖRTE. A subfaction labeled 2/B was obtained by column chromatography and crystallization. Three alkaloids were isolated by preparative TLC and they were identified by GC/MS and 1 H a 13 C NMR analyzes as (+)-canadine, (+)-tetrahydropalmatine and domestine. Isolated alkaloids were tested by spectrophotometric Ellman method for inhibitory activity against human erythrocyte acetylcholinesterase (HuAChE) and plasma butyrylcholinesterase (HuBuChE). In comparison with the refernce substances, from these isolated alkaloids only (+)-canadine showed an relatively high inhibitory activity against HuAChE (12,4 µM). (+)-Tetrahydropalmatine and (+)-domestine had no significant inhibitory activity in this direction, against both HuAChE and HuBuChE. Key words: Corydalis cava, (+)-canadine, (+)-tetrahydropalmatine,...
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Krupnik, Eduardo. "Butyrylcholinesterase activity, glucose transporter (GLUT-1) and P-glycoprotein immunoreactivity in endothelial cells in the auditory brainstem of the young postnatal rat." 1993. http://hdl.handle.net/1993/29413.

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Michal, Vojtěch. "Studium biologické aktivity alkaloidů izolovaných z Argemone grandiflora (Papaveraceae)II." Master's thesis, 2015. http://www.nusl.cz/ntk/nusl-379194.

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Michal, Vojtěch: STUDY OF BIOLOGICAL ACTIVITY OF ISOLATED ALKALOIDS FROM ARGEMONE GRANDIFLORA (PAPAVERACEAE) II. Diploma thesis 2015. Charles University in Prague, Faculty of Pharmacy in Hradec Králové, Department of Pharmaceutical Botany and Ecology. Supervisor: PharmDr. Jakub Chlebek, PhD. Key words: Argemone grandiflora Sweet, Papaveraceae, alkaloids, isolation, acetylcholinesterase, butyrylcholinesterase, prolyloligopeptidase, Alzheimerʼs disease, in vitro assay. Diethylether alkaloid extract obtained from stem and roots of Argemone grandiflora Sweet was chromatografically analyzed. Using common chromatografic methods, three alkaloids were isolated in clean form. These substances were identified as allocryptopine, (-)-munitagine and (-)-norargemonine by structural analysis (MS, NMR). These obtained alkaloids were tested for their inhibitory activity against human erythrocyte acetylcholinesterase (AChE) and human plasma butyrylcholinestrase (BuChE) by Ellman's method. The results were represented as IC50 values (allocryptopine: IC50 AChE = 250,0 ± 2,52 μM, IC50 BuChE = 530 ± 28,2 μM; (-)-munitagine: IC50 AChE = 62,29 ± 5,81 μM, IC50 BuChE = 837,4 ± 23,03 μM; (-)-norargemonine: IC50 AChE = 205,17 ± 11,6 μM, IC50 BuChE = 4158,20 ± 495,78 μM). Inhibition against prolyloligopeptidase was tested for...
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Adamcová, Markéta. "Studium biologické aktivity alkaloidů izolovaných z Argemone grandiflora (Papaveraceae)I." Master's thesis, 2015. http://www.nusl.cz/ntk/nusl-331749.

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Adamcová, M.: Study of biological activity of alkaloids isolated from Argemone grandiflora (Papaveraceae) I. Diploma thesis, Charles University in Prague, Faculty of Pharmacy in Hradec Králové, Department of Pharmaceutical Botany and Ecology, Hradec Králové 2015. The aim of this study was isolation of substances from total diethyl ether alkaloid extract of Argemone grandiflora Sweet, their identification and assessment of their inhibition activity towards acetylcholinesterase, butyrylcholinesterase and prolyl oligopeptidase. Using common chromatografic methods, four alkaloids were isolated, that was identified as (+)-laudanosine, protopine, (-)-argemonine a (-)-platycerine. These substances was tested for their inhibition activity IC50: (+)-laudanosine (IC50 AChE = 617,00 ± 46,55 μM, IC50 BuChE = 644,77 ± 55,52 μM, IC50 POP = not mesured yet); protopine (IC50 AChE = 229,98 ± 21,02 μM, IC50 BuChE = 208,87 ± 17,67 μM, IC50 POP ˃ 1000 μM); (-)-argemonine (IC50 AChE = 4677,75 ± 1241,08 μM, IC50 BuChE = 885,45 ± 119,50 μM, IC50 POP = 337 ± 83,1 μM); (-)-platycerine (IC50 AChE = 223,65 ± 19,61 μM, IC50 BuChE = 1651,25 ± 327,7 μM, IC50 POP = 687 ± 74 μM). In comparison with the standards galanthamine (IC50 AChE = 1,710 ± 0,065 μM, IC50 BuChE = 42,30 ± 1,30 μM) and huperzine A (IC50 AChE = 0,033 ± 0,001...
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Hulcová, Daniela. "Biologická aktivita obsahových látek rostlin XXVII. Alkaloidy Fumaria officinalis L. a jejich účinek na acetylcholinesterasu a butyrylcholinesterasu." Master's thesis, 2014. http://www.nusl.cz/ntk/nusl-337392.

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Charles University in Prague Faculty of Pharmacy in Hradec Králové Department of Pharmaceutical Botany and Ecology Candidate: Daniela Hulcová Consultant: Prof. RNDr. Lubomír Opletal, CSc. Title of Diploma Thesis: Biological aktivity of plants metabolites. XXVII. Alkaloids of Fumaria officinalis L. and their effect on acetylcholinesterase and butyrylcholinesterase The summary ethanolic and diethylether extract were prepared from the herbs of a plant Fumaria officinalis L. We have obtained 201 fractions from this extract by column chromatography on the neutral Al2O3 (aluminium oxide). Joined fraction 68-76 were processed by thin layer chromatography, and 3 substances were obtained in pure state: DH-1, DH-2, DH-3. These 3 compounds were identified as protopine, (+)-fumariline and N- methylcorydaldine by the comparison with the literature and results of MS and NMR. These alkaloids were tested for the inhibitory activity against human erythrocytic acetylcholinesterase and plasmatic butyrylcholinesterase by Ellman`s method. The isolated alkaloids did not show any significant inhibitory activity (IC50, µM) compared with the standard galanthamine (IC50, µM; AChE 1,710 ± 0,065, BuChE 42,30 ± 1,30): protopin: AChE: 345,42 ± 31,12, BuChE: 239,66 ± 20,89, (+)-fumarilin: AChE: 2939,2 ± 309,41, BuChE: 330,62 ±...
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Book chapters on the topic "Butyrylcholinesterase activity"

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Albaret, Christine, Patrick Masson, Clarence A. Broomfield, Laurent El Kaim, and Pierre-Louis Fortier. "Mechanical Aspects of the Phosphotriesterase Activity of Human Butyrylcholinesterase G117H Mutant." In Structure and Function of Cholinesterases and Related Proteins, 399–405. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-1540-5_111.

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Albaret, Christine, Patrick Masson, Clarence A. Broomfield, Laurent El Kaim, and Pierre-Louis Fortier. "Mechanical Aspects of the Phosphotriesterase Activity of Human Butyrylcholinesterase G117H Mutant." In Structure and Function of Cholinesterases and Related Proteins, 434. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-1540-5_117.

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Genovese, Raymond F., Averi R. Roberts, William E. Fantegrossi, Roberta Larrison, and Bhupendra P. Doctor. "Horse Serum Butyrylcholinesterase Does Not Disrupt Passive Avoidance Learning or Spontaneous Motor Activity in Rats." In Enzymes of the Cholinesterase Family, 473–74. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4899-1051-6_100.

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Broomfield, C. A., C. B. Millard, O. Lockridge, and T. L. Caviston. "Mutation of Human Butyrylcholinesterase Glycine 117 to Histidine Preserves Activity but Confers Resistance to Organophosphorus Inhibitors." In Enzymes of the Cholinesterase Family, 169–75. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4899-1051-6_35.

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Eremenko, Arkadiy, Il'ya Kurochkin, and Nataliya Nechaeva. "Bioanalytical systems based on cholinesterases for detection of organophosphates." In ORGANOPHOSPHORUS NEUROTOXINS, 205–18. ru: Publishing Center RIOR, 2020. http://dx.doi.org/10.29039/32_205-218.

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Various types of electrochemical sensors based on the inhibition of butyrylcholinesterase (BChE) have been presented for the analysis of organophosphates (OPC). A special design of thick film sensors and electrochemical detector for cholinesterases assay and their inhibitors in aqueous samples has been developed. For this assay, thiol sensitive sensors based on screen printed graphite electrode modified with nanoparticles of manganese dioxide were used. High sensitivity of manganese dioxide modified thick film sensors towards thiocholine and therefore low detection limit of BChE (1 pM) enabled their use for subnanomolar detection of an organophosphate pesticide diazinon, and other irreversible inhibitors of BChE. This work also presents modern innovative approach for the analysis of BChE by Raman spectroscopy. New SERS-substrates based on silver paste for sensitive quantification of BChE activity were obtained, characterized and applied to thiocholine detection, with LOD (TCh) being 260 nM. Real samples of human plasma were analyzed; a good correlation between spectrophotometric detection and Raman detection was shown. The developed technique is inexpensive and easy-to-use and has promising potential for analysis of OPC.
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Eremenko, Arkadiy, Il'ya Kurochkin, and Nataliya Nechaeva. "Bioanalytical systems based on cholinesterases for detection of organophosphates." In Organophosphorous Neurotoxins, 0. ru: Publishing Center RIOR, 2020. http://dx.doi.org/10.29039/chapter_5e4132b6096d14.18045940.

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Various types of electrochemical sensors based on the inhibition of butyrylcholinesterase (BChE) have been presented for the analysis of organophosphates (OPC). A special design of thick film sensors and electrochemical detector for cholinesterases assay and their inhibitors in aqueous samples has been developed. For this assay, thiol sensitive sensors based on screen printed graphite electrode modified with nanoparticles of manganese dioxide were used. High sensitivity of manganese dioxide modified thick film sensors towards thiocholine and therefore low detection limit of BChE (1 pM) enabled their use for subnanomolar detection of an organophosphate pesticide diazinon, and other irreversible inhibitors of BChE. This work also presents modern innovative approach for the analysis of BChE by Raman spectroscopy. New SERS-substrates based on silver paste for sensitive quantification of BChE activity were obtained, characterized and applied to thiocholine detection, with LOD (TCh) being 260 nM. Real samples of human plasma were analyzed; a good correlation between spectrophotometric detection and Raman detection was shown. The developed technique is inexpensive and easy-to-use and has promising potential for analysis of OPC.
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Weingand-Ziadé, A., F. Renault, and P. Masson. "Combined Action of Temperature and Pressure on the Catalytic Activity of Wild-Type and D70G Mutant of Human Butyrylcholinesterase." In Advances in High Pressure Bioscience and Biotechnology, 279–82. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-60196-5_62.

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Varfolomeev, Sergey, Bella Grigorenko, Sofya Lushchekina, Patrick Masson, Galina Mahaeva, Dana Novichkova, and Alexander Nemuchin. "Study and modeling of mechanisms of cholinesterasis reactions in order to improve their catalytic properties in the neutralization reactions of organophosphorus compounds." In ORGANOPHOSPHORUS NEUROTOXINS, 140–80. ru: Publishing Center RIOR, 2020. http://dx.doi.org/10.29039/23_140-180.

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“Biocleaners” or “bioscavengers” are biological objects (enzymes, catalytic antibodies) that are capable of binding and/or hydrolyzing organophosphorus compounds (OPC). Their use seems to be the most effective alternative to traditional antidotes to neutralize or detoxify OPC. The introduction of bioscavengers allows neutralizing toxicant molecules in the bloodstream before they reach their biological targets, thereby providing protection against poisoning. Bioscavengers of the first-generation neutralized OPC molecules by stoichiometrically binding to them. The safety and efficacy of human butyrylcholinesterase (BChE) for protecting against OPC poisoning has been shown. However, the stoichiometric neutralization of OPC requires the introduction of a huge amount of expensive biopharmaceuticals. Catalytic bioscavengers that hydrolytically neutralize OPC were introduced at a much lower dose to achieve the same degree of effectiveness. The most effective catalytic bioscavengers are enzymes. The most promising enzymes are artificial mammalian paraoxonase mutants and bacterial phosphotriesterases. However, studies of other enzymes, such as prolidases, oxidases, artificial mutants of cholinesterases and carboxyl esterases and catalytic antibodies are actively ongoing. Since OPC are pseudosubstrates of cholinesterases (ChEs), a detailed description of the mechanisms of inhibition, dealkylation, and spontaneous reactivation of phosphorylated ChEs is critical for the development of ChEs mutants with a high rate of hydrolysis of OPC. The review presents an analysis of different views on the mechanisms of interaction of ChEs with OPC, discusses the possible directions of creating effective catalytic biological traps based on BChE and changes in their mechanism of action as compared to the native enzyme. A separate section is devoted to the effect of mutations, both polymorphic and artificial, on the stability of the protein molecule of BChE.
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Varfolomeev, Sergey, Bella Grigorenko, Sofya Lushchekina, Patrick Masson, Galina Mahaeva, Dana Novichkova, and Alexander Nemuchin. "Study and modeling of mechanisms of cholinesterasis reactions in order to improve their catalytic properties in the neutralization reactions of organophosphorous compounds." In Organophosphorous Neurotoxins, 134–74. ru: Publishing Center RIOR, 2020. http://dx.doi.org/10.29039/chapter_5e4132b603bfc4.70818543.

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“Biocleaners” or “bioscavengers” are biological objects (enzymes, catalytic antibodies) that are capable of binding and/or hydrolyzing organophosphorus compounds (OPC). Their use seems to be the most effective alternative to traditional antidotes to neutralize or detoxify OPC. The introduction of bioscavengers allows neutralizing toxicant molecules in the bloodstream before they reach their biological targets, thereby providing protection against poisoning. Bioscavengers of the first-generation neutralized OPC molecules by stoichiometrically binding to them. The safety and efficacy of human butyrylcholinesterase (BChE) for protecting against OPC poisoning has been shown. However, the stoichiometric neutralization of OPC requires the introduction of a huge amount of expensive biopharmaceuticals. Catalytic bioscavengers that hydrolytically neutralize OPC were introduced at a much lower dose to achieve the same degree of effectiveness. The most effective catalytic bioscavengers are enzymes. The most promising enzymes are artificial mammalian paraoxonase mutants and bacterial phosphotriesterases. However, studies of other enzymes, such as prolidases, oxidases, artificial mutants of cholinesterases and carboxyl esterases and catalytic antibodies are actively ongoing. Since OPC are pseudosubstrates of cholinesterases (ChEs), a detailed description of the mechanisms of inhibition, dealkylation, and spontaneous reactivation of phosphorylated ChEs is critical for the development of ChEs mutants with a high rate of hydrolysis of OPC. The review presents an analysis of different views on the mechanisms of interaction of ChEs with OPC, discusses the possible directions of creating effective catalytic biological traps based on BChE and changes in their mechanism of action as compared to the native enzyme. A separate section is devoted to the effect of mutations, both polymorphic and artificial, on the stability of the protein molecule of BChE.
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10

Harris, Brian, and Kris Ferguson. "Butyrylcholinesterase (Pseudocholinesterase) Deficiency." In Advanced Anesthesia Review, edited by Alaa Abd-Elsayed, 101—C37.S9. Oxford University PressNew York, 2023. http://dx.doi.org/10.1093/med/9780197584521.003.0037.

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Abstract Pseudocholinesterase is a plasma enzyme that functions to hydrolyze esters in succinylcholine, mivacurium, and ester-type local anesthetic. Pseudocholinesterase is produced in the liver and exists as an α2-globulin. Pseudocholinesterase deficiency is a rare disorder that can be acquired or inherited. Patients are asymptomatic unless given a medication that requires hydrolysis for termination of action. Pseudocholinesterase deficiency can cause delayed awakening due to prolonged action of succinylcholine. The metabolism of chloroprocaine is significantly prolonged, leading to an extended duration of nerve blockade. Cocaine’s effects can be exaggerated as cocaine is an ester-linked local anesthetic. The dibucaine number can be used to quantify pseudocholinesterase activity. Treatment is typically supportive if pseudocholinesterase deficiency is undiagnosed.
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Conference papers on the topic "Butyrylcholinesterase activity"

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Donozo, Martina, Valeria Cavallaro, Ana Paula Murray, and Carlos Javier Baier. "Microwave-Assisted Synthesis and Butyrylcholinesterase Inhibitory Activity of New Azobenzene Derivatives." In ECMC 2022. Basel Switzerland: MDPI, 2022. http://dx.doi.org/10.3390/ecmc2022-13464.

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Delogu, Giovanna Lucia, Benedetta Era, Amit Kumar, Francesca Pintus, and Antonella Fais. "Synthesis, butyrylcholinesterase inhibitory activity and molecular docking of novel hydroxylated 2-benzylbenzofuran derivatives." In 7th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/ecmc2021-11381.

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3

Ślusarczyk, S., F. Sezer Senol, A. Matkowski, A. Perez Garrido, F. Girón Rodríguezd, P. Cerón-Carrasco José, H. den Haan, et al. "Selective in vitro and in silico butyrylcholinesterase inhibitory activity of diterpenes and polyphenols from traditional Asian medicinal plants." In GA 2017 – Book of Abstracts. Georg Thieme Verlag KG, 2017. http://dx.doi.org/10.1055/s-0037-1608088.

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4

Krunić, Mihajlo J., Jelena Z. Penjišević, Slađana Kostić-Rajačić, Vladimir B. Šukalović, Deana B. Andrić, and Ivana I. Jevtić. "Pyrazole/tacrine derivatives as potential cholinesterase inhibitors." In 2nd International Conference on Chemo and Bioinformatics. Institute for Information Technologies, University of Kragujevac, 2023. http://dx.doi.org/10.46793/iccbi23.567k.

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Two new tacrine/pyrazole conjugates were designed, synthesized, and pharmacologically evaluated for their inhibitory activity toward acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE). A scalable and cost-efficient synthetic route was developed, and key reaction steps for the synthesis of compounds 4a,b were nucleophilic substitution of α-aroylketene dithioacetals with tacrine intermediates, followed by cyclocondensation of respective N,S-acetals with hydrazine hydrate. The preliminary pharmacological evaluation revealed high inhibitory activities of 4a,b toward AChE (180 and 259 nM, respectively) and BuChE (51 and 95 nM, respectively) as compared with known inhibitor, tacrine. Overall, both compounds were more efficient BuChE inhibitors while 4a, with a shorter linker connecting tacrine and phenylpyrazole moieties, showed higher inhibitory activity toward both enzymes. Molecular docking analysis strongly corroborated pharmacological results since both compounds interacted favorably with target enzymes. Calculated pharmacokinetic properties (absorption, distribution, metabolism, and excretion (ADME) showed that 4a,b obey Lipinski’s rule of druglikeness and are promising lead compounds for the development of new drug candidates.
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