Cholinesterase inhibition by phenothiazine and nonphenothiazine antihistaminics: Analysis of its postulated role in synergizing organophosphate toxicity
Several antihistaminic compounds inhibit in vitro pseudocholinesterase (ChE) from several sources (human, rat, or horse plasma), pI50 ranging from 5.0 to 6.0. This inhibition is competitive with acetylcholine (ACh) and is reversible. Acetylcholinesterase (AChE) from rat brain was nonsensitive to ant...
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todo:paper_0041008X_v31_n2_p179_Fernandez2023-10-03T14:51:16Z Cholinesterase inhibition by phenothiazine and nonphenothiazine antihistaminics: Analysis of its postulated role in synergizing organophosphate toxicity Fernández, G. Díaz Gómez, M.I. Castro, JosA. antihistaminic agent chlorpheniramine cholinesterase cholinesterase inhibitor dichlorvos dimenhydrinate diphenhydramine diphenhydramine 8 bromotheophyllinate mepyramine mepyramine maleate organophosphate phenothiazine derivative proadifen promazine promethazine tripelennamine brain drug potentiation drug toxicity environmental health horse human intoxication normal human pesticide poisoning rat theoretical study Animal Cholinesterase Inhibitors Cholinesterases Dichlorvos Diphenhydramine Drug Synergism Female Histamine H1 Antagonists Horses Human In Vitro Organophosphorus Compounds Phenothiazines Proadifen Rats Several antihistaminic compounds inhibit in vitro pseudocholinesterase (ChE) from several sources (human, rat, or horse plasma), pI50 ranging from 5.0 to 6.0. This inhibition is competitive with acetylcholine (ACh) and is reversible. Acetylcholinesterase (AChE) from rat brain was nonsensitive to antihistaminics even at a concentration of 4 mm. Antihistaminics do not compete with either organophosphates or quaternary ammonium compounds in inhibiting ChE. Inhibition of ChE by antihistaminics is more pronounced at alkaline pH values than at acidic or neutral pH. Administration of promethazine ip to rats at a dose of 50 mg/kg resulted in a 90% inhibition of ChE 1 hr later, while the AChE was totally nonsensitive to the inhibitor even when the dose of the antihistamine was doubled. Results were analyzed in relation to the postulated role of ChE inhibition in antihistaminic potentiation of organophosphorus intoxication. © 1975. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0041008X_v31_n2_p179_Fernandez |
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Universidad de Buenos Aires |
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I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
antihistaminic agent chlorpheniramine cholinesterase cholinesterase inhibitor dichlorvos dimenhydrinate diphenhydramine diphenhydramine 8 bromotheophyllinate mepyramine mepyramine maleate organophosphate phenothiazine derivative proadifen promazine promethazine tripelennamine brain drug potentiation drug toxicity environmental health horse human intoxication normal human pesticide poisoning rat theoretical study Animal Cholinesterase Inhibitors Cholinesterases Dichlorvos Diphenhydramine Drug Synergism Female Histamine H1 Antagonists Horses Human In Vitro Organophosphorus Compounds Phenothiazines Proadifen Rats |
| spellingShingle |
antihistaminic agent chlorpheniramine cholinesterase cholinesterase inhibitor dichlorvos dimenhydrinate diphenhydramine diphenhydramine 8 bromotheophyllinate mepyramine mepyramine maleate organophosphate phenothiazine derivative proadifen promazine promethazine tripelennamine brain drug potentiation drug toxicity environmental health horse human intoxication normal human pesticide poisoning rat theoretical study Animal Cholinesterase Inhibitors Cholinesterases Dichlorvos Diphenhydramine Drug Synergism Female Histamine H1 Antagonists Horses Human In Vitro Organophosphorus Compounds Phenothiazines Proadifen Rats Fernández, G. Díaz Gómez, M.I. Castro, JosA. Cholinesterase inhibition by phenothiazine and nonphenothiazine antihistaminics: Analysis of its postulated role in synergizing organophosphate toxicity |
| topic_facet |
antihistaminic agent chlorpheniramine cholinesterase cholinesterase inhibitor dichlorvos dimenhydrinate diphenhydramine diphenhydramine 8 bromotheophyllinate mepyramine mepyramine maleate organophosphate phenothiazine derivative proadifen promazine promethazine tripelennamine brain drug potentiation drug toxicity environmental health horse human intoxication normal human pesticide poisoning rat theoretical study Animal Cholinesterase Inhibitors Cholinesterases Dichlorvos Diphenhydramine Drug Synergism Female Histamine H1 Antagonists Horses Human In Vitro Organophosphorus Compounds Phenothiazines Proadifen Rats |
| description |
Several antihistaminic compounds inhibit in vitro pseudocholinesterase (ChE) from several sources (human, rat, or horse plasma), pI50 ranging from 5.0 to 6.0. This inhibition is competitive with acetylcholine (ACh) and is reversible. Acetylcholinesterase (AChE) from rat brain was nonsensitive to antihistaminics even at a concentration of 4 mm. Antihistaminics do not compete with either organophosphates or quaternary ammonium compounds in inhibiting ChE. Inhibition of ChE by antihistaminics is more pronounced at alkaline pH values than at acidic or neutral pH. Administration of promethazine ip to rats at a dose of 50 mg/kg resulted in a 90% inhibition of ChE 1 hr later, while the AChE was totally nonsensitive to the inhibitor even when the dose of the antihistamine was doubled. Results were analyzed in relation to the postulated role of ChE inhibition in antihistaminic potentiation of organophosphorus intoxication. © 1975. |
| format |
JOUR |
| author |
Fernández, G. Díaz Gómez, M.I. Castro, JosA. |
| author_facet |
Fernández, G. Díaz Gómez, M.I. Castro, JosA. |
| author_sort |
Fernández, G. |
| title |
Cholinesterase inhibition by phenothiazine and nonphenothiazine antihistaminics: Analysis of its postulated role in synergizing organophosphate toxicity |
| title_short |
Cholinesterase inhibition by phenothiazine and nonphenothiazine antihistaminics: Analysis of its postulated role in synergizing organophosphate toxicity |
| title_full |
Cholinesterase inhibition by phenothiazine and nonphenothiazine antihistaminics: Analysis of its postulated role in synergizing organophosphate toxicity |
| title_fullStr |
Cholinesterase inhibition by phenothiazine and nonphenothiazine antihistaminics: Analysis of its postulated role in synergizing organophosphate toxicity |
| title_full_unstemmed |
Cholinesterase inhibition by phenothiazine and nonphenothiazine antihistaminics: Analysis of its postulated role in synergizing organophosphate toxicity |
| title_sort |
cholinesterase inhibition by phenothiazine and nonphenothiazine antihistaminics: analysis of its postulated role in synergizing organophosphate toxicity |
| url |
http://hdl.handle.net/20.500.12110/paper_0041008X_v31_n2_p179_Fernandez |
| work_keys_str_mv |
AT fernandezg cholinesteraseinhibitionbyphenothiazineandnonphenothiazineantihistaminicsanalysisofitspostulatedroleinsynergizingorganophosphatetoxicity AT diazgomezmi cholinesteraseinhibitionbyphenothiazineandnonphenothiazineantihistaminicsanalysisofitspostulatedroleinsynergizingorganophosphatetoxicity AT castrojosa cholinesteraseinhibitionbyphenothiazineandnonphenothiazineantihistaminicsanalysisofitspostulatedroleinsynergizingorganophosphatetoxicity |
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1807318810239172608 |