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Degradation of acetylcholine in human airways: role of butyrylcholinesterase
Author(s) -
Norel X.,
Angrisani M.,
Labat C.,
Gorenne I.,
Dulmet E.,
Rossi F.,
Brink C.
Publication year - 1993
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.1993.tb13486.x
Subject(s) - neostigmine , acetylcholine , carbachol , butyrylcholinesterase , chemistry , cholinesterase , methacholine , atropine , acetylcholinesterase , biochemistry , pharmacology , enzyme , medicine , endocrinology , aché , biology , lung , respiratory disease , receptor
1 Neostigmine and BW284C51 induced concentration‐dependent contractions in human isolated bronchial preparations whereas tetraisopropylpyrophosphoramide (iso‐OMPA) was inactive on airway resting tone. 2 Neostigmine (0.1 μ m ) or iso‐OMPA (100 μ m ) increased acetylcholine sensitivity in human isolated bronchial preparations but did not alter methacholine or carbachol concentration‐effect curves. 3 In the presence of iso‐OMPA (10 μ m ) the bronchial rings were more sensitive to neostigmine. The pD 2 values were, control: 6.05 ± 0.15 and treated: 6.91 ± 0.14. 4 Neostigmine or iso‐OMPA retarded the degradation of acetylcholine when this substrate was exogenously added to human isolated airways. A marked reduction of acetylcholine degradation was observed in the presence of both inhibitors. Exogenous butyrylcholine degradation was prevented by iso‐OMPA (10 μ m ) but not by neostigmine (0.1 μ m ). 5 These results suggest the presence of butyrylcholinesterase activity in human bronchial muscle and this enzyme may co‐regulate the degradation of acetylcholine in this tissue.