Methylmercury-cholinesterase interactions in rats.

The interaction of methylmercury hydroxide (MMH) and cholinesterases was studied in male and female rats. MMH administered subcutaneously in doses of 10 mg/kg for 2 days reduced the level of plasma cholinesterase (ButChE) by 68% in females and 47% in males while brain acetylcholinesterase (AChE) was...

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Main Authors: Hastings, F L, Lucier, G W, Klein, R
Format: Online
Language:English
Published: 1975
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1475021/
id pubmed-1475021
recordtype oai_dc
spelling pubmed-14750212006-06-09 Methylmercury-cholinesterase interactions in rats. Hastings, F L Lucier, G W Klein, R Research Article The interaction of methylmercury hydroxide (MMH) and cholinesterases was studied in male and female rats. MMH administered subcutaneously in doses of 10 mg/kg for 2 days reduced the level of plasma cholinesterase (ButChE) by 68% in females and 47% in males while brain acetylcholinesterase (AChE) was unaffected. Normal females had higher but more variable ButChE levels than normal males. In a time-course experiment, a single dose of MMH (10 mg/kg) reduced ButChE levels when mercury levels reached 22 mug/ml in the blood. A 10% reduction in brain AChE was observed at 72 hours; however, mercury reached a concentration of only 2.0 mug/g in brain tissue. The determination of the Michaelis constant Km and maximum velocity value Vmax for butyrylcholine and ButChE in control and MMH-treated (1 mg/kg) animals indicated that MMH reduced Vmax only. Since no loss in ButChE activity occurred when MMH and control plasma were incubated in vitro, MMH is not a direct inhibitor of ButChE. Because only the inactive monomeric form of ButChE contains free sulfhydryl groups, it is postulated that MMH combines covalently with the sulfur, preventing formation of active enzyme. By analogy, it is believed this is also the case with AChE. 1975-12 /pmc/articles/PMC1475021/ /pubmed/1227853 Text en
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Hastings, F L
Lucier, G W
Klein, R
spellingShingle Hastings, F L
Lucier, G W
Klein, R
Methylmercury-cholinesterase interactions in rats.
author_facet Hastings, F L
Lucier, G W
Klein, R
author_sort Hastings, F L
title Methylmercury-cholinesterase interactions in rats.
title_short Methylmercury-cholinesterase interactions in rats.
title_full Methylmercury-cholinesterase interactions in rats.
title_fullStr Methylmercury-cholinesterase interactions in rats.
title_full_unstemmed Methylmercury-cholinesterase interactions in rats.
title_sort methylmercury-cholinesterase interactions in rats.
description The interaction of methylmercury hydroxide (MMH) and cholinesterases was studied in male and female rats. MMH administered subcutaneously in doses of 10 mg/kg for 2 days reduced the level of plasma cholinesterase (ButChE) by 68% in females and 47% in males while brain acetylcholinesterase (AChE) was unaffected. Normal females had higher but more variable ButChE levels than normal males. In a time-course experiment, a single dose of MMH (10 mg/kg) reduced ButChE levels when mercury levels reached 22 mug/ml in the blood. A 10% reduction in brain AChE was observed at 72 hours; however, mercury reached a concentration of only 2.0 mug/g in brain tissue. The determination of the Michaelis constant Km and maximum velocity value Vmax for butyrylcholine and ButChE in control and MMH-treated (1 mg/kg) animals indicated that MMH reduced Vmax only. Since no loss in ButChE activity occurred when MMH and control plasma were incubated in vitro, MMH is not a direct inhibitor of ButChE. Because only the inactive monomeric form of ButChE contains free sulfhydryl groups, it is postulated that MMH combines covalently with the sulfur, preventing formation of active enzyme. By analogy, it is believed this is also the case with AChE.
publishDate 1975
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1475021/
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