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THE FINE STRUCTURAL LOCALIZATION OF ACETYLCHOLINESTERASE AT THE MYONEURAL JUNCTION

A study of the cytochemical localization of acetylcholiriesterase activity, combining histochemistry with electron microscopy, showed that the final product of the reaction, which was deposited at or near enzyme sites, occurred at four places in the myoneural junction. These included: plasma membran...

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Detalles Bibliográficos
Autor principal: Barrnett, Russell J.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1962
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2106031/
https://www.ncbi.nlm.nih.gov/pubmed/13865270
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author Barrnett, Russell J.
author_facet Barrnett, Russell J.
author_sort Barrnett, Russell J.
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description A study of the cytochemical localization of acetylcholiriesterase activity, combining histochemistry with electron microscopy, showed that the final product of the reaction, which was deposited at or near enzyme sites, occurred at four places in the myoneural junction. These included: plasma membrane of the muscle covering the junctional folds, the primary and secondary synaptic clefts, parts of the plasma membrane covering the axon terminal, and vesicular structures in the terminal axoplasm. No reaction occurred in the presence of 10(-4) eserine or DFP, whereas 10(-5) DFP inhibited the reaction at all sites except in the vesicles of the terminal axon. These findings are discussed with reference to the histochemical method used and to the occurrence of esterolytic activity in the vesicles, as well as to some of the current hypotheses concerning the relationship of the site of acetylcholinesterase and synaptic transmission.
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spelling pubmed-21060312008-05-01 THE FINE STRUCTURAL LOCALIZATION OF ACETYLCHOLINESTERASE AT THE MYONEURAL JUNCTION Barrnett, Russell J. J Cell Biol Article A study of the cytochemical localization of acetylcholiriesterase activity, combining histochemistry with electron microscopy, showed that the final product of the reaction, which was deposited at or near enzyme sites, occurred at four places in the myoneural junction. These included: plasma membrane of the muscle covering the junctional folds, the primary and secondary synaptic clefts, parts of the plasma membrane covering the axon terminal, and vesicular structures in the terminal axoplasm. No reaction occurred in the presence of 10(-4) eserine or DFP, whereas 10(-5) DFP inhibited the reaction at all sites except in the vesicles of the terminal axon. These findings are discussed with reference to the histochemical method used and to the occurrence of esterolytic activity in the vesicles, as well as to some of the current hypotheses concerning the relationship of the site of acetylcholinesterase and synaptic transmission. The Rockefeller University Press 1962-02-01 /pmc/articles/PMC2106031/ /pubmed/13865270 Text en Copyright © Copyright, 1962, by The Rockefeller Institute Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Barrnett, Russell J.
THE FINE STRUCTURAL LOCALIZATION OF ACETYLCHOLINESTERASE AT THE MYONEURAL JUNCTION
title THE FINE STRUCTURAL LOCALIZATION OF ACETYLCHOLINESTERASE AT THE MYONEURAL JUNCTION
title_full THE FINE STRUCTURAL LOCALIZATION OF ACETYLCHOLINESTERASE AT THE MYONEURAL JUNCTION
title_fullStr THE FINE STRUCTURAL LOCALIZATION OF ACETYLCHOLINESTERASE AT THE MYONEURAL JUNCTION
title_full_unstemmed THE FINE STRUCTURAL LOCALIZATION OF ACETYLCHOLINESTERASE AT THE MYONEURAL JUNCTION
title_short THE FINE STRUCTURAL LOCALIZATION OF ACETYLCHOLINESTERASE AT THE MYONEURAL JUNCTION
title_sort fine structural localization of acetylcholinesterase at the myoneural junction
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2106031/
https://www.ncbi.nlm.nih.gov/pubmed/13865270
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