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LOCALIZATION OF PRODUCTS OF ATP HYDROLYSIS IN MAMMALIAN SMOOTH MUSCLE CELLS

The sites of lead phosphate precipitation in mouse bladder smooth muscle incubated with adenosine triphosphate and lead nitrate were studied by electron microscopy. The media constituents and incubating conditions were independently varied so that we could determine optimal conditions for histochemi...

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Detalles Bibliográficos
Autor principal: Lane, Bernard P.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1967
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2107186/
https://www.ncbi.nlm.nih.gov/pubmed/4227958
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author Lane, Bernard P.
author_facet Lane, Bernard P.
author_sort Lane, Bernard P.
collection PubMed
description The sites of lead phosphate precipitation in mouse bladder smooth muscle incubated with adenosine triphosphate and lead nitrate were studied by electron microscopy. The media constituents and incubating conditions were independently varied so that we could determine optimal conditions for histochemical demonstration of ATPase activity in agranular endoplasmic reticulum. Specimens of glutaraldehyde-fixed bladder muscle, frozen, cut into 10–40-µ sections, and incubated for 1 hr at 25°C in medium containing 0.025 M ATP, 0.0025 M lead nitrate, 0.05 M magnesium chloride, and 0.09 M sodium acetate buffer at pH 6.2, exhibited microcrystalline deposits in agranular endoplasmic reticulum and pinocytotic vesicles. Lead salt deposition was also noted in terminal cisternae of sarcoplasmic reticulum in skeletal muscle similarly treated, suggesting that the organelle systems in the two types of muscle cells subserve a common function.
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spelling pubmed-21071862008-05-01 LOCALIZATION OF PRODUCTS OF ATP HYDROLYSIS IN MAMMALIAN SMOOTH MUSCLE CELLS Lane, Bernard P. J Cell Biol Article The sites of lead phosphate precipitation in mouse bladder smooth muscle incubated with adenosine triphosphate and lead nitrate were studied by electron microscopy. The media constituents and incubating conditions were independently varied so that we could determine optimal conditions for histochemical demonstration of ATPase activity in agranular endoplasmic reticulum. Specimens of glutaraldehyde-fixed bladder muscle, frozen, cut into 10–40-µ sections, and incubated for 1 hr at 25°C in medium containing 0.025 M ATP, 0.0025 M lead nitrate, 0.05 M magnesium chloride, and 0.09 M sodium acetate buffer at pH 6.2, exhibited microcrystalline deposits in agranular endoplasmic reticulum and pinocytotic vesicles. Lead salt deposition was also noted in terminal cisternae of sarcoplasmic reticulum in skeletal muscle similarly treated, suggesting that the organelle systems in the two types of muscle cells subserve a common function. The Rockefeller University Press 1967-09-01 /pmc/articles/PMC2107186/ /pubmed/4227958 Text en Copyright © 1967 by The Rockefeller University 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
Lane, Bernard P.
LOCALIZATION OF PRODUCTS OF ATP HYDROLYSIS IN MAMMALIAN SMOOTH MUSCLE CELLS
title LOCALIZATION OF PRODUCTS OF ATP HYDROLYSIS IN MAMMALIAN SMOOTH MUSCLE CELLS
title_full LOCALIZATION OF PRODUCTS OF ATP HYDROLYSIS IN MAMMALIAN SMOOTH MUSCLE CELLS
title_fullStr LOCALIZATION OF PRODUCTS OF ATP HYDROLYSIS IN MAMMALIAN SMOOTH MUSCLE CELLS
title_full_unstemmed LOCALIZATION OF PRODUCTS OF ATP HYDROLYSIS IN MAMMALIAN SMOOTH MUSCLE CELLS
title_short LOCALIZATION OF PRODUCTS OF ATP HYDROLYSIS IN MAMMALIAN SMOOTH MUSCLE CELLS
title_sort localization of products of atp hydrolysis in mammalian smooth muscle cells
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2107186/
https://www.ncbi.nlm.nih.gov/pubmed/4227958
work_keys_str_mv AT lanebernardp localizationofproductsofatphydrolysisinmammaliansmoothmusclecells