Cargando…

Fragmin induces tension reduction of actomyosin threads in the presence of micromolar levels of Ca2+

Fragmin was able to reduce the isometric tension of Physarum actomyosin threads to 15-30% of the control tension at the Ca2+ concentrations greater than 10(-6) M. However, fragmin had no effect on the tension of threads when the Ca2+ concentration was lowered below 10(-7) M. The tension once reduced...

Descripción completa

Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1983
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112246/
https://www.ncbi.nlm.nih.gov/pubmed/6681818
_version_ 1782139912684830720
collection PubMed
description Fragmin was able to reduce the isometric tension of Physarum actomyosin threads to 15-30% of the control tension at the Ca2+ concentrations greater than 10(-6) M. However, fragmin had no effect on the tension of threads when the Ca2+ concentration was lowered below 10(-7) M. The tension once reduced by fragmin could not be recovered by the removal of Ca2+. The remaining tension was shown to be still active from the experiment with quick release or stretch of the thread. This tension reduction is parallel to the decrease in viscosity of F-actin solution by fragmin. Electron microscopy showed that F-actin filaments became shorter in the thread after the tension was reduced by fragmin. Therefore, the severing of F-actin by fragmin in micromolar concentration of calcium resulted in the relaxation of tension by actomyosin threads.
format Text
id pubmed-2112246
institution National Center for Biotechnology Information
language English
publishDate 1983
publisher The Rockefeller University Press
record_format MEDLINE/PubMed
spelling pubmed-21122462008-05-01 Fragmin induces tension reduction of actomyosin threads in the presence of micromolar levels of Ca2+ J Cell Biol Articles Fragmin was able to reduce the isometric tension of Physarum actomyosin threads to 15-30% of the control tension at the Ca2+ concentrations greater than 10(-6) M. However, fragmin had no effect on the tension of threads when the Ca2+ concentration was lowered below 10(-7) M. The tension once reduced by fragmin could not be recovered by the removal of Ca2+. The remaining tension was shown to be still active from the experiment with quick release or stretch of the thread. This tension reduction is parallel to the decrease in viscosity of F-actin solution by fragmin. Electron microscopy showed that F-actin filaments became shorter in the thread after the tension was reduced by fragmin. Therefore, the severing of F-actin by fragmin in micromolar concentration of calcium resulted in the relaxation of tension by actomyosin threads. The Rockefeller University Press 1983-01-01 /pmc/articles/PMC2112246/ /pubmed/6681818 Text en 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 Articles
Fragmin induces tension reduction of actomyosin threads in the presence of micromolar levels of Ca2+
title Fragmin induces tension reduction of actomyosin threads in the presence of micromolar levels of Ca2+
title_full Fragmin induces tension reduction of actomyosin threads in the presence of micromolar levels of Ca2+
title_fullStr Fragmin induces tension reduction of actomyosin threads in the presence of micromolar levels of Ca2+
title_full_unstemmed Fragmin induces tension reduction of actomyosin threads in the presence of micromolar levels of Ca2+
title_short Fragmin induces tension reduction of actomyosin threads in the presence of micromolar levels of Ca2+
title_sort fragmin induces tension reduction of actomyosin threads in the presence of micromolar levels of ca2+
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112246/
https://www.ncbi.nlm.nih.gov/pubmed/6681818