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Interactions of actin, myosin, and an actin-binding protein of rabbit pulmonary macrophages. III. Effects of cytochalasin B
Low concentrations (greater than or equal to 10(-7) M) of cytochalasin B reversibly inhibit the temperature-dependent gelation of actin by an actin-binding protein. The cytochalasin B concentrations which maximally inhibit actin gel formation are 10-fold lower than the concentrations which maximally...
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Lenguaje: | English |
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The Rockefeller University Press
1976
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2109726/ https://www.ncbi.nlm.nih.gov/pubmed/135766 |
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collection | PubMed |
description | Low concentrations (greater than or equal to 10(-7) M) of cytochalasin B reversibly inhibit the temperature-dependent gelation of actin by an actin-binding protein. The cytochalasin B concentrations which maximally inhibit actin gel formation are 10-fold lower than the concentrations which maximally impair phagocytosis by intact macrophages. Cytochalasin B also prevents the polymerization of monomeric actin in sucrose extracts of macrophages in the absence but not the presence of 0.1 M CKl. 10(-6) M cytochalasin B dissolves macrophage extract gels and gels comprised of purified actin and actin- binding protein by dissociating actin-binding protein from actin filaments. This concentration of cytochalasin B, however, does not depolymerize the actin filatments. |
format | Text |
id | pubmed-2109726 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1976 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21097262008-05-01 Interactions of actin, myosin, and an actin-binding protein of rabbit pulmonary macrophages. III. Effects of cytochalasin B J Cell Biol Articles Low concentrations (greater than or equal to 10(-7) M) of cytochalasin B reversibly inhibit the temperature-dependent gelation of actin by an actin-binding protein. The cytochalasin B concentrations which maximally inhibit actin gel formation are 10-fold lower than the concentrations which maximally impair phagocytosis by intact macrophages. Cytochalasin B also prevents the polymerization of monomeric actin in sucrose extracts of macrophages in the absence but not the presence of 0.1 M CKl. 10(-6) M cytochalasin B dissolves macrophage extract gels and gels comprised of purified actin and actin- binding protein by dissociating actin-binding protein from actin filaments. This concentration of cytochalasin B, however, does not depolymerize the actin filatments. The Rockefeller University Press 1976-10-01 /pmc/articles/PMC2109726/ /pubmed/135766 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 Interactions of actin, myosin, and an actin-binding protein of rabbit pulmonary macrophages. III. Effects of cytochalasin B |
title | Interactions of actin, myosin, and an actin-binding protein of rabbit pulmonary macrophages. III. Effects of cytochalasin B |
title_full | Interactions of actin, myosin, and an actin-binding protein of rabbit pulmonary macrophages. III. Effects of cytochalasin B |
title_fullStr | Interactions of actin, myosin, and an actin-binding protein of rabbit pulmonary macrophages. III. Effects of cytochalasin B |
title_full_unstemmed | Interactions of actin, myosin, and an actin-binding protein of rabbit pulmonary macrophages. III. Effects of cytochalasin B |
title_short | Interactions of actin, myosin, and an actin-binding protein of rabbit pulmonary macrophages. III. Effects of cytochalasin B |
title_sort | interactions of actin, myosin, and an actin-binding protein of rabbit pulmonary macrophages. iii. effects of cytochalasin b |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2109726/ https://www.ncbi.nlm.nih.gov/pubmed/135766 |