| pubmed-article:3023337 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3023337 | lifeskim:mentions | umls-concept:C1524059 | lld:lifeskim |
| pubmed-article:3023337 | lifeskim:mentions | umls-concept:C0031327 | lld:lifeskim |
| pubmed-article:3023337 | lifeskim:mentions | umls-concept:C0010738 | lld:lifeskim |
| pubmed-article:3023337 | lifeskim:mentions | umls-concept:C2244412 | lld:lifeskim |
| pubmed-article:3023337 | pubmed:issue | 34 | lld:pubmed |
| pubmed-article:3023337 | pubmed:dateCreated | 1987-1-7 | lld:pubmed |
| pubmed-article:3023337 | pubmed:abstractText | Fluorescence changes using actin covalently labeled with N-(1-pyrenyl)iodoacetamide have been used to determine the effect of cytochalasin D on actin polymerization. A mechanism for the effect of cytochalasin D on actin polymerization is presented, which explains the experimental observation of a cytochalasin D-induced increase in the initial rate of polymerization and a decrease in the final extent of the reaction. Central to this mechanism is the Mg2+-dependent formation of cytochalasin D-induced dimers. The dimers serve as nuclei to enhance the polymerization rate. Binding of Mg2+ to a low affinity site on the dimer induces a conformational change which can be observed as a rapid fluorescence increase. A subsequent time-dependent fluorescence decrease observed prior to polymerization appears to represent ATP hydrolysis resulting in dissociation of the dimer and release of actin monomers containing ADP. We postulate that a slow rate of exchange of ATP for bound ADP relative to hydrolysis results in the accumulation of monomers containing ADP. As these monomers have a high critical concentration, the final extent of polymerization is reduced dramatically. The Mg2+ dependence of the final extent of polymerization in the presence of cytochalasin D is also explained in the context of this mechanism. | lld:pubmed |
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| pubmed-article:3023337 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:3023337 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3023337 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3023337 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:3023337 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:3023337 | pubmed:author | pubmed-author:FriedelEE | lld:pubmed |
| pubmed-article:3023337 | pubmed:author | pubmed-author:GoddetteD WDW | lld:pubmed |
| pubmed-article:3023337 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3023337 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:3023337 | pubmed:volume | 261 | lld:pubmed |
| pubmed-article:3023337 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3023337 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3023337 | pubmed:pagination | 15974-80 | lld:pubmed |
| pubmed-article:3023337 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:3023337 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3023337 | pubmed:articleTitle | Actin polymerization. The mechanism of action of cytochalasin D. | lld:pubmed |
| pubmed-article:3023337 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3023337 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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