| pubmed-article:2995403 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2995403 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
| pubmed-article:2995403 | lifeskim:mentions | umls-concept:C1622186 | lld:lifeskim |
| pubmed-article:2995403 | lifeskim:mentions | umls-concept:C0061187 | lld:lifeskim |
| pubmed-article:2995403 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:2995403 | lifeskim:mentions | umls-concept:C0301644 | lld:lifeskim |
| pubmed-article:2995403 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:2995403 | lifeskim:mentions | umls-concept:C0150312 | lld:lifeskim |
| pubmed-article:2995403 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:2995403 | pubmed:dateCreated | 1985-11-7 | lld:pubmed |
| pubmed-article:2995403 | pubmed:abstractText | Platelet gelsolin (G), a 90,000-mol-wt protein, binds tightly to actin (A) and calcium at low ionic strength to form a 1:2:2 complex, GA2Ca2 (Bryan, J., and M. Kurth, 1984, J. Biol. Chem. 259:7480-7487). Chromatography of actin and gelsolin mixtures in EGTA-containing solutions isolates a stable binary complex, GA1Ca1 (Kurth, M., and J. Bryan, 1984, J. Biol. Chem. 259:7473-7479). The effects of platelet gelsolin and the binary gelsolin-actin complex on the depolymerization kinetics of rabbit skeletal muscle actin were studied by diluting pyrenyl F-actin into gelsolin or complex-containing buffers; a decrease in fluorescence represents disassembly of filaments. Dilution of F-actin to below the critical concentration required for filament assembly gave a biphasic depolymerization curve with both fast and slow components. Dilution into buffers containing gelsolin, as GCa2, increased the rate of depolymerization and gave a first order decay. The rate of decrease in fluorescence was found to be gelsolin concentration dependent. Electron microscopy of samples taken shortly after dilution into GCa2 showed a marked reduction in filament length consistent with filament severing and an increase in the number of ends. Conversely, occupancy of the EGTA-stable actin-binding site by an actin monomer eliminated the severing activity. Dilution of F-actin into the gelsolin-actin complex, either as GA1Ca1 or GA1Ca2, resulted in a decrease in the rate of depolymerization that was consistent with filament end capping. This result indicates that the EGTA-stable binding site is required and must be unoccupied for filament severing to occur. The effectiveness of gelsolin, GCa2, in causing filament depolymerization was dependent upon the ionic conditions: in KCI, actin filaments appeared to be more stable and less susceptible to gelsolin, whereas in Mg2+, actin filaments were more easily fragmented. Finally, a comparison of the number of kinetically active ends generated when filaments were diluted into gelsolin versus the number formed when gelsolin can function as a nucleation site suggests that gelsolin may sever more than once. The data are consistent with a mechanism where gelsolin, with both actin-binding sites unoccupied, can sever but not cap F-actin. Occupancy of the EGTA-stable binding site yields a gelsolin-actin complex that can no longer sever filaments, but can cap filament ends. | lld:pubmed |
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| pubmed-article:2995403 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2995403 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2995403 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2995403 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:2995403 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:2995403 | pubmed:author | pubmed-author:BryanJJ | lld:pubmed |
| pubmed-article:2995403 | pubmed:author | pubmed-author:ColuccioL MLM | lld:pubmed |
| pubmed-article:2995403 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2995403 | pubmed:volume | 101 | lld:pubmed |
| pubmed-article:2995403 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2995403 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2995403 | pubmed:pagination | 1236-44 | lld:pubmed |
| pubmed-article:2995403 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2995403 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:2995403 | pubmed:articleTitle | Kinetic analysis of F-actin depolymerization in the presence of platelet gelsolin and gelsolin-actin complexes. | lld:pubmed |
| pubmed-article:2995403 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2995403 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2995403 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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