细胞松弛素的作用机制：它与肌动蛋白丝末端结合的证据。
Mechanism of action of cytochalasin: evidence that it binds to actin filament ends.
作者信息
Brown S S, Spudich J A
出版信息
J Cell Biol. 1981 Mar;88(3):487-91. doi: 10.1083/jcb.88.3.487.
Abstract
To test the idea that cytochalasin retards actin assembly by binding to filament ends, we have designed a new assay for cytochalasin binding in which the number of filament ends can be varied independently of the total actin concentration. Actin is reacted with polylysine-coated polystyrene beads to make filament ends (Brown and Spudich, 1979, J. Cell Biol. 80:499-504) and then reacted with [3H]cytochalasin B. We have found that cytochalasin B binds to beads in the presence of actin, and that the number of cytochalasin B binding sites can be varied as a function of the number of filament ends independent of the total actin concentration by varying the bead concentration.
摘要
为了验证细胞松弛素通过结合细丝末端来延缓肌动蛋白组装的观点，我们设计了一种新的细胞松弛素结合测定法，在该方法中，细丝末端的数量可以独立于总肌动蛋白浓度而变化。将肌动蛋白与聚赖氨酸包被的聚苯乙烯珠子反应以形成细丝末端（Brown和Spudich，1979年，《细胞生物学杂志》80:499 - 504），然后与[³H]细胞松弛素B反应。我们发现，在肌动蛋白存在的情况下，细胞松弛素B会结合到珠子上，并且通过改变珠子浓度，细胞松弛素B结合位点的数量可以作为细丝末端数量的函数而变化，而与总肌动蛋白浓度无关。
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Cytochalasins block actin filament elongation by binding to high affinity sites associated with F-actin.细胞松弛素通过与F-肌动蛋白相关的高亲和力位点结合来阻断肌动蛋白丝的伸长。
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Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation.细胞松弛素通过阻止细丝伸长来抑制细胞核诱导的肌动蛋白聚合。
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