Association of actin with chromaffin granule membranes and the effect of cytochalasin B on the polarity of actin filament elongation.
Association of actin with chromaffin granule membranes and the effect of cytochalasin B on the polarity of actin filament elongation.
复制标题
肌动蛋白与嗜铬颗粒膜的结合以及细胞松弛素 B 对肌动蛋白丝伸长极性的影响。
DOI:
10.1016/0005-2736(81)90137-1
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发表时间:
1981
期刊:
影响因子:
--
通讯作者:
Lin,S
中科院分区:
文献类型:
--
作者:
Wilkins,JA;Lin,S
Membranes of chromaffin granules isolated from bovine adrenal medulla are shown to bind dihydrocytochalasin B with high affinity. These membranes also bound [3H]actin in a time- and Mg2+-dependent manner and electron microscopy showed the presence of membrane-attached actin filaments following addition of exogenous actin.Binding of [3H]actin was partially inhibited by cytochalasin B. Electron microscopic analysis of heavy meromyosin-decorated, membrane-attached filaments showed terminally (end-on) attached filaments with both possible polarities (i.e., filaments with arrowheads pointing both towards and away from the membranes). Treatment of samples with cytochalasin B preferentially inhibited growth of filaments with their ‘barbed’ ends pointing away from membranes. These results are discussed with respect to the role of actin in secretory granule function and the mechanism of cytochalasin action.