INTERACTION BETWEEN INSULIN-STORAGE GRANULES AND F-ACTIN INVITRO
INTERACTION BETWEEN INSULIN-STORAGE GRANULES AND F-ACTIN INVITRO
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DOI：
10.1042/bj1780367
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发表时间：
1979-01-01
影响因子：
4.1
通讯作者：
TYHURST, M
中科院分区：
文献类型：
--
作者：
HOWELL, SL;TYHURST, M
通过比较聚合(F-)肌动蛋白与大鼠胰岛胰岛素储存颗粒在不同浓度肌动蛋白存在下的沉降，研究了它们之间可能的相互作用。在0.1-0.5 mg/ml的浓度范围内，肌动蛋白对颗粒沉降率的抑制与颗粒与肌动蛋白细丝的结合一致。这种相互作用在加入ATP(2 MM)时增强，而在CaCl2(0.1 mM)中加入则减弱。颗粒与肌动蛋白的结合不受环状AMP或颗粒与磷脂酶C预先孵育的影响，相互作用的特异性通过使用解聚(G-)肌动蛋白和肌球蛋白来提供类似粘度的溶液来证实；这两者都不会引起颗粒沉淀的任何改变。简要讨论了胰岛素储存颗粒与肌动蛋白相互作用对胰岛素分泌机制的可能影响。
Possible interactions between polymerized (F-) actin and insulin-storage granules from rat islets of Langerhans were examined in vitro by comparing the sedimentation of the granules in the presence of various actin concentrations. Actin in the concentration range 0.1-0.5 mg/ml produced a retardation in granule-sedimentation rates consistent with binding of the granules to the actin filaments. This interaction was increased by addition of ATP (2 mM), but was decreased by CaCl2 (0.1 mM). Binding of granules to actin was unaffected by cyclic AMP or by preincubation of the granules with phospholipase C. Specificity of the interaction was confirmed by the use of depolymerized (G-) actin and of myosin to provide a solution of comparable viscosity; neither of these caused any alteration of granule sedimentation. Possible implications of this interaction of insulin-storage granules with actin for the mechanism of insulin secretion are briefly discussed.