胰岛素储存颗粒与F-肌动蛋白在体外的相互作用。
Interaction between insulin-storage granules and F-actin in vitro.
作者信息
Howell S L, Tyhurst M
出版信息
Biochem J. 1979 Feb 15;178(2):367-71. doi: 10.1042/bj1780367.
Abstract
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. The interaction was increased by addition of ATP (2mM), 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.
摘要
通过比较在不同肌动蛋白浓度下胰岛细胞胰岛素储存颗粒的沉降情况，对来自大鼠胰岛的聚合态（F-）肌动蛋白与胰岛素储存颗粒之间可能的相互作用进行了体外研究。浓度范围为0.1 - 0.5mg/ml的肌动蛋白使颗粒沉降速率减慢，这与颗粒与肌动蛋白丝的结合一致。添加ATP（2mM）可增强这种相互作用，但CaCl2（0.1mM）会使其减弱。颗粒与肌动蛋白的结合不受环磷酸腺苷影响，也不受颗粒与磷脂酶C预孵育的影响。通过使用解聚态（G-）肌动蛋白和肌球蛋白来提供具有可比粘度的溶液，证实了这种相互作用的特异性；这两者均未引起颗粒沉降的任何改变。简要讨论了胰岛素储存颗粒与肌动蛋白这种相互作用对胰岛素分泌机制可能的影响。
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