钙结合蛋白对膜融合的调节作用。
Modulation of membrane fusion by calcium-binding proteins.
作者信息
Hong K, Düzgüneş N, Papahadjopoulos D
出版信息
Biophys J. 1982 Jan;37(1):297-305. doi: 10.1016/S0006-3495(82)84678-X.
Abstract
The effects of several Ca2+-binding proteins (calmodulin, prothrombin, and synexin) on the kinetics of Ca2+-induced membrane fusion were examined. Membrane fusion was assayed by following the mixing of aqueous contents of phospholipid vesicles. Calmodulin inhibited slightly the fusion of phospholipid vesicles. Bovine prothrombin and its proteolytic fragment 1 had a strong inhibitory effect on fusion. Depending on the phospholipid composition, synexin could either facilitate or inhibit Ca2+-induced fusion of vesicles. The effects of synexin were Ca2+ specific. 10 microM Ca2+ was sufficient to induce fusion of vesicles composed of phosphatidic acid/phosphatidylethanolamine (1:3) in the presence of synexin and 1 mM Mg2+. We propose that synexin may be involved in intracellular membrane fusion events mediated by Ca2+, such as exocytosis, and discuss possible mechanisms facilitating fusion.
摘要
研究了几种钙结合蛋白（钙调蛋白、凝血酶原和突触融合蛋白）对钙离子诱导的膜融合动力学的影响。通过追踪磷脂囊泡中水性内容物的混合来测定膜融合。钙调蛋白对磷脂囊泡的融合有轻微抑制作用。牛凝血酶原及其蛋白水解片段1对融合有强烈抑制作用。根据磷脂组成，突触融合蛋白可以促进或抑制钙离子诱导的囊泡融合。突触融合蛋白的作用具有钙离子特异性。在存在突触融合蛋白和1 mM镁离子的情况下，10 microM钙离子足以诱导由磷脂酸/磷脂酰乙醇胺（1:3）组成的囊泡融合。我们提出突触融合蛋白可能参与由钙离子介导的细胞内膜融合事件，如胞吐作用，并讨论了促进融合的可能机制。
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Modulation of membrane fusion by calcium-binding proteins.钙结合蛋白对膜融合的调节作用。
Biophys J. 1982 Jan;37(1):297-305. doi: 10.1016/S0006-3495(82)84678-X.
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