Spector I, Braet F, Shochet N R, Bubb M R
Department of Physiology and Biophysics, SUNY at Stony Brook, Stony Brook, New York 11794-8661, USA.
Microsc Res Tech. 1999 Oct 1;47(1):18-37. doi: 10.1002/(SICI)1097-0029(19991001)47:1<18::AID-JEMT3>3.0.CO;2-E.
The high degree of structural and molecular complexity of the actin-based cytoskeleton, combined with its ability to reorganize rapidly and locally in response to stimuli, and its force-generating properties, have made it difficult to assess how the different actin structures are assembled in cells, and how they regulate cell behavior. An obvious approach to study the relationships between actin organization, dynamics, and functions is the specific perturbation of actin structures using pharmacological means. Until recently there were only a few agents available that interfered with cellular activities by binding to actin and most of our knowledge concerning the involvement of actin in basic cellular processes was based on the extensive use of the cytochalasins. In recent years we have identified an increasing number of actin-targeted marine natural products, including the latrunculins, jasplakinolides (jaspamides), swinholide A, misakinolide A, halichondramides, and pectenotoxin II, which are discussed in this article. All these marine-sponge-derived compounds are unusual macrolides and can be classified into several major families, each with its own distinct chemical structures. We describe the current state of knowledge concerning the actin-binding properties of these compounds and show that each class of drugs alters the distribution patterns of actin in a unique way, and that even within a chemical class, structurally similar compounds can have different biochemical properties and cellular effects. We also discuss the effects of these new drugs on fenestrae formation in liver endothelial cells as an example of their usefulness as powerful tools to selectively unmask actin-mediated dynamic processes.
基于肌动蛋白的细胞骨架具有高度的结构和分子复杂性,再加上其能够响应刺激而在局部迅速重组的能力以及产生力的特性,使得评估不同的肌动蛋白结构如何在细胞中组装以及它们如何调节细胞行为变得困难。研究肌动蛋白组织、动力学和功能之间关系的一种明显方法是使用药理学手段对肌动蛋白结构进行特异性扰动。直到最近,只有少数几种试剂可通过与肌动蛋白结合来干扰细胞活动,而且我们关于肌动蛋白参与基本细胞过程的大部分知识都是基于对细胞松弛素的广泛使用。近年来,我们已经鉴定出越来越多的靶向肌动蛋白的海洋天然产物,包括拉春库林、茉莉酮酸内酯(茉莉酰胺)、斯氏藻素A、米沙酮酸内酯A、海兔毒素和pectenotoxin II,本文将对它们进行讨论。所有这些源自海洋海绵的化合物都是不寻常的大环内酯类化合物,可分为几个主要家族,每个家族都有其独特的化学结构。我们描述了关于这些化合物肌动蛋白结合特性的当前知识状态,并表明每类药物都以独特的方式改变肌动蛋白的分布模式,而且即使在一个化学类别中,结构相似的化合物也可能具有不同的生化特性和细胞效应。我们还将讨论这些新药对肝内皮细胞窗孔形成的影响,以此为例说明它们作为强大工具选择性揭示肌动蛋白介导的动态过程的有用性。