Hou L, Lanni F, Luby-Phelps K
Center for Fluorescence Research in Biomedical Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.
Biophys J. 1990 Jul;58(1):31-43. doi: 10.1016/S0006-3495(90)82351-1.
We have previously reported that self-diffusion of inert tracer particles in the cytoplasm of living Swiss 3T3 cells is hindered in a size-dependent manner (Luby-Phelps, K., D.L. Taylor, and F. Lanni. 1986. J. Cell Biol. 102:2015-2022; Luby-Phelps, K., P.E. Castle, D.L. Taylor, and F. Lanni. 1987. Proc Natl. Acad. Sci. USA. 84:4910-4913). Lacking a theory that completely explains our data, we are attempting to understand the molecular architecture responsible for this phenomenon by studying tracer diffusion in simple, reconstituted model systems. This report contains our findings on tracer diffusion in concentrated solutions of Ficoll 70 or Ficoll 400, in solutions of entangled F-actin filaments, and in solutions of entangled F-actin containing a background of concentrated Ficoll particles or concentrated bovine serum albumin (BSA). A series of size-fractionated fluorescein-Ficolls were used as tracer particles. By fluorescence recovery after photobleaching (FRAP), we obtained the mean diffusion coefficients in a dilute, aqueous reference phase (Do), the mean diffusion coefficients in the model matrices (D), and the mean hydrodynamic radii (RH) for selected tracer fractions. For each model matrix, the results were compared with similar data obtained from living cells. As in concentrated solutions of globular proteins (Luby-Phelps et al., 1987), D/Do was not significantly size-dependent in concentrated solutions of Ficoll 400 or Ficoll 70. In contrast, D/Do decreased monotonically with increasing RH in solutions of F-actin ranging in concentration from 1 to 12 mg/ml. This size dependence was most pronounced at higher F-actin concentrations. However, the shape of the curve and the extrapolated value of D/Do in the limit, RH----O did not closely resemble the cellular data for tracers in the same size range (3 less than RH less than 30 nm). In mixtures of F-actin and Ficoll or F-actin and BSA, D/Do was well approximated by D/Do for the same concentration of F-actin alone multiplied by D/Do for the same concentrations of Ficoll or BSA alone. Based on these results, it is possible to model the submicroscopic architecture of cytoplasm in living cells as a densely entangled filament network (perhaps made up of F-actin and other filamentous structures) interpenetrated by a fluid phase crowded with globular macromolecules, which in cytoplasm would be primarily proteins.
我们之前报道过,惰性示踪颗粒在活的瑞士3T3细胞胞质中的自扩散以尺寸依赖的方式受到阻碍(Luby-Phelps, K., D.L. Taylor, and F. Lanni. 1986. J. Cell Biol. 102:2015 - 2022; Luby-Phelps, K., P.E. Castle, D.L. Taylor, and F. Lanni. 1987. Proc Natl. Acad. Sci. USA. 84:4910 - 4913)。由于缺乏一个能完全解释我们数据的理论,我们试图通过研究示踪剂在简单的、重构的模型系统中的扩散来理解导致这种现象的分子结构。本报告包含了我们关于示踪剂在Ficoll 70或Ficoll 400浓溶液中、在缠结的F - 肌动蛋白丝溶液中以及在含有浓Ficoll颗粒或浓牛血清白蛋白(BSA)背景的缠结F - 肌动蛋白溶液中的扩散研究结果。一系列按尺寸分级的荧光素 - Ficolls被用作示踪颗粒。通过光漂白后的荧光恢复(FRAP),我们获得了在稀水参考相中的平均扩散系数(Do)、在模型基质中的平均扩散系数(D)以及选定示踪剂级分的平均流体动力学半径(RH)。对于每个模型基质,将结果与从活细胞获得的类似数据进行了比较。与球状蛋白质浓溶液的情况一样(Luby-Phelps等人,1987),在Ficoll 400或Ficoll 70浓溶液中,D/Do对尺寸的依赖性不显著。相比之下,在浓度为1至12 mg/ml的F - 肌动蛋白溶液中,D/Do随着RH的增加而单调下降。这种尺寸依赖性在较高的F - 肌动蛋白浓度下最为明显。然而,曲线的形状以及在RH→0极限情况下D/Do的外推值与相同尺寸范围(3<RH<30 nm)内活细胞中示踪剂的细胞数据并不十分相似。在F - 肌动蛋白与Ficoll或F - 肌动蛋白与BSA的混合物中,D/Do可以很好地近似为相同浓度的单独F - 肌动蛋白的D/Do乘以相同浓度的单独Ficoll或BSA的D/Do。基于这些结果,有可能将活细胞胞质的亚微观结构模拟为一个由密集缠结的丝状网络(可能由F - 肌动蛋白和其他丝状结构组成),该网络被充满球状大分子的流体相贯穿,在胞质中这些球状大分子主要是蛋白质。