Papakonstanti E A, Emmanouel D S, Gravanis A, Stournaras C
Department of Biochemistry, School of Medicine, University of Crete, Heraklion, Greece.
Biochem J. 1996 Apr 1;315 ( Pt 1)(Pt 1):241-7. doi: 10.1042/bj3150241.
We studied with biochemical and immunofluorescent techniques the interactions between the actin microfilament and tubulin microtubule cytoskeleton and Na+/P1 co-transport in opossum kidney cells, a line with proximal tubular characteristics. On brief (5 min) incubation of the cells with a low (0.1 mM) concentration of Pi, a rapid F-actin depolymerization takes place, which fails to occur in cells incubated under similar conditions with 1 mM Pi. The disassembly of actin microfilaments could be quantitatively expressed as a 33% increase in the ration of monomeric G-actin to polymerized F-actin (G/F-actin ration from 0.80 +/- 0.03 to 1.06 +/- 0.06, n = 28, P<0.01), owing to a significant decrease in the latter. Under these conditions microfilaments were also markedly destabilized, as shown by their diminished resistance to graded cytochalasin B concentrations. In addition, incubation of opossum kidney cells with low Pi concentrations (0.1 mM) resulted within 5 min in a substantial depolymerization of microtubules, shown by immunofluorescence microscopy and measured as a 70.9 +/- 6.9% (n = 11, P<0.01) decrement by immunoblot analysis. These changes, which occur only when extracellular Pi concentrations are kept low, seem to be related to a significant increase within 5 min in the rate of cellular Pi uptake by 25.5% under these conditions. The shifts in the dynamic equilibria between monomeric and polymerized actin and tubulin in response to cellular Pi uptake were transient, being fully reversible within 30 min. Moreover, the effect of Pi seemed to be specific because inhibition of its uptake by phosphonoformic acid blunted microtubular disassembly markedly. In contrast, measurement of Pi uptake in the presence of agents known to stabilize cytoskeletal structures showed a substantial decrease with phallacidin, which stabilized microfilaments, whereas the microtubule stabilizer taxol had no apparent effect. These results indicate that acute alterations in the polymerization dynamics and stability of both microfilaments and microtubules are involved in the modulation of Na+/Pi co-transport and suggest important cytoskeletal participation in proximal tubular transport functions.
我们运用生化和免疫荧光技术,研究了负鼠肾细胞(一种具有近端小管特征的细胞系)中肌动蛋白微丝和微管蛋白微管细胞骨架与Na⁺/Pi共转运之间的相互作用。用低浓度(0.1 mM)的Pi短暂(5分钟)孵育细胞时,会发生快速的F-肌动蛋白解聚,而在类似条件下用1 mM Pi孵育的细胞中则不会发生这种情况。肌动蛋白微丝的解体可以定量表示为单体G-肌动蛋白与聚合的F-肌动蛋白的比例增加33%(G/F-肌动蛋白比例从0.80±0.03增加到1.06±0.06,n = 28,P<0.01),这是由于后者显著减少所致。在这些条件下,微丝也明显不稳定,这表现为它们对不同浓度细胞松弛素B的抵抗力降低。此外,用低Pi浓度(0.1 mM)孵育负鼠肾细胞5分钟内会导致微管大量解聚,免疫荧光显微镜显示了这一点,免疫印迹分析测得其减少了70.9±6.9%(n = 11,P<0.01)。这些变化仅在细胞外Pi浓度保持较低时发生,似乎与在这些条件下5分钟内细胞Pi摄取速率显著增加25.5%有关。响应细胞Pi摄取,单体和聚合的肌动蛋白及微管蛋白之间动态平衡的变化是短暂的,在30分钟内完全可逆。此外,Pi的作用似乎具有特异性,因为膦甲酸抑制其摄取会明显减弱微管的解聚。相反,在已知能稳定细胞骨架结构的试剂存在下测量Pi摄取时,发现与稳定微丝的鬼笔环肽一起时摄取量大幅下降,而微管稳定剂紫杉醇则没有明显作用。这些结果表明,微丝和微管聚合动力学及稳定性的急性改变参与了Na⁺/Pi共转运的调节,并提示细胞骨架在近端小管转运功能中具有重要作用。