Pouli A E, Emmanouilidou E, Zhao C, Wasmeier C, Hutton J C, Rutter G A
Department of Biochemistry, School of Medical Sciences, University Walk, University of Bristol, Bristol BS8 1TD, U.K.
Biochem J. 1998 Jul 1;333 ( Pt 1)(Pt 1):193-9. doi: 10.1042/bj3330193.
To image the behaviour in real time of single secretory granules in neuroendocrine cells we have expressed cDNA encoding a fusion construct between the dense-core secretory-granule-membrane glycoprotein, phogrin (phosphatase on the granule of insulinoma cells), and enhanced green fluorescent protein (EGFP). Expressed in INS-1 beta-cells and pheochromocytoma PC12 cells, the chimaera was localized efficiently (up to 95%) to dense-core secretory granules (diameter 200-1000 nm), identified by co-immunolocalization with anti-(pro-)insulin antibodies in INS-1 cells and dopamine beta-hydroxylase in PC12 cells. Using laser-scanning confocal microscopy and digital image analysis, we have used this chimaera to monitor the effects of secretagogues on the dynamics of secretory granules in single living cells. In unstimulated INS-1 beta-cells, granule movement was confined to oscillatory movement (dithering) with period of oscillation 5-10 s and mean displacement <1 microm. Both elevated glucose concentrations (30 mM), and depolarization of the plasma membrane with K+, provoked large (5-10 microm) saltatory excursions of granules across the cell, which were never observed in cells maintained at low glucose concentration. By contrast, long excursions of granules occurred in PC12 cells without stimulation, and occurred predominantly from the cell body towards the cell periphery and neurite extensions. Purinergic-receptor activation with ATP provoked granule movement towards the membrane of PC12 cells, resulting in the transfer of fluorescence to the plasma membrane consistent with fusion of the granule and diffusion of the chimaera in the plasma membrane. These results illustrate the potential use of phogrin-EGFP chimeras in the study of secretory-granule dynamics, the regulation of granule-cytoskeletal interactions and the trafficking of a granule-specific transmembrane protein during the cycle of exocytosis and endocytosis.
为了实时成像神经内分泌细胞中单个分泌颗粒的行为,我们表达了编码一种融合构建体的cDNA,该融合构建体由致密核心分泌颗粒膜糖蛋白phogrin(胰岛素瘤细胞颗粒上的磷酸酶)和增强型绿色荧光蛋白(EGFP)组成。该嵌合体在INS-1β细胞和嗜铬细胞瘤PC12细胞中表达,通过与INS-1细胞中的抗(原)胰岛素抗体以及PC12细胞中的多巴胺β-羟化酶进行共免疫定位,有效地(高达95%)定位于致密核心分泌颗粒(直径200 - 1000 nm)。利用激光扫描共聚焦显微镜和数字图像分析,我们使用这种嵌合体来监测促分泌剂对单个活细胞中分泌颗粒动力学的影响。在未受刺激的INS-1β细胞中,颗粒运动局限于振荡运动(抖动),振荡周期为5 - 10秒,平均位移<1微米。高葡萄糖浓度(30 mM)以及用K⁺使质膜去极化,都会引发颗粒在细胞内进行大的(5 - 10微米)跳跃式移动,而在维持低葡萄糖浓度的细胞中从未观察到这种情况。相比之下,PC12细胞在未受刺激时颗粒会发生长距离移动,且主要从细胞体向细胞周边和神经突延伸方向移动。用ATP激活嘌呤能受体可引发颗粒向PC12细胞质膜移动,导致荧光转移到质膜,这与颗粒融合以及嵌合体在质膜中扩散一致。这些结果说明了phogrin - EGFP嵌合体在研究分泌颗粒动力学、颗粒 - 细胞骨架相互作用的调节以及在胞吐和胞吞循环过程中颗粒特异性跨膜蛋白的运输方面的潜在用途。