Movement of endocytic shuttle vesicles from the sinusoidal to the bile canalicular face of hepatocytes does not depend on occupation of receptor sites
Movement of endocytic shuttle vesicles from the sinusoidal to the bile canalicular face of hepatocytes does not depend on occupation of receptor sites
复制标题
内吞穿梭囊泡从肝细胞的肝窦到胆小管面的运动不依赖于受体位点的占据
DOI:
10.1016/0014-5793(80)80591-6
复制
发表时间:
1980
期刊:
影响因子:
3.5
通讯作者:
R. Hinton
中科院分区:
文献类型:
--
作者:
B. Mullock;Robin S. Jones;R. Hinton
Three of the major proteins of rat bile, namely IgA, secretory component and the haptoglobin: haemoglobin complex, reach bile by means of specialised endocytic vesicles [l-4]. The route for IgA and secretory component transport is understood. Secretory component is made in hepatocytes [3, 5] and transported to the sinusoidal surface of the cells. Here the secretory component remains firmly bound to the surface of the cells but is capable of binding polymeric IgA [3, 6]. The IgA-secretory component complex is then taken up into vesicles and transported across hepatocytes to the bile canalicular face of the cell [1, 2]. The transport of haptoglobin: haemoglobin complexes is essentially the same [4], although, in this case, the receptor has not been identified.Although the route of transfer of these proteins across hepatocytes is now understood, the mechanics of the process require further investigation. The simplest explanation for the initiation of formation of the endocytic vesicles is that the binding of IgA to secretory component, or ofhaptoglobin: haemoglobin complexes to their receptor, triggers the uptake. However, bile contains large amounts of free secretory component [7]. Although this might perhaps arise from dissociation of secretory IgA in the bile or from carriage of some free secretory component molecules adjacent in the plasma membrane to a secretory component molecule which had bound IgA, the large amounts suggested that the receptor might be transferred to bile whether or not IgA was bound. We now report that formation of the endocytic ‘shut-