Burgoyne R D, Morgan A, Robinson I, Pender N, Cheek T R
Department of Physiology, University of Liverpool, UK.
J Anat. 1993 Oct;183 ( Pt 2)(Pt 2):309-14.
Recent advances have led to an increased understanding of the Ca(2+)-signalling pathway leading to exocytosis in bovine adrenal chromaffin cells. Video-imaging studies have allowed the temporal and spatial aspects of the Ca2+ signal to be investigated in detail. Ca2+ entry at the plasma membrane appears to be crucial for the activation of exocytosis. Ca2+ can enter through the nicotinic channel or characterised voltage-activated channels, or through other poorly defined pathways due to a variety of agonists. Emptying of internal Ca2+ stores is sufficient to activate a Ca2+ entry pathway. The elevation of cytosolic Ca2+ concentration leads to a reorganisation of the cortical actin network and to the triggering of exocytosis. Studies on permeabilised chromaffin cells have resulted in the identification of some of the proteins that control Ca(2+)-dependent exocytosis. These include the peripheral plasma membrane protein annexin II and the cytosolic proteins, protein kinase C and 14-3-3 proteins (Exo1).
最近的进展使人们对牛肾上腺嗜铬细胞中导致胞吐作用的Ca(2+)信号通路有了更深入的了解。视频成像研究能够详细探究Ca2+信号的时间和空间方面。质膜上的Ca2+内流似乎对胞吐作用的激活至关重要。Ca2+可以通过烟碱通道或已明确的电压激活通道进入,或者由于多种激动剂通过其他定义不明确的途径进入。内部Ca2+储存库的排空足以激活Ca2+内流途径。胞质Ca2+浓度的升高导致皮质肌动蛋白网络的重组并触发胞吐作用。对透化嗜铬细胞的研究已鉴定出一些控制Ca(2+)依赖性胞吐作用的蛋白质。这些蛋白质包括外周质膜蛋白膜联蛋白II以及胞质蛋白、蛋白激酶C和14-3-3蛋白(Exo1)。