Friedman J E, Lelkes P I, Rosenheck K, Oplatka A
J Biol Chem. 1986 May 5;261(13):5745-50.
We have incorporated the myosin fragment heavy meromyosin (HMM), which is known to interact mechanochemically and enzymatically with actin filaments, into intact chromaffin cells of the bovine adrenal medulla, in order to study the possible involvement of actin and myosin in stimulus-secretion coupling. HMM was found to stimulate secretion of catecholamines, to cause depolarization of the plasma membrane, and to enhance 22Na+ uptake. HMM-stimulated catecholamine secretion was dependent on the presence of extracellular Na+. The Na+ uptake caused by HMM was inhibited by 10 microM amiloride. Acetylcholine-stimulated catecholamine secretion and 22Na+ uptake were both enhanced by HMM incorporation. A Na+/H+ antiporter, activated by the interaction of HMM with the cells' microfilaments, seems to be involved in HMM action and could possibly also be a component of stimulus-secretion coupling in chromaffin cells, induced by regular agonists.
我们已将肌球蛋白片段重酶解肌球蛋白(HMM)(已知其能与肌动蛋白丝发生机械化学和酶促相互作用)引入牛肾上腺髓质的完整嗜铬细胞中,以研究肌动蛋白和肌球蛋白在刺激 - 分泌偶联中可能的参与情况。发现HMM可刺激儿茶酚胺分泌,导致质膜去极化,并增强22Na+摄取。HMM刺激的儿茶酚胺分泌依赖于细胞外Na+的存在。HMM引起的Na+摄取可被10微摩尔的氨氯吡咪抑制。乙酰胆碱刺激的儿茶酚胺分泌和22Na+摄取都因引入HMM而增强。一种由HMM与细胞微丝相互作用激活的Na+/H+反向转运体似乎参与了HMM的作用,并且也可能是常规激动剂诱导的嗜铬细胞刺激 - 分泌偶联的一个组成部分。