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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >cAMP regulates plasma membrane vacuolar-type H+-ATPase assembly and activity in blowfly salivary glands
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cAMP regulates plasma membrane vacuolar-type H+-ATPase assembly and activity in blowfly salivary glands

机译：cAMP调节苍蝇唾液腺中的质膜液泡型H + -ATPase组装和活性

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摘要

Reversible assembly of the V0V1 holoenzyme from V-0 and V-1 subcomplexes is a widely used mechanism for regulation of vacuolar-type H+-ATPases (V-ATPases) in animal cells. in the blowfly (Calliphora vicina) salivary gland, V-ATPase is located in the apical membrane of the secretory cells and energizes the secretion of a KCl-rich saliva in response to the hormone serotonin. We have examined whether the CAMP pathway, known to be activated by serotonin, controls V-ATPase assembly and activity. Fluorescence measurements of pH changes at the luminal surface of isolated glands demonstrate that CAMP, Sp-adenosine-3',5'-cyclic monophosphorothioate, or forskolin, similar to serotonin, cause V-ATPase-dependent luminal acidification. In addition, V-ATPase-dependent ATP hydrolysis increases upon treatment with these agents. Immunofluorescence microscopy and pelleting assays have demonstrated further that V, components become translocated from the cytoplasm to the apical membrane and V-ATPase holoenzymes are assembled at the apical membrane during conditions that increase intracellular cAMP. Because these actions occur without a change in cytosolic Ca2+, our findings suggest that the cAMP pathway mediates the reversible assembly and activation of V-ATPase molecules at the apical membrane upon hormonal stimulus.
机译：V-0和V-1亚复合物可逆组装V0V1全酶是调节动物细胞液泡型H + -ATPase（V-ATPase）的广泛使用的机制。在蝇蝇（唾液腺）的唾液腺中，V-ATPase位于分泌细胞的顶膜，并响应于血清素5-羟色胺而激发富含KCl的唾液的分泌。我们已经检查了已知由5-羟色胺激活的CAMP途径是否控制V-ATPase的组装和活性。对离体腺体腔表面pH值变化的荧光测量表明，与血清素类似，CAMP，Sp-腺苷3'，5'-环一硫代磷酸酯或毛喉素会引起V-ATPase依赖性腔内酸化。另外，用这些试剂处理后，依赖于V-ATP酶的ATP水解增加。免疫荧光显微镜检查和沉淀试验进一步证明，在增加细胞内cAMP的条件下，V，组分从细胞质易位到顶膜，并且V-ATPase全酶在顶膜组装。由于这些作用的发生没有改变胞质Ca2 +，因此我们的发现表明cAMP途径在激素刺激下介导了可逆装配和V-ATPase分子在顶膜的活化。

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