Bambauer H J, Ueno S, Umar H, Ueck M
Cell Tissue Res. 1984;237(3):491-7. doi: 10.1007/BF00228433.
Ca++-ATPase activity (cf. Ando et al. 1981) was examined both light- and electron-microscopically in the neurohypophysis of the guinea pig. Apart from a strong activity within the walls of the blood vessels, in the parenchyma of the neurohypophysis the reaction product of the Ca++-ATPase activity was restricted to the plasmalemma of the pituicytes. This reaction was completely dependent upon Ca++ and the substrate, ATP; the reaction was inhibited by 0.1 mM quercetin, an inhibitor of Ca++-ATPase. A reduction of the enzyme activity occurred by 1) adding Mg++ to the standard incubation medium, and 2) substituting Ca++ with Mg++ at varying concentrations. In all experiments the neurosecretory fibers were devoid of Ca++-ATPase activity. The function of the Ca++-ATPase activity in the plasmalemma of the pituicytes is discussed in connection with the regulation of the extracellular Ca++ concentration, which seems to be important with respect to the discharge of secretory material from the neurosecretory fibers.
采用光镜和电镜检查了豚鼠神经垂体中Ca++-ATP酶活性(参见安藤等人,1981年)。除血管壁内有较强活性外,在神经垂体实质中,Ca++-ATP酶活性的反应产物仅限于垂体细胞的质膜。该反应完全依赖于Ca++和底物ATP;该反应被Ca++-ATP酶抑制剂0.1 mM槲皮素抑制。酶活性降低是由于:1)在标准孵育培养基中加入Mg++;2)用不同浓度的Mg++替代Ca++。在所有实验中,神经分泌纤维均无Ca++-ATP酶活性。结合细胞外Ca++浓度的调节,讨论了垂体细胞质膜中Ca++-ATP酶活性的功能,细胞外Ca++浓度的调节似乎对神经分泌纤维分泌物质的释放很重要。