Bambauer H J, Ueno S, Umar H, Ueck M
Histochemistry. 1985;83(3):195-200. doi: 10.1007/BF00953983.
The histo- and cytochemical localization of Ca++-ATPase activity in the adenohypophysis of the guinea pig was studied utilizing a newly developed method (Ando et al. 1981). An intense reaction was observed in the wall of the blood vessels and between non-secretory cells (stellate cells) and endocrine cells of the pars distalis. Under the electron microscope the Ca++-ATPase reaction product was located extracellularly in relation to the plasmalemma of the stellate cells. This reaction was dependent on Ca++ and the substrate, ATP, and reduced by the addition of 0,1 mM quercetin to the standard incubation medium. Preheating of the sections before incubation completely inhibited the enzyme activity. When Mg++ in different concentrations were substituted for Ca++ in the incubation medium the reaction was always reduced. Both Ca++ and Mg++ in the incubation medium also reduced the reaction. The plasmalemma of the endocrine cells contains no demonstrable amount of Ca++-ATPase activity. The function of the Ca++-ATPase activity is discussed in relation to the regulation of the extracellular Ca++ concentration which seems to be important with respect not only to the secretory process of the endocrine cells but also to the metabolism of the adenohypophysis.
利用一种新开发的方法(安藤等人,1981年)研究了豚鼠腺垂体中Ca++ -ATP酶活性的组织化学和细胞化学定位。在远侧部的血管壁以及非分泌细胞(星状细胞)与内分泌细胞之间观察到强烈反应。在电子显微镜下,Ca++ -ATP酶反应产物位于星状细胞质膜的细胞外。该反应依赖于Ca++和底物ATP,并通过向标准孵育培养基中添加0.1 mM槲皮素而减弱。孵育前对切片进行预热可完全抑制酶活性。当在孵育培养基中用不同浓度的Mg++替代Ca++时,反应总是减弱。孵育培养基中的Ca++和Mg++也会减弱反应。内分泌细胞的质膜未显示出可检测到的Ca++ -ATP酶活性。结合细胞外Ca++浓度的调节对Ca++ -ATP酶活性的功能进行了讨论,细胞外Ca++浓度的调节不仅对内分泌细胞的分泌过程似乎很重要,而且对腺垂体的代谢也很重要。