Malassiné A
Histochemistry. 1980;65(3):239-48. doi: 10.1007/BF00493173.
The ultrastructural localizations of alkaline phosphatase (ALPase) and of Na+-K+-dependent adenosine triphosphatase (Na+-K+-ATPase) were studied in the placental labyrinth of the cat during the last days of gestation. ALPase activity could be detected in the syncytiotrophoblast but was absent from maternal tissues. Enzyme activity was observed only along plasma membranes of microvilli and absorption tubules on the maternal surface of the syncytium and also on the podocytes-like cytoplasmic processes of the fetal face. The localization of the Na+-K+-ATPase activity as obtained with the method of Ernst was identical with that of ALPase. This activity was not very ouabaine sensitive or K+ dependent, but was almost completely inhibited by levamisole. The strong ALPase activity of the syncytiotrophoblast does not allow a specific detection of Na+-K+-ATPase. However, the localization of these enzymes activities on syncytiotrophoblast surfaces directly related to fetal and maternal capillaries could suggest that these surfaces are associated with transport mechanisms of the trophoblast.
在妊娠最后几天,对猫胎盘迷路中碱性磷酸酶(ALPase)和钠钾依赖性三磷酸腺苷酶(Na⁺-K⁺-ATPase)的超微结构定位进行了研究。在合体滋养层中可检测到ALPase活性,但母体组织中没有。仅在合体滋养层母体表面的微绒毛和吸收小管的质膜上以及胎儿面的足细胞样细胞质突起上观察到酶活性。用恩斯特方法获得的Na⁺-K⁺-ATPase活性定位与ALPase相同。这种活性对哇巴因不太敏感,也不依赖钾,但几乎完全被左旋咪唑抑制。合体滋养层的强ALPase活性不允许特异性检测Na⁺-K⁺-ATPase。然而,这些酶活性在与胎儿和母体毛细血管直接相关的合体滋养层表面的定位可能表明这些表面与滋养层的转运机制有关。