Salem A O, Kressin M, Schnorr B
Department of Veterinary Anatomy, Histology and Embryology, University of Giessen, FRG.
Acta Anat (Basel). 1991;142(3):242-5. doi: 10.1159/000147196.
The localization of calcium adenosine triphosphatase (Ca(2+)-ATPase) was determined histo- and ultracytochemically in the gizzard gland cells of the adult domestic fowl. Surface and chief gland cells exhibited faint and inconstant basolateral activity in contrast to basal cells, whose basolateral cell membrane constantly showed deposition on the external side. Intracellular enzyme activity was localized on the luminal aspect of Golgi membranes in all types of gland cells. Lysosomes also reacted positive for Ca(2+)-ATPase. Neither membranes of secretory vesicles nor cortical cytoplasm of the secretory pole exhibited enzyme activity. From these results it is speculated that calcium is not essentially involved in the secretion of the koilin membrane in terms of storage of the secretory material, transport to the secretory surface and release into the lumen. Ca(2+)-ATPase activity rather seems to be related to differentiation and maturation processes and to intracellular storage of Ca2+.
采用组织化学和超微细胞化学方法，对成年家鸡肌胃腺细胞中钙三磷酸腺苷酶（Ca(2+)-ATPase）进行了定位研究。与基底细胞相比，表面腺细胞和主腺细胞的基底外侧活性微弱且不稳定，基底细胞的基底外侧细胞膜外侧持续出现沉积物。在所有类型的腺细胞中，细胞内酶活性定位于高尔基膜的腔面。溶酶体对Ca(2+)-ATPase也呈阳性反应。分泌小泡膜和分泌极的皮质细胞质均未表现出酶活性。从这些结果推测，就分泌物质的储存、运输到分泌表面以及释放到管腔而言，钙在壳膜分泌过程中并非起关键作用。Ca(2+)-ATPase活性似乎与分化和成熟过程以及细胞内Ca2+的储存有关。
