Dolapchieva S
Department of Anatomy and Histology, Medical University, Sofia, Bulgaria.
Eur J Morphol. 1995 Jul;33(3):247-55.
In order to reveal and characterize Na+,K(+)-ATPase distribution in axon-myelin-Schwann cell units of sciatic nerves of adult and 15 days old Wistar rats, the ultracytochemical lead-paranitrophenyl-phosphatase technique was used. The activity of K(+)-dependent paranitrophenylphosphatase, a component of Na+,K(+)-ATPase, was found on the cytoplasmic side of the axolemma and Schwann cell plasma membrane, as well as on the major dense lines of the myelin sheath. K(+)-paranitrophenylphosphatase activity was localized also at the axoplasmic profiles and at the Golgi apparatus of the Schwann cells. Ouabain inhibition made it possible to distinguish alpha 1 from alpha 2 and alpha 3 isoforms of Na+,K(+)-ATPase. The results suggest that the activity of the axolemma and myelin sheath is determined by alpha 2 and alpha 3 isozymes. The enzyme activity of the Schwann cell plasma membrane and Golgi complex was not visibly influenced by ouabain. These results suggest that the activity of these glial structures is determined mainly by alpha 1 isozyme.
为了揭示和表征成年及15日龄Wistar大鼠坐骨神经轴突-髓鞘-施万细胞单元中Na⁺,K⁺-ATP酶的分布,采用了超细胞化学对硝基苯磷酸铅技术。作为Na⁺,K⁺-ATP酶组分的K⁺依赖性对硝基苯磷酸酶活性,在轴膜和施万细胞质膜的胞质侧以及髓鞘的主致密线上被发现。K⁺-对硝基苯磷酸酶活性也定位于施万细胞的轴质轮廓和高尔基体。哇巴因抑制使得区分Na⁺,K⁺-ATP酶的α1、α2和α3同工型成为可能。结果表明,轴膜和髓鞘的活性由α2和α3同工酶决定。施万细胞质膜和高尔基体复合体的酶活性未受到哇巴因的明显影响。这些结果表明,这些神经胶质结构的活性主要由α1同工酶决定。