Distribution of sodium‐potassium ATPase in the rat testis and epididymis
- 1 May 1990
- journal article
- research article
- Published by Wiley in Journal of Anatomy
- Vol. 188 (1) , 31-43
- https://doi.org/10.1002/aja.1001880105
Abstract
Sodium‐potassium ATPase (Na+ K+‐ATPase) is a ubiquitous plasma membrane enzyme which uses the hydrolysis of ATP to regulate cellular Na+ and K+ levels and fluid volume. This ion pumping action is also thought to be involved in fluid movement across certain epithelia. There are several different genes for this enzyme, some of which are tissue specific. Using an antibody specific for the catalytic subunit of canine kidney Na+ K+‐ATPase, we have localized immunoreactivity in the seminiferous and epididymal epithelium of rats of various ages. There was no specific staining of 10‐day‐old rat testis. Faint staining was detected at 13 days and appeared to be associated with the borders of Sertoli cells. At 16 days prominent apical and lateral staining but no basal staining of Sertoli cell membranes was observed. This type of distribution continued until spermatids were present in the epithelium. In the adult rat testis, specific staining was detected in Sertoli cell crypts associated with elongating spermatids, and on the apical and lateral Sertoli cell membrane. In some instances immunoreactivity was concentrated at presumed sites of junctional specializations. In the excurrent ducts of immature and mature rats, Na+ K+‐ATPase staining was heavy in the efferent ducts and somewhat lighter in the epididymis. In all regions, the staining was basolateral although there were variations in intensity among the different parts of the epididymis. These results show (1) that rat testis and epididymal Na+ K+‐ATPase share some immunological determinants with the canine enzyme; (2) that the epididymal enzyme is located in the conventional basolateral position; and (3) that the distribution of Sertoli cell Na+ K+‐ATPase is probably apical and lateral rather than basal.Keywords
This publication has 41 references indexed in Scilit:
- Immunofluorescence assessment of the timing of appearance and cellular distribution of Na/K-ATPase during mouse embryogenesisDevelopmental Biology, 1988
- Identification of an endosomal antigen specific to absorptive cells of suckling rat ileum.The Journal of cell biology, 1987
- Localization of Na+,K+-ATPase alpha-subunit to the sinusoidal and lateral but not canalicular membranes of rat hepatocytes.The Journal of cell biology, 1987
- Evidence that the α and α(+) isoforms of the catalytic subunit of (Na+,K+)-ATPase reside in distinct ciliary epithelial cells of the mammalian eyeBiochemical and Biophysical Research Communications, 1987
- Intracellular sorting and polarized cell surface delivery of (Na+,K+)ATPase, an endogenous component of MDCK cell basolateral plasma membranesCell, 1986
- Micropuncture Studies of Receptor-Mediated Endocytosis of Transferrin in the Rat Epididymis1Biology of Reproduction, 1986
- Arrangement and possible function of actin filament bundles in ectoplasmic specializations of ground squirrel Sertoli cellsThe Journal of cell biology, 1985
- Further Observations on the Microfilament Bundles of Sertoli Cell Junctional ComplexesAnnals of the New York Academy of Sciences, 1984
- Study of the interaction between germ cells and Sertoli cells in vitroExperimental Cell Research, 1984
- Thallium interaction with the gastric (K, H)-ATPaseThe Journal of Membrane Biology, 1981