Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Distribution of sodium-potassium ATPase in the rat testis and epididymis. 169 57

Myoid cells of the human caput epididymidis are replaced by large cells with ultrastructural features of smooth muscle cells (SMC) in chronic obstruction of the male genital tract. To evaluate whether these cellular changes are associated with different functional phenotypes we analysed the immunohistochemical expression of myosin heavy chain isoforms and of extracellular matrix (EM) components in the human caput epididymidis contractile cells in normal and in obstructed epididymides. Normal caput epididymidis myoid cells expressed a scattered immunostaining for SM2, marker of differentiated contractile SMC, while no staining was detected for SMemb (the non-muscle-type myosin heavy chain isoform) and for its transcription factor BTEB2, markers of undifferentiated proliferating SMC. A faint immunoreaction (IR) for EM was observed in the peritubular wall of the normal caput. In the contractile wall of the obstructed caput epididymidis a strong IR was detected for all myosin heavy chain isoforms as well as for collagen type IV and for fibronectin, markers for a secretory function of SMC. These findings, unknown in other models of SMC pathophysiology, suggest that myoid cells resume the molecular machinery of both mature SMC and of differentiating/secretory cells in the chronic obstruction of the human caput. Contractile cells of the epididymal duct represent a unique model to study the plasticity of SMC.
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PMID:Immunophenotypical characterization of contractile cells in caput epididymidis of men affected by congenital or post-inflammatory obstructive azoospermia. 1573 98