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Adrenocorticoid regulation of sodium potassium atpase in adult rat kidney effects on post translational processing and mrna abundance

, : Adrenocorticoid regulation of sodium potassium atpase in adult rat kidney effects on post translational processing and mrna abundance. Acta Physiologica Scandinavica 145(2): 85-91

The mechanisms by which adreno-corticoid hormones regulate Na+,K+-ATPase in adult kidney were studied in adrenalectomized (Adx) rats. Five days after adrenalectomy, Na+,K+-ATPase activity was significantly reduced in the renal cortex homogenate (C = 13.0 .+-. 0.8 vs. Adx = 7.1 .+-. 0.7 .mu.mol Pi mg-1 protein h-) and in renal microsomes (C = 30.3 .+-. 1.9 vs Adx = 14.6 .+-. 1.3 .mu.mol Pi mg-1 protein h-). Glucocorticoid replacement treatment of adrenalectomized rats with betamethasone (20 .mu.g kg-1 body wt twice daily for 5 days) effectively counteracted the observed reduction in Na+,K+-ATPase activity. In cortical homogenate the protein level of .alpha.1 and .beta.1 subunits measured in immunoblots was not significantly different in Adx and control rats, indicating that 5 days after adrenalectomy the .alpha.1 and .beta.1 subunits were present in renal cortical cells to almost normal extent but could not be assembled into a transmembrane functional unit. In support of this conclusion we found that the protein level of both the .alpha.1 and .beta.1 subunits was significantly lower (P < 0.001 for both subunits) in microsomes from Adx than in control rats. The mRNA abundance for .alpha.1 and .beta.1 subunits were not lower in Adx as compared to control rats 1 and 5 days after surgery. However, if Adx rats were given a single dose of betamethasone (600 .mu.g kg-1 body wt), a significant 2-fold increase in both .alpha.1 and .beta.1 mRNAs was observed (P < 0.05 for both subunits). These data suggest that glucocorticoids can upregulate the mRNA of both Na+,K+-ATPase subunits but that the low renal Na+,K+-ATPase activity in adult Adx rats is mainly due to loss of glucocorticoid regulation of the post-translational processing of the enzyme.


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