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- W58882877 abstract "This chapter describes aldosterone binding proteins (ABP). Conventional cell fractionation techniques were used to study the specificity of aldosterone-binding systems in the kidney of adrenalectomized rats. The aldosterone-metabolites, physiologically inert analogs, were used as the indicators of nonspecific steroidal binding sites. Isolated renal nuclei were found to contain aldosterone-binding sites that were saturable within the physiological range of plasma aldosterone concentrations. If the cytosol and nuclear ABP's constitute the physiological receptor mechanism, one possible basis for tissue specificity in the response to mineralocorticoids would be the presence of these receptors. Accordingly, cytosol and nuclear ABP content was determined in rat kidney, duodenal mucosa, liver, spleen and brain. The ABP content of both the cytosol and nuclear fractions, expressed as moles of 3H-aldosterone bound per mg of protein, was highest in the kidney and duodenal mucosa, and was significantly lower in the spleen, liver and brain. The relative affinities of d-aldosterone, 9α-fluorocortisol, isoaldosterone-17α, and estradiol-17β were similar in these fractions in all of the organs. Thus, regardless of ABP content, the mine-ralocorticoids competed for the 3H-aldosterone binding sites but the inactive steroids failed to do so. The significance of lesser quantities of ABP in spleen, liver and brain may bear on their ability to respond to the steroid. Although it is known that the kidney and duodenal mucosa are the target tissues for mineralocorticoids, it cannot be asserted with equal certainty that active extrusion of Na+ from the intracellular phase of spleen, liver and brain is not stimulated by mineralocorticoids or that the response is less than in the kidney or gut." @default.
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- W58882877 date "1971-01-01" @default.
- W58882877 modified "2023-09-23" @default.
- W58882877 title "Aldosterone Binding Proteins" @default.
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- W58882877 doi "https://doi.org/10.1016/b978-0-08-017578-2.50020-1" @default.
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