Angiotensin II receptors in chromatin.

When isolated rat hepatic nuclei or bovine thymus nuclei were incubated with 125I-angiotensin II (ANG II) in the presence or absence of cold hormone, displaceable binding was consistently detected in micrococcal nuclease generated fragments Nanomolar concentrations of ANG II produced detectable displacement. Little or no specific binding was found when nuclei were first digested and then treated with hormone, suggesting that ANG II solubilizes its own receptor. The binding moiety was partially purified by DNP gel electrophoresis. These studies indicate the existence in chromatin of high affinity receptors for ANG II, and further suggest that hormone binding to these receptors produces conformational changes in chromatin similar to those seen during enhanced transcriptional activity. Thus, the present studies suggest the existence of functional intracellular renin-angiotensin systems.