Vasopressin, angiotensin and adrenergic receptors of rat liver Golgi fractions--molecular weight of the angiotensin-receptor irreversible complex after in vitro and in vivo labelling.

The binding of vasopressin, angiotensin II and prazosin (alpha 1-adrenergic antagonist) to purified heavy (GH) and (intermediate + light) (GI + L) rat liver Golgi fractions was studied. The three types of ligands showed a saturable and specific binding in Golgi fractions; the maximal specific binding of [3H]vasopressin, [3H]prazosin and [125I]Sar-N3-Phe-angiotensin II was respectively 5-10%, 20-30% and 30-40% of that detected in purified plasma membranes. The apparent binding affinities of the three ligands were the same whether determined in Golgi fractions or plasma membranes. The presence of vasopressin, alpha 1-adrenergic and angiotensin receptors in very different proportions, as compared to the amount of receptor detected in plasma membranes, in GH and GI + L Golgi fractions was not compatible with the idea that a plasma membrane impurity accounted for the detection of receptor in the purified intracellular particulate fractions. In vivo injection of [125I]Sar-N3-Phe-angiotensin II resulted in a receptor-mediated endocytosis of the iodo-angiotensin analog into the GH and GI + L Golgi fractions. The apparent molecular weight of the irreversible complex, [125I]angiotensin-receptor, was estimated in subcellular fractions using SDS-PAGE electrophoresis. This value was identical after either in vivo or in vitro labelling (MW = 63,000) and was indistinguishable from the molecular weight of the irreversible hormone receptor complex present in the plasma membranes.