C. A. Kanashiro

TL;DR: Results indicate that AT1 residues Val254, His256, and Phe259 are not involved in ligand binding but participate in signal transduction, and it is suggested that, in addition to the His256 imidazole ring, the Phe 259 aromatic ring interacts with the AII's Phe8, thus contributing to the signal-triggering mechanism.

TL;DR: The results suggest that conformational change of the AII-receptor complex within the plasma membrane, but not internalization, is the most important factor responsible for tachyphylaxis.

TL;DR: The results suggest that angiotensin II desensitization involves protein kinase C inhibition of a step in the stimulus-response chain that is subsequent to phospholipase C-activation.

TL;DR: A construct containing a "Flag" sequence added to the N-terminus of the rat AT1 receptor was stably expressed in Chinese hamster ovary cells and quantified in the cell membrane by confocal microscopy, suggesting migration of the ligand-receptor complex to the nuclear membrane.

TL;DR: The hypothesis that activation of protein kinase C is responsible for the desensitization and that tachyphylaxis is due to the slow dissociation of angiotensin II from a postulated Na+-dependent regulatory site on the receptor is supported.