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Vol. 61, Issue 4, 768-777, April 2002
Molecular Endocrinology Laboratory, Baker Medical Research
Institute, Melbourne, Australia (A.C.H., H.Q., L.P., W.G.T.);
Department of Pharmacology, University of Melbourne, Parkville,
Australia (J.Z., M.J.L.); Department of Molecular Cardiology, Cleveland
Clinic Foundation, Cleveland, Ohio (S.-I.M., S.K.); and Department of
Gastrology and Nutrition, Murdoch Childrens Research Institute, Royal
Children's Hospital, Parkville, Australia (B.R.S.)
Binding of the peptide hormone angiotensin II (AngII) to the type 1 (AT1A) receptor and the subsequent activation of
phospholipase C-mediated signaling, involves specific determinants
within the AngII peptide sequence. In contrast, the contribution of
such determinants to AT1A receptor internalization,
phosphorylation and activation of mitogen-activated protein kinase
(MAPK) signaling is not known. In this study, the internalization of an
enhanced green fluorescent protein-tagged AT1A receptor
(AT1A-EGFP), in response to AngII and a series of
substituted analogs, was visualized and quantified using confocal
microscopy. AngII-stimulation resulted in a rapid,
concentration-dependent internalization of the chimeric receptor, which
was prevented by pretreatment with the nonpeptide AT1
receptor antagonist EXP3174. Remarkably, AT1A receptor
internalization was unaffected by substitution of AngII side chains,
including single and double substitutions of Tyr4 and
Phe8 that abolish phospholipase C signaling through the
receptor. AngII-induced receptor phosphorylation was significantly
inhibited by several substitutions at Phe8 as well as
alanine replacement of Asp1. The activation of MAPK was
only significantly inhibited by substitutions at position eight in the
peptide and specific substitutions did not equally inhibit inositol
phosphate production, receptor phosphorylation and MAPK activation.
These results indicate that separate, yet overlapping, contacts made
between the AngII peptide and the AT1A receptor
select/induce distinct receptor conformations that preferentially affect particular receptor outcomes. The requirements for
AT1A receptor internalization seem to be less stringent
than receptor activation and signaling, suggesting an inherent bias
toward receptor deactivation.
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