(Hypertension. 1995;25:726-730.)
© 1995 American Heart Association, Inc.
Articles |
Mapping of G Protein Coupling Sites of the Angiotensin II Type 1 Receptor
From the Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tenn (H.S., T.I.); Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan (K.T.); and Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, University of Tokyo (Japan) (T.K.).
Correspondence to Tadashi Inagami, PhD, Department of Biochemistry, Vanderbilt University School of Medicine, 23rd Ave S at Pierce Ave, LH663, Nashville, TN 37232.
Abstract Angiotensin II type 1 (AT1) receptors
have been identified in a wide variety of tissues, including the
kidney, liver, adrenal gland, cardiovascular system, and brain.
AT1 receptors also mediate complex signaling mechanisms
that elicit a diversity of specific physiological effects. The rat
AT1A receptor has seven transmembrane domains and couples
with three distinct G proteins: Gq,
Gi, and Go. But it is unknown which
domains of AT1A couple with and activate each type of G
protein. To identify the domains responsible for the activation of
various types of G protein, we studied the effect of five different
synthetic peptides representing different domains of cytosolic
segments of the rat AT1A receptor on the binding of the
35S-labeled stable analogue of GTP, GTP
S. Peptides P-3,
which is located in the N-terminal region of the putative third
intracellular loop of AT1A (residues 216 through 230), and
P-5 (residues 306 through 320), corresponding to the N-terminal region
of the C-terminal tail, were found to activate purified
Gi1, Gi2, and Go
proteins. These results indicate that not only the third cytosolic loop
but also the C-terminal cytosolic domain of AT1A is
important for Gi1, Gi2, and
Go protein coupling and activation.
Key Words: angiotensin II • receptors, angiotensin • G protein • signal transduction • rats
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