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(Received for publication, February 26, 1996, and in revised form, April 26, 1996)
From the Natriuretic peptide receptor C (NPR-C) is a
disulfide-linked homodimer with an approximately 440-amino acid
extracellular domain and a 37-amino acid cytoplasmic domain; it
functions in the internalization and degradation of bound ligand. The
use of NPR-C-specific natriuretic peptide analogs has implicated this
receptor in mediating the inhibition of adenylyl cyclase or activation
of phospholipase C. In the present studies we have investigated the
role of the cytoplasmic domain of NPR-C in signaling the inhibition of
adenylyl cyclase. Polyclonal rabbit antisera were raised against a
37-amino acid synthetic peptide (R37A) corresponding to the cytoplasmic
domain of NPR-C. Incubation of anti-R37A with rat heart particulate
fractions blocked atrial natriuretic peptide-dependent
inhibition of adenylyl cyclase. The cytoplasmic domain peptides R37A
and TMC (10 residues of transmembrane domain appended on R37A) were
equipotent in inhibiting adenylyl cyclase (Ki ~1
nM) in a GTP-dependent manner, whereas K37E (a
scrambled peptide control for R37A) did not inhibit adenylyl cyclase
activity. Prior incubation of membranes with pertussis toxin blocked
R37A or TMC inhibition of cAMP production. Detergent solubilization of
the rat heart particulate fraction destroyed natriuretic peptide
inhibition of adenylyl cyclase, but TMC was able to inhibit cAMP
production in a dose-dependent manner. Our results provide
evidence that the 37-amino acid cytoplasmic domain of NPR-C is
sufficient for signaling inhibition of adenylyl cyclase through a
pertussis toxin-sensitive G protein.
Volume 271, Number 32,
Issue of August 9, 1996
pp. 19324-19329
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
INVOLVEMENT OF A PERTUSSIS TOXIN-SENSITIVE G PROTEIN
,
Department of Physiology, University of
Montreal, Montreal, Quebec H3C-3J7, Canada and the
¶ Cardiovascular Research Department, Genentech,
South San Francisco, California 94080
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