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J. Biol. Chem., Vol. 266, Issue 7, 4088-4093, 03, 1991
M Chinkers, S Singh and DL Garbers
Atrial natriuretic peptide (ANP) binds to a transmembrane receptor having
intrinsic guanylyl cyclase activity; this receptor has been designated
GC-A. Binding of ANP to GC-A stimulates its catalytic activity, resulting
in increased production of the second messenger, cyclic GMP. Here we show
that GC-A can be expressed in insect cells using a recombinant baculovirus
and that the expressed protein retained its abilities to bind ANP and to
function as an ANP-activated guanylyl cyclase. In addition, GC-A produced
in insect cells was absolutely dependent on the presence of adenine
nucleotides for activation by ANP. Millimolar concentrations of ATP were
required for optimal activation. The relative potencies of various
nucleotides for activation was adenosine 5'-O-(thiotriphosphate) greater
than ATP greater than ADP, adenosine 5'-(beta, gamma-imino)triphosphate
greater than ADP beta S. AMP had no effect. These studies suggest that
binding of an adenine nucleotide, most likely to the protein kinase-like
domain of GC-A, is absolutely required for ANP activation. Regulation of
guanylyl cyclase activation by adenine nucleotides represents a novel
mechanism for the modulation of signal transduction, possibly analogous in
some respects to the role of guanine nucleotides and G proteins in the
regulation of adenylyl cyclase activity.
Adenine nucleotides are required for activation of rat atrial natriuretic peptide receptor/guanylyl cyclase expressed in a baculovirus system
Howard Hughes Medical Institute, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0295.
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