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J Biol Chem, Vol. 274, Issue 7, 4293-4299, February 12, 1999
From the Howard Hughes Medical Institute and Department of
Pharmacology, University of Texas Southwestern Medical Center,
Dallas, Texas 75235-9050
The fibroblast, a cell central to effective wound
remodeling, not only contains various growth factor receptors but also
high activities of a guanylyl cyclase receptor (GC-B). Here we
demonstrate that marked elevations of cyclic GMP induced by C-type
natriuretic peptide (CNP), the ligand of GC-B, blocks activation of the
mitogen-activated protein kinase cascade in fibroblasts. We also show
that platelet-derived growth factor, fibroblast growth factor, serum,
or Na3VO4 rapidly (within 5 min) and
extensively (up to 85% inhibition) disrupt CNP-dependent
elevations of cyclic GMP. In addition, the mitogens also lower cyclic
GMP concentrations (50% decrease) in cells not treated with CNP.
Cytoplasmic forms of guanylyl cyclase, in contrast to the
CNP-stimulated pathway, are not antagonized by the various mitogens.
The effects of the mitogens on cellular cyclic GMP are fully explained
by a direct and stable inactivation of GC-B. Homogenates obtained from
fibroblasts treated with or without the various mitogens contain
equivalent amounts of GC-B protein, but both ligand-dependent and ligand-independent activity are
markedly (up to 90% inhibition of CNP-dependent activity)
decreased after mitogen addition. The stable inactivation is correlated
with the dephosphorylation of phosphoserine and phosphothreonine
residues of the cyclase receptor. These results not only establish a
specific and reciprocal antagonistic relationship between
mitogen-activated and GC-B-regulated signaling pathways in the
fibroblast but also suggest that one of the earliest events following
mitogen activation of a fibroblast is an interruption of cyclic GMP
production from this receptor.
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