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Vol. 273, Issue 2, 1032-1037, January 9, 1998
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From the A novel membrane form of guanylyl cyclase (GC-G)
has been identified through the isolation of a full-length cDNA
clone; it is predicted to contain an extracellular ligand binding
domain, a single transmembrane segment, and intracellular protein
kinase-like and cyclase catalytic domains. That GC-G represents a
guanylyl cyclase was confirmed by both transient expression in COS-7
cells and stable expression in H293 cells. Endogenous cyclic GMP
concentrations of transfected or stable cells, however, were much
higher than control cells, suggesting an inability of the cells to
effectively regulate GC-G cyclase activity. Of six Cys residues found
within the extracellular domain of guanylyl cyclase-A (GC-A), the
receptor for atrial natriuretic peptide, five are conserved within
GC-G. Ligands for the other cyclase receptors, nevertheless, failed to
stimulate GC-G expressed in transient or stable cells, suggesting that
the unknown ligands possess a structure different from the natriuretic
peptides or heat-stable enterotoxins. 125I-ANP also
failed to bind to H293 cells overexpressing GC-G. Based on Northern
hybridization, mRNA for GC-G was predominantly expressed in lung,
intestine, and skeletal muscle. Using the candidate gene approach to
potentially define function, the gene for GC-G was mapped to the distal
region of mouse chromosome 19 (syntenic with human chromosome 10q), but
no human genetic defect has been ascribed to the GC-G locus. The
finding of a new membrane form of guanylyl cyclase in peripheral
tissues suggests the existence of another family or subfamily of
ligands that signal through elevations of cGMP.
Howard Hughes Medical Institute and the
Department of Pharmacology, University of Texas
Southwestern Medical Center, Dallas, Texas 75235-9050
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