Hormonal induction of low affinity receptor guanylyl cyclase.
We describe a unique transient binding phenomenon for atrial natriuretic peptide (ANP) binding to the natriuretic peptide receptor-A (NPR-A) guanylyl cyclase stably expressed in 293 cells. The time course of ANP binding to intact cells peaked at 15 min followed by a subsequent decrease. Reduced binding was a consequence of an ANP induced low affinity state of NPR-A, and required the receptors' kinase homology domain. In a particulate fraction, ANP-stimulated cGMP production was dependent on ATP as a cofactor, and ATP promoted a lower affinity state. Our findings suggest that the kinase homology domain of NPR-A mediates the regulatory action of ATP, not only for signal transduction, but in the modulation of NPR-A hormone affinity.[1]References
- Hormonal induction of low affinity receptor guanylyl cyclase. Jewett, J.R., Koller, K.J., Goeddel, D.V., Lowe, D.G. EMBO J. (1993) [Pubmed]
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