Hormonal induction of low affinity receptor guanylyl cyclase.

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