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Hormonal induction of low affinity receptor guanylyl cyclase.
Author(s) -
Jewett J.R.,
Koller K.J.,
Goeddel D.V.,
Lowe D.G.
Publication year - 1993
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1993.tb05711.x
Subject(s) - biology , guanylate cyclase , soluble guanylyl cyclase , receptor , hormone , biochemistry
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.