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PMID: 8095019 Published · ppublish English Journal Article

Hormonal induction of low affinity receptor guanylyl cyclase.

The EMBO journal ·Vol. 12 ·No. 2 ·1993-02-00 ·Pages 769-77

Jewett JR, Koller KJ, Goeddel DV, Lowe DG

Abstract

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.

MeSH Terms
Adenosine Triphosphate/metabolism Amiloride/pharmacology Atrial Natriuretic Factor/metabolism Cells, Cultured Cloning, Molecular Enzyme Induction Guanylate Cyclase/biosynthesis Humans Models, Biological Phosphotransferases/metabolism Protein Binding/drug effects Receptors, Atrial Natriuretic Factor/metabolism Signal Transduction Substrate Specificity
Chemicals
Amiloride Atrial Natriuretic Factor Adenosine Triphosphate Phosphotransferases Guanylate Cyclase Receptors, Atrial Natriuretic Factor
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Jewett J R
Department of Molecular Biology, Genentech, Inc., South San Francisco, CA 94080.
Koller K J
Goeddel D V
Lowe D G
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1993-02-00
Pages
769-77
Language
English
Region
England
NLM ID
8208664
PMCID
PMC413264
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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