Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Adenine nucleotides decrease the apparent Km of endogenous natriuretic peptide receptors for GTP.

Laura K Antos1, Lincoln R Potter

  • 1Dept. of Biochemistry, Molecular Biology and Biophysics, Univ. of Minnesota, 6-155 Jackson, 321 Church St. SE, Minneapolis, MN 55455, USA.

American Journal of Physiology. Endocrinology and Metabolism
|September 13, 2007
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The Concise Guide to PHARMACOLOGY 2025/26: Catalytic receptors.

British journal of pharmacology·2025
Same author

Phosphorylation-Dependent Regulation of Guanylyl Cyclase (GC)-A and Other Membrane GC Receptors.

Endocrine reviews·2024
Same author

The Concise Guide to PHARMACOLOGY 2023/24: Catalytic receptors.

British journal of pharmacology·2023
Same author

Novel enhancers of guanylyl cyclase-A activity acting via allosteric modulation.

British journal of pharmacology·2023
Same author

Vicinal glutamates are better phosphomimetics: Phosphorylation is required for allosteric activation of guanylyl cyclase-A.

Frontiers in molecular neuroscience·2022
Same author

Epitope-tagged and phosphomimetic mouse models for investigating natriuretic peptide-stimulated receptor guanylyl cyclases.

Frontiers in molecular neuroscience·2022

Adenosine triphosphate (ATP) enhances natriuretic peptide receptor (NPR) activity by lowering GTP affinity, not by direct phosphorylation. This mechanism boosts receptor function over time in endogenous settings.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Natriuretic peptide receptors A (NPR-A) and B (NPR-B) are crucial for natriuretic peptide signaling, primarily through cGMP synthesis.
  • Adenosine triphosphate (ATP) is known to increase NPR activity, but the underlying mechanism remains unclear.

Purpose of the Study:

  • To investigate the mechanism by which ATP enhances NPR-A and NPR-B activity in endogenous settings.
  • To determine if ATP's effect is phosphorylation-dependent and to identify key regions involved in ATP modulation.

Main Methods:

  • Kinetic analysis of NPR-A and NPR-B activity with ATP and AMPPNP.
  • Site-directed mutagenesis of putative ATP-binding sites and phosphorylation sites.
  • Assays of guanylyl cyclase activity in response to ANP and ATP.

Related Experiment Videos

Main Results:

  • Both ATP and AMPPNP significantly reduced the apparent K(m) for GTP for both NPR-A and NPR-B, without affecting V(max).
  • ATP's effect was independent of known phosphorylation sites.
  • Mutating K535A abolished ATP responsiveness, while mutating the 630-KSS region eliminated cyclase activity entirely.

Conclusions:

  • ATP is not essential for the initial activation of NPRs but enhances their activity over time.
  • The mechanism involves a reduction in the apparent K(m) for GTP, suggesting a role for specific residues like K535 in ATP modulation.