Evidence map›Paper›PMID 37399424›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

Discovery of another mechanism for the inhibition of particulate guanylyl cyclases by the natriuretic peptide clearance receptor.

Dianxin Liu, Ryan P Ceddia, Wei Zhang, Fubiao Shi, Huafeng Fang, Sheila Collins

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 24% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Dianxin LiuDivision of Cardiovascular Medicine, Department of Medicine, Vanderbilt University Medical Center, Nashville TN 37232.
Ryan P CeddiaDivision of Cardiovascular Medicine, Department of Medicine, Vanderbilt University Medical Center, Nashville TN 37232.ORCID 0000-0001-7743-1755
Wei ZhangDivision of Cardiovascular Medicine, Department of Medicine, Vanderbilt University Medical Center, Nashville TN 37232.
Fubiao ShiDivision of Cardiovascular Medicine, Department of Medicine, Vanderbilt University Medical Center, Nashville TN 37232.
Huafeng FangIntegrative Metabolism Program, Sanford Burnham Prebys Medical Discovery Institute, Orlando, FL 32827.
Sheila CollinsDivision of Cardiovascular Medicine, Department of Medicine, Vanderbilt University Medical Center, Nashville TN 37232.ORCID 0000-0001-6812-8551
Vanderbilt University Medical Center · USSanford Burnham Prebys Medical Discovery Institute · USVanderbilt University · US

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI Ben Ho Park · 1995 to 2026
$172.8M
Translational Analysis CoreP30DK058404 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MARY Kay WASHINGTON · 2002 to 2026
$29.9M
Vanderbilt Diabetes Research CenterP30DK020593 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI OWEN P MCGUINNESS · 2012 to 2026
$29.3M
Natriuretic peptide receptors, adipose browning and energy expenditureR01DK103056 · NIDDK · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI COLLINS, SHEILA · 2014 to 2017
$1.7M
The role of phosphodiesterase 9 in the regulation of adipocyte thermogenesis and obesity-related diseasesF32DK116520 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI CEDDIA, RYAN PATRICK · 2017 to 2020
$190k
NCI NIH HHS P30 CA068485NIDDK NIH HHS F32 DK116520NIDDK NIH HHS P30 DK020593NIDDK NIH HHS P30 DK058404NIDDK NIH HHS R01 DK103056
6 · The paper itself

Abstract

The cardiac natriuretic peptides (NPs) control pivotal physiological actions such as fluid and electrolyte balance, cardiovascular homeostasis, and adipose tissue metabolism by activating their receptor enzymes [natriuretic peptide receptor-A (NPRA) and natriuretic peptide receptor-B (NPRB)]. These receptors are homodimers that generate intracellular cyclic guanosine monophosphate (cGMP). The natriuretic peptide receptor-C (NPRC), nicknamed the clearance receptor, lacks a guanylyl cyclase domain; instead, it can bind the NPs to internalize and degrade them. The conventional paradigm is that by competing for and internalizing NPs, NPRC blunts the ability of NPs to signal through NPRA and NPRB. Here we show another previously unknown mechanism by which NPRC can interfere with the cGMP signaling function of the NP receptors. By forming a heterodimer with monomeric NPRA or NPRB, NPRC can prevent the formation of a functional guanylyl cyclase domain and thereby suppress cGMP production in a cell-autonomous manner.

Indexed as

Guanylate CyclaseReceptors, Atrial Natriuretic FactorAtrial Natriuretic FactorCyclic GMPNatriuretic PeptidesReceptors, PeptideSignal TransductionAtrial Natriuretic FactorCyclic GMPGuanylate CyclaseNatriuretic PeptidesReceptors, Atrial Natriuretic FactorReceptors, Peptidenatriuretic peptideNPRANPRBNPRCreceptors

Identifiers

PMID37399424
PMCPMC10334801
OpenAlexW4382931950

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.