Evidence map›Paper›PMID 23430254›Full record

ArticleThe Journal of biological chemistry2013

Renal proteinase-activated receptor 2, a new actor in the control of blood pressure and plasma potassium level.

Luciana Morla, Gaëlle Brideau, Marc Fila, Gilles Crambert, Lydie Cheval, Pascal Houillier, Sureshkrishna Ramakrishnan, Martine Imbert-Teboul, Alain Doucet

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Serine proteases and protease-activated receptors signaling in the kidney.American journal of physiology. Cell physiology · 2025
    Review
  2. Review
  3. Article
  4. Article
  5. Kidney stone formation in a novel murine model of polycystic kidney disease.American journal of physiology. Renal physiology · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Protease-activated receptors in kidney disease progression.American journal of physiology. Renal physiology · 2016
    Review
  12. Article
  13. Review
  14. Article
  15. 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

9 authors at 2 institutions in 2 countries.

Luciana MorlaCentre de Recherche des Cordeliers, Université Pierre et Marie Curie, Université Paris-Descartes, INSERM (UMRS872) and Centre National de la Recherche Scientifique (ERL7226), 75270 Paris cedex 06.
Gaëlle BrideauCentre de Recherche des Cordeliers, Université Pierre et Marie Curie, Université Paris-Descartes, INSERM (UMRS872) and Centre National de la Recherche Scientifique (ERL7226), 75270 Paris cedex 06.
Marc FilaCentre de Recherche des Cordeliers, Université Pierre et Marie Curie, Université Paris-Descartes, INSERM (UMRS872) and Centre National de la Recherche Scientifique (ERL7226), 75270 Paris cedex 06.
Gilles CrambertCentre de Recherche des Cordeliers, Université Pierre et Marie Curie, Université Paris-Descartes, INSERM (UMRS872) and Centre National de la Recherche Scientifique (ERL7226), 75270 Paris cedex 06.
Lydie ChevalCentre de Recherche des Cordeliers, Université Pierre et Marie Curie, Université Paris-Descartes, INSERM (UMRS872) and Centre National de la Recherche Scientifique (ERL7226), 75270 Paris cedex 06.
Pascal HouillierCentre de Recherche des Cordeliers, Université Pierre et Marie Curie, Université Paris-Descartes, INSERM (UMRS872) and Centre National de la Recherche Scientifique (ERL7226), 75270 Paris cedex 06; Faculté de Médecine, Université Paris-Descartes, 75006 Paris; Département de Physiologie, Hôpital Européen Georges Pompidou, Assistance Publique-Hôpitaux de Paris, 75004 Paris, France.
Sureshkrishna RamakrishnanCentre de Recherche des Cordeliers, Université Pierre et Marie Curie, Université Paris-Descartes, INSERM (UMRS872) and Centre National de la Recherche Scientifique (ERL7226), 75270 Paris cedex 06.
Martine Imbert-TeboulCentre de Recherche des Cordeliers, Université Pierre et Marie Curie, Université Paris-Descartes, INSERM (UMRS872) and Centre National de la Recherche Scientifique (ERL7226), 75270 Paris cedex 06.
Alain DoucetCentre de Recherche des Cordeliers, Université Pierre et Marie Curie, Université Paris-Descartes, INSERM (UMRS872) and Centre National de la Recherche Scientifique (ERL7226), 75270 Paris cedex 06. Electronic address: alain.doucet@crc.jussieu.fr.
Inserm · FRDélégation Paris 5 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteinase-activated receptor 2 (PAR2) is a G protein-coupled membrane receptor that is activated upon cleavage of its extracellular N-terminal domain by trypsin and related proteases. PAR2 is expressed in kidney collecting ducts, a main site of control of Na(+) and K(+) homeostasis, but its function remains unknown. We evaluated whether and how PAR2 might control electrolyte transport in collecting ducts, and thereby participate in the regulation of blood pressure and plasma K(+) concentration. PAR2 is expressed at the basolateral border of principal and intercalated cells of the collecting duct where it inhibits K(+) secretion and stimulates Na(+) reabsorption, respectively. Invalidation of PAR2 gene impairs the ability of the kidney to control Na(+) and K(+) balance and promotes hypotension and hypokalemia in response to Na(+) and K(+) depletion, respectively. This study not only reveals a new role of proteases in the control of blood pressure and plasma potassium level, but it also identifies a second membrane receptor, after angiotensin 2 receptor, that differentially controls sodium reabsorption and potassium secretion in the late distal tubule. Conversely to angiotensin 2 receptor, PAR2 is involved in the regulation of sodium and potassium balance in the context of either stimulation or nonstimulation of the renin/angiotensin/aldosterone system. Therefore PAR2 appears not only as a new actor of the aldosterone paradox, but also as an aldosterone-independent modulator of blood pressure and plasma potassium.

Indexed as

Gene Expression RegulationAldosteroneAnimalsBlood PressureCalciumDiureticsHomeostasisKidneyMaleMiceMice, TransgenicPerfusionPotassiumRatsRats, Sprague-DawleyReceptor, PAR-2AldosteroneCalciumDiureticsPotassiumReceptor, PAR-2Sodium

Identifiers

PMID23430254
PMCPMC3617255
OpenAlexW2132302426

What OpenQuestion holds

Textmetadata
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.