Evidence map›Paper›PMID 20181668›Full record

ReviewAmerican journal of physiology. Renal physiology2010

Role of the energy sensor AMP-activated protein kinase in renal physiology and disease.

Kenneth R Hallows, Peter F Mount, Núria M Pastor-Soler, David A Power

Open access · greenAbstract readReview
In one paragraph

Review in American journal of physiology. Renal physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
10.4field-weighted citation impact, top 1% 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

81 citing papers in PubMed, 157 citations in OpenAlex.

  1. Metformin Therapy in Autosomal Dominant Polycystic Kidney Disease: A Feasibility Study.American journal of kidney diseases : the official journal of the National Kidney Foundation · 2022
    Trial
  2. Review
  3. Article
  4. Article
  5. Phosphate and Inflammation in Health and Kidney Disease.International journal of molecular sciences · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. Reprogramming of Energy Metabolism in HumanInternational journal of molecular sciences · 2024
    Article
  10. Article
  11. Article
  12. International journal of molecular sciences · 2022
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Review

21 more citing papers are in PubMed but not listed here.

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

4 authors at 3 institutions in 2 countries.

Kenneth R HallowsRenal-Electrolyte Division, Department of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, USA.
Peter F Mount
Núria M Pastor-Soler
David A Power
University of Pittsburgh · USAustin Health · AUUniversity of Melbourne · AU

Funding

Mechanisms and Relevance of Sodium Transport Regulation by AMPKR01DK075048 · NIDDK · UNIVERSITY OF SOUTHERN CALIFORNIA · PI HALLOWS, KENNETH R · 2007 to 2015
$2.5M
Mechanisms of Kinase-dependent Regulation of the V-ATPase in KidneyR01DK084184 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI PASTOR-SOLER, NURIA M. · 2009 to 2013
$1.5M
NIDDK NIH HHS R01 DK075048NIDDK NIH HHS R01 DK084184
6 · The paper itself

Abstract

The ultrasensitive energy sensor AMP-activated protein kinase (AMPK) orchestrates the regulation of energy-generating and energy-consuming pathways. AMPK is highly expressed in the kidney where it is reported to be involved in a variety of physiological and pathological processes including ion transport, podocyte function, and diabetic renal hypertrophy. Sodium transport is the major energy-consuming process in the kidney, and AMPK has been proposed to contribute to the coupling of ion transport with cellular energy metabolism. Specifically, AMPK has been identified as a regulator of several ion transporters of significance in renal physiology, including the cystic fibrosis transmembrane conductance regulator (CFTR), the epithelial sodium channel (ENaC), the Na(+)-K(+)-2Cl(-) cotransporter (NKCC), and the vacuolar H(+)-ATPase (V-ATPase). Identified regulators of AMPK in the kidney include dietary salt, diabetes, adiponectin, and ischemia. Activation of AMPK in response to adiponectin is described in podocytes, where it reduces albuminuria, and in tubular cells, where it reduces glycogen accumulation. Reduced AMPK activity in the diabetic kidney is associated with renal accumulation of triglyceride and glycogen and the pathogenesis of diabetic renal hypertrophy. Acute renal ischemia causes a rapid and powerful activation of AMPK, but the functional significance of this observation remains unclear. Despite the recent advances, there remain significant gaps in the present understanding of both the upstream regulating pathways and the downstream substrates for AMPK in the kidney. A more complete understanding of the AMPK pathway in the kidney offers potential for improved therapies for several renal diseases including diabetic nephropathy, polycystic kidney disease, and ischemia-reperfusion injury.

Indexed as

AMP-Activated Protein KinasesAnimalsEnergy MetabolismHomeostasisHumansIon TransportKidneyKidney DiseasesModels, AnimalSignal TransductionAMP-Activated Protein Kinases

Identifiers

PMID20181668
PMCPMC2867412
OpenAlexW2158809211

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.