Evidence map›Paper›PMID 24877601›Full record

ArticleMolecular endocrinology (Baltimore, Md.)2014

Convergence of IPMK and LKB1-AMPK signaling pathways on metformin action.

Sookhee Bang, Yong Chen, Rexford S Ahima, Sangwon F Kim

Abstract read
In one paragraph

Article in Molecular endocrinology (Baltimore, Md.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
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

31 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. The Inositol Phosphate System-A Coordinator of Metabolic Adaptability.International journal of molecular sciences · 2022
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Inositol polyphosphate multikinase is a metformin target that regulates cell migration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Pleiotropic Effects of Metformin on Cancer.International journal of molecular sciences · 2018
    Review
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.

Sookhee BangDepartment of Psychiatry and Pharmacology, Center for Neurobiology and Behavior (S.B., Y.C., S.F.K.); and Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism and the Institute for Diabetes, Obesity, and Metabolism (R.S.A.), Perelman School of Medicine at the University of Pennsylvania, Philadelphia, Pennsylvania 19104.
Yong Chen
Rexford S Ahima
Sangwon F Kim

Funding

UNIVERSITY OF PENNSYLVANIA CAN CTR SUPPORT GRANTP30CA016520 · NCI · UNIVERSITY OF PENNSYLVANIA · PI SHELLEY L BERGER · 1985 to 2026
$222.3M
Molecular basis of atypical antipsychotic drugs-induced weight gainR01DK084336 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI KIM, SANGWON F · 2010 to 2014
$1.5M
NCI NIH HHS P30 CA016520NIDDK NIH HHS DK084336NIDDK NIH HHS R01 DK084336
6 · The paper itself

Abstract

Metformin is a biguanide drug that is widely prescribed for type 2 diabetes. Metformin suppresses hepatic gluconeogenesis and increases fatty acid oxidation. Although studies have suggested that metformin acts, at least in part, via activation of the liver kinase B1 (LKB1)/AMP-activated protein kinase (AMPK) pathway, the specific molecular mechanisms underlying metformin's regulation of glucose and lipid metabolism have not been well delineated. Recently, we have shown that inositol polyphosphate multikinase (IPMK) plays an important role in cellular energy metabolism and glucose-mediated AMPK regulation. Here we investigated the role of IPMK in metformin-induced AMPK activation. We observed that metformin-mediated activation of AMPK was impaired in the absence of IPMK. Overexpression of wild-type IPMK was sufficient to restore LKB1-AMPK activation by either metformin or AICAR in IPMK(-/-) murine embryonic fibroblast cells, suggesting that IPMK may act as an upstream regulator of LKB1-AMPK signaling in response to metformin. Moreover, this regulation was mediated by protein-protein interaction between IPMK and LKB1 as a dominant-negative peptide, which abrogates this interaction, attenuated metformin's ability to activate AMPK. Our data demonstrate that IPMK plays an important role in LKB1/AMPK signaling and may be targeted for treatment of metabolic diseases.

Indexed as

Aminoimidazole CarboxamideAMP-Activated Protein KinasesAnimalsCell Line, TumorDiabetes Mellitus, Type 2Energy MetabolismFatty AcidsGene Knockout TechniquesGluconeogenesisGlucoseHEK293 CellsHeLa CellsHumansHypoglycemic AgentsLipid MetabolismLiverAICA ribonucleotideAminoimidazole CarboxamideAMP-Activated Protein KinasesFatty AcidsGlucoseHypoglycemic Agentsinositol polyphosphate multikinaseMetforminPhosphotransferases (Alcohol Group Acceptor)Protein Serine-Threonine KinasesRibonucleotidesStk11 protein, mouse

Identifiers

PMID24877601
PMCPMC4075158

What OpenQuestion holds

Texttitle and abstract
Read underepoch 390

Registered trials

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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.