Evidence map›Paper›PMID 9794792›Full record

ArticleThe Biochemical journal1998

AMP-activated protein kinase is activated by low glucose in cell lines derived from pancreatic beta cells, and may regulate insulin release.

I P Salt, G Johnson, S J Ashcroft, D G Hardie

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 155 papers.

0numbers the graph read from it
0cells of the map it votes in
155citing papers in PubMed
10.2field-weighted citation impact, top 2% 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

155 citing papers in PubMed, 411 citations in OpenAlex.

  1. Trial
  2. Insulin resistance with aging: effects of diet and exercise.Sports medicine (Auckland, N.Z.) · 2000
    Trial
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Cells · 2024
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. New insights into activation and function of the AMPK.Nature reviews. Molecular cell biology · 2023
    Review
  18. Article
  19. A Review ofMolecules (Basel, Switzerland) · 2023
    Review
  20. Article

95 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 2 institutions in 1 country.

I P SaltBiochemistry Department, MSI/WTB Complex, Dow Street, University of Dundee, Dundee DD1 5EH, Scotland, UK.
G Johnson
S J Ashcroft
D G Hardie
John Radcliffe Hospital · GBUniversity of Dundee · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

The role of the AMP-activated protein kinase (AMPK) cascade in the glucose-sensitive pancreatic beta cell lines HIT-T15 and INS-1 was addressed. In both cell types, removal of glucose leads to a >5-fold activation of AMPK activity. Activation of AMPK was due to phosphorylation, since the effect was reversed by protein phosphatase treatment of the extracts, and was restored by re-addition of MgATP and the purified upstream kinase. When the effects of different concentrations of medium glucose were examined, insulin secretion and AMPK activity were inversely related, and varied over the same concentration range. The activation in response to glucose removal appeared to be due to changes in the concentration of the known regulators of the cascade, i.e. AMP and ATP, since AMPK activation was associated with a large increase in the cellular AMP/ATP ratio, and the two parameters varied over the same range of glucose concentrations. In late-passage HIT-T15 cells that had lost the glucose-dependent insulin secretion response, both AMPK activity and the AMP/ATP ratio also became insensitive to the extracellular glucose concentration. Treatment of INS-1 cells, but not HIT-T15 cells, with AICA riboside (5-aminoimidazole-4-carboxamide riboside) results in accumulation of the ribotide, ZMP (AICA riboside monophosphate), and activation of AMPK. AICA riboside treatment of INS-1 cells, and of isolated rat islets, had both inhibitory and stimulatory effects on insulin secretion. These results show that in beta cell lines the AMP-activated protein kinase, like its yeast homologue the SNF1 complex, can respond to the level of glucose in the medium, and may be involved in regulating insulin release.

Indexed as

Protein Serine-Threonine KinasesAdenosine DiphosphateAdenosine MonophosphateAdenosine TriphosphateAmino Acid SequenceAminoimidazole CarboxamideAMP-Activated Protein KinasesAnimalsCatalytic DomainCell LineEnzyme ActivationGlucoseInsulinInsulin SecretionIn Vitro TechniquesIslets of LangerhansAdenosine DiphosphateAdenosine MonophosphateAdenosine TriphosphateAICA ribonucleotideAminoimidazole CarboxamideAMP-Activated Protein KinasesGlucoseInsulinMultienzyme ComplexesPeptide FragmentsProtein KinasesProtein Serine-Threonine KinasesProtein Tyrosine PhosphatasesRibonucleotides

Identifiers

PMID9794792
PMCPMC1219813
OpenAlexW1913661755

What Socratic 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 Socratic graph.