Evidence map›Paper›PMID 8389451›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1993

The ras signaling pathway mimics insulin action on glucose transporter translocation.

L Kozma, K Baltensperger, J Klarlund, A Porras, E Santos, M P Czech

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. 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. Article
  3. Article
  4. Article
  5. Article
  6. Profibrotic up-regulation of glucose transporter 1 by TGF-β involves activation of MEK and mammalian target of rapamycin complex 2 pathways.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016
    Article
  7. Article
  8. Article
  9. Article
  10. Insulin receptor-independent upregulation of cellular glucose uptake.International journal of obesity (2005) · 2013
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Insulin regulation of the Ras activation/inactivation cycle.Molecular and cellular biochemistry · 1998
    Review
  18. Article
  19. Article
  20. 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.

L KozmaProgram in Molecular Medicine, University of Massachusetts Medical Center, Worcester 01605.
K Baltensperger
J Klarlund
A Porras
E Santos
M P Czech

Funding

PROPERTIES OF THE HIGH-AFFINITY INSULIN RECEPTORR01DK030648 · NIDDK · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CZECH, MICHAEL P · 1986 to 2008
$3.6M
NIDDK NIH HHS DK30648
6 · The paper itself

Abstract

Recent observations suggest that insulin increases cellular levels of activated, GTP-bound Ras protein. We tested whether the acute actions of insulin on hexose uptake and glucose-transporter redistribution to the cell surface are mimicked by activated Ras. 3T3-L1 fibroblasts expressing an activated mutant (Lys-61) N-Ras protein exhibited a 3-fold increase in 2-deoxyglucose uptake rates compared with non-transfected cells. Insulin stimulated hexose uptake by approximately 2-fold in parental fibroblasts but did not stimulate hexose uptake in the N-Ras61K-expressing fibroblasts. Overexpression of N-Ras61K also mimicked the large effect of insulin on 2-deoxyglucose transport in 3T3-L1 adipocytes, and again the effects of the two agents were not additive. Total glucose transporter protein (GLUT) 1 was similar between parental and N-Ras61K-expressing 3T3-L1 fibroblasts or adipocytes, whereas total GLUT-4 protein was actually lower in the N-Ras61K-expressing compared with parental adipocytes. However, expression of N-Ras61K in 3T3-L1 adipocytes markedly elevated both GLUT-1 and GLUT-4 in plasma membranes relative to intracellular membranes, and insulin had no further effect. These modulations of glucose transporters by N-Ras61K expression are not due to upstream regulation of insulin receptors because receptor tyrosine phosphorylation and association of phosphatidylinositol 3-kinase with tyrosine-phosphorylated proteins were unaffected. These results show that activated Ras mimics the actions of insulin on membrane trafficking of glucose transporters, consistent with the concept that Ras proteins function as intermediates in this insulin signaling pathway.

Indexed as

3T3 CellsAnimalsBiological TransportCell MembraneDeoxyglucoseGlucoseInsulinIn Vitro TechniquesMiceMonosaccharide Transport ProteinsPhosphatidylinositol 3-KinasesPhosphotransferasesProto-Oncogene Proteins p21(ras)Receptor, InsulinSignal TransductionDeoxyglucoseGlucoseInsulinMonosaccharide Transport ProteinsPhosphatidylinositol 3-KinasesPhosphotransferasesProto-Oncogene Proteins p21(ras)Receptor, Insulin

Identifiers

PMID8389451
PMCPMC46531

What OpenQuestion holds

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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.