Evidence map›Paper›PMID 14519103›Full record

ArticleThe Biochemical journal2004

Transcriptional and translational control of ornithine decarboxylase during Ras transformation.

Lisa M Shantz

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

26 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Elucidating the Role ofMedical sciences (Basel, Switzerland) · 2022
    Article
  5. Article
  6. The Emerging Clinical Role of Spermine in Prostate Cancer.International journal of molecular sciences · 2021
    Review
  7. Review
  8. Article
  9. Review
  10. Myc, Oncogenic Protein Translation, and the Role of Polyamines.Medical sciences (Basel, Switzerland) · 2018
    Review
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Pathophysiology of the diabetic kidney.Comprehensive Physiology · 2011
    Review
  19. The proximal tubule in the pathophysiology of the diabetic kidney.American journal of physiology. Regulatory, integrative and comparative physiology · 2011
    Review
  20. Posttranscriptional regulation of ornithine decarboxylase.Methods in molecular biology (Clifton, N.J.) · 2011
    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

1 author at 1 institution in 1 country.

Lisa M ShantzDepartment of Cellular and Molecular Physiology, The Milton S. Hershey Medical Center, The Pennsylvania State University College of Medicine, 500 University Drive, Hershey, PA 17033, USA. lms17@psu.edu
Penn State Milton S. Hershey Medical Center · US

Funding

Role of ornithine decarboxylase in Ras transformationR01CA082768 · NCI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI SHANTZ, LISA M · 1999 to 2006
$1.4M
NCI NIH HHS CA82768NCI NIH HHS R01 CA082768
6 · The paper itself

Abstract

ODC (ornithine decarboxylase) activity is induced following ras activation. However, the Ras effector pathways responsible are unknown. These experiments used NIH-3T3 cells expressing partial-loss-of-function Ras mutants to activate selectively pathways downstream of Ras and examined the contribution of each pathway to ODC induction. Overexpression of Ras12V, a constitutively active mutant, resulted in ODC activities up to 20-fold higher than controls. Stable transfections of Ras partial-loss-of-function mutants and constitutively active forms of MEK (MAPK kinase) and Akt indicated that activation of more than one Ras effector pathway is necessary for the complete induction of ODC activity. The increase in ODC activity in Ras12V-transformed cells is not owing to a substantial change in ODC protein half-life, which increased by <2-fold. Northern-blot analysis and reporter assays suggested that the mechanism of ODC induction involves both a modest increase in the transcription of ODC mRNA and a much more considerable increase in the translation of mRNA into protein. ODC transcription was controlled through a pathway dependent on Raf/MEK/ERK (where ERK stands for extracellular-signal-regulated kinase) activation, whereas activation of the phosphoinositide 3-kinase and the Raf/MEK/ERK pathways were necessary for translational regulation of ODC. The increase in ODC synthesis was accompanied by changes in phosphorylation of eukaryotic initiation factor 4E and its binding protein 4E-BP1. Results show that the phosphoinositide 3-kinase pathway regulates phosphorylation of both proteins, whereas the Raf/MEK/ERK pathway affects only the eukaryotic initiation factor 4E phosphorylation.

Indexed as

Protein BiosynthesisTranscription, GeneticAnimalsCell Line, TransformedEnzyme InhibitorsGene Expression RegulationMiceMutationNIH 3T3 CellsOrnithine DecarboxylaseProtein Kinase InhibitorsProto-Oncogene Proteins p21(ras)Signal TransductionEnzyme InhibitorsOrnithine DecarboxylaseProtein Kinase InhibitorsProto-Oncogene Proteins p21(ras)

Identifiers

PMID14519103
PMCPMC1223852
OpenAlexW2031434842

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.