Evidence map›Paper›PMID 7688751›Full record

ArticleThe Journal of cell biology1993

Polyamines are essential for cell transformation by pp60v-src: delineation of molecular events relevant for the transformed phenotype.

E Hölttä, M Auvinen, L C Andersson

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1993. 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
1.8field-weighted citation impact, top 14% 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, 73 citations in OpenAlex.

  1. Article
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  8. Antizyme and antizyme inhibitor, a regulatory tango.Cellular and molecular life sciences : CMLS · 2009
    Review
  9. Article
  10. Polyamines and nonmelanoma skin cancer.Toxicology and applied pharmacology · 2007
    Review
  11. Article
  12. Article
  13. Article
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  19. Review
  20. Specific requirement of putrescine for the mitogenic action of juvenile hormone on adult insect neuroblasts.Proceedings of the National Academy of Sciences of the United States of America · 1997
    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

3 authors at 1 institution in 1 country.

E HölttäDepartment of Pathology, University of Helsinki, Finland.
M Auvinen
L C Andersson
University of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ornithine decarboxylase (ODC), the key enzyme of polyamine biosynthesis, becomes upregulated during cell proliferation and transformation. Here we show that intact ODC activity is needed for the acquisition of a transformed phenotype in rat 2R cells infected with a temperature-sensitive mutant of Rous sarcoma virus. Addition of the ODC inhibitor alpha-difluoromethyl ornithine (DFMO) to the cells (in polyamine-free medium) before shift to permissive temperature prevented the depolymerization of filamentous actin and morphological transformation. Polyamine supplementation restored the transforming potential of pp60v-src. DFMO did not interfere with the expression of pp60v-src or its in vitro tyrosine kinase activity. The tyrosine phosphorylation of most cellular proteins, including ras GAP, did not either display clear temperature- or DFMO-sensitive changes. A marked increase was, however, observed in the tyrosine phosphorylation of phosphatidylinositol 3-kinase and proteins of 33 and 36 kD upon the temperature shift, and these hyperphosphorylations were partially inhibited by DFMO. A DFMO-sensitive increase was also found in the total phosphorylation of calpactins I and II. The well-documented association of GAP with the phosphotyrosine-containing proteins p190 and p62 did not correlate with transformation, but a novel 42-kD tyrosine phosphorylated protein was complexed with GAP in a polyamine- and transformation-dependent manner. Further, tyrosine phosphorylated proteins of 130, 80/85, and 36 kD were found to coimmunoprecipitate with pp60v-src in a transformation-related manner. Altogether, this model offers a tool for sorting out the protein phosphorylations and associations critical for the transformed phenotype triggered by pp60v-src, and implicates a pivotal role for polyamines in cell transformation.

Indexed as

Cell Transformation, ViralActin CytoskeletonActinsAnimalsCell LineEflornithineGTPase-Activating ProteinsOncogene Protein pp60(v-src)Ornithine DecarboxylasePhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationPhosphotransferasesPhosphotyrosinePolyaminesProteinsActinsEflornithineGTPase-Activating ProteinsOncogene Protein pp60(v-src)Ornithine DecarboxylasePhosphatidylinositol 3-KinasesPhosphoproteinsPhosphotransferasesPhosphotyrosinePolyaminesProteinsras GTPase-Activating ProteinsTyrosine

Identifiers

PMID7688751
PMCPMC2119593
OpenAlexW2053504500

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.