Evidence map›Paper›PMID 9182707›Full record

ArticleThe Biochemical journal1997

Sphingosine 1-phosphate stimulates rho-mediated tyrosine phosphorylation of focal adhesion kinase and paxillin in Swiss 3T3 fibroblasts.

F Wang, C D Nobes, A Hall, S Spiegel

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

23 citing papers in PubMed, 112 citations in OpenAlex.

  1. Targeting Sphingosine-1-Phosphate Signaling in Breast Cancer.International journal of molecular sciences · 2024
    Review
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  10. SHEP1 partners with CasL to promote marginal zone B-cell maturation.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  11. Article
  12. Review
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  16. Sphingosine 1-phosphate potentiates human lung fibroblast chemotaxis through the S1P2 receptor.American journal of respiratory cell and molecular biology · 2008
    Article
  17. Article
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  19. Review
  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

4 authors at 1 institution in 2 countries.

F WangDepartment of Biochemistry and Molecular Biology, Georgetown University Medical Center, Washington DC 20007, USA.
C D Nobes
A Hall
S Spiegel
Georgetown University · US

Funding

Sphingosine Kinases in Cancer Cell SignalingR01CA061774 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI SPIEGEL, SARAH · 1994 to 2015
$3.8M
NCI NIH HHS QR01 CA61774
6 · The paper itself

Abstract

Sphingosine 1-phosphate (SPP), a sphingolipid second messenger implicated in the mitogenic action of platelet-derived growth factor [Olivera, A. and Spiegel, S. (1993) Nature (London) 365, 557-560], induced rapid reorganization of the actin cytoskeleton resulting in stress-fibre formation. SPP also induced transient tyrosine phosphorylation of focal adhesion kinase (p125(FAK)), a cytosolic tyrosine kinase that localizes in focal adhesions, and of the cytoskeleton-associated protein paxillin. Exoenzyme C3 transferase, which ADP-ribosylates Rho (a Ras-related small GTP binding protein) on asparagine-41 and renders it biologically inactive, inhibited both stress-fibre formation and protein tyrosine phosphorylation induced by SPP. Thus Rho may be an upstream regulator of both stress-fibre formation and tyrosine phosphorylation of p125(FAK) and paxillin. Pretreatment with PMA, an activator of protein kinase C (PKC), inhibited the stimulation of stress-fibre formation induced by 1-oleoyl-lysophosphatidic acid (LPA) but not that by SPP. Similarly, PMA also decreased LPA-induced tyrosine phosphorylation of p125(FAK) and paxillin without abrogating the response to SPP. Thus PKC is involved in LPA- but not SPP-dependent signalling. The polyanionic drug suramin, a broad-specificity inhibitor of ligand-receptor interactions, did not inhibit either the mitogenic effect of SPP or its stimulation of tyrosine phosphorylation of p125(FAK). However, suramin markedly inhibited these responses induced by LPA. These results suggest that in contrast with LPA, SPP may be acting intracellularly in Swiss 3T3 fibroblasts to stimulate tyrosine phosphorylation of p125(FAK) and paxillin and cell growth.

Indexed as

Botulinum ToxinsSecond Messenger Systems3T3 CellsActin CytoskeletonActinsADP Ribose TransferasesAnimalsCell Adhesion MoleculesCell DivisionCytoskeletal ProteinsDNA ReplicationEnzyme ActivationFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGTP-Binding ProteinsLysophospholipidsActinsADP Ribose TransferasesBotulinum ToxinsCell Adhesion MoleculesCytoskeletal Proteinsexoenzyme C3, Clostridium botulinumFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGTP-Binding Proteinslysophosphatidic acidLysophospholipidsPaxillinPhosphoproteinsProtein Kinase CProtein-Tyrosine KinasesPtk2 protein, mousePxn protein, mouseRecombinant Proteinsrho GTP-Binding ProteinsSphingosinesphingosine 1-phosphateSuraminTetradecanoylphorbol Acetate

Identifiers

PMID9182707
PMCPMC1218455
OpenAlexW117297844

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.