Evidence map›Paper›PMID 27351226›Full record

ArticleOncotarget2016

Cell surface protease activation during RAS transformation: Critical role of the plasminogen receptor, S100A10.

Patricia A Madureira, Alamelu G Bharadwaj, Moamen Bydoun, Katy Garant, Paul O'Connell, Patrick Lee, David M Waisman

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

18 citing papers in PubMed, 24 citations in OpenAlex.

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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

7 authors at 2 institutions in 2 countries.

Patricia A MadureiraCentre for Biomedical Research (CBMR), University of Algarve, Campus of Gambelas, Faro, Portugal.
Alamelu G BharadwajDepartment of Biochemistry and Molecular Biology, Dalhousie University, Halifax, Nova Scotia, Canada.
Moamen BydounDepartment of Pathology, Dalhousie University, Halifax, Nova Scotia, Canada.
Katy GarantDepartment of Pathology, Dalhousie University, Halifax, Nova Scotia, Canada.
Paul O'ConnellDepartment of Biochemistry and Molecular Biology, Dalhousie University, Halifax, Nova Scotia, Canada.
Patrick LeeDepartment of Pathology, Dalhousie University, Halifax, Nova Scotia, Canada.
David M WaismanDepartment of Biochemistry and Molecular Biology, Dalhousie University, Halifax, Nova Scotia, Canada.
Dalhousie University · CAUniversity of Algarve · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The link between oncogenic RAS expression and the acquisition of the invasive phenotype has been attributed to alterations in cellular activities that control degradation of the extracellular matrix. Oncogenic RAS-mediated upregulation of matrix metalloproteinase 2 (MMP-2), MMP-9 and urokinase-type plasminogen activator (uPA) is critical for invasion through the basement membrane and extracellular matrix. The uPA converts cell surface-bound plasminogen to plasmin, a process that is regulated by the binding of plasminogen to specific receptors on the cell surface, however, the identity of the plasminogen receptors that function in this capacity is unclear. We have observed that transformation of cancer cells with oncogenic forms of RAS increases plasmin proteolytic activity by 2- to 4-fold concomitant with a 3-fold increase in cell invasion. Plasminogen receptor profiling revealed RAS-dependent increases in both S100A10 and cytokeratin 8. Oncogenic RAS expression increased S100A10 gene expression which resulted in an increase in S100A10 protein levels. Analysis with the RAS effector-loop mutants that interact specifically with Raf, Ral GDS pathways highlighted the importance of the RalGDS pathways in the regulation of S100A10 gene expression. Depletion of S100A10 from RAS-transformed cells resulted in a loss of both cellular plasmin generation and invasiveness. These results strongly suggest that increases in cell surface levels of S100A10, by oncogenic RAS, plays a critical role in RAS-stimulated plasmin generation, and subsequently, in the invasiveness of oncogenic RAS expressing cancer cells.

Indexed as

A549 CellsAnimalsAnnexin A2Cell Line, TumorCell Transformation, NeoplasticEnzyme ActivationFibrinolysinGenes, rasHCT116 CellsHEK293 CellsHumansMCF-7 CellsMiceNIH 3T3 CellsPeptide Hydrolasesras ProteinsAnnexin A2FibrinolysinPeptide Hydrolasesras ProteinsS100 Calcium Binding Protein A10S100 Proteinsannexin A2plasminplasminogenRASS100A10

Identifiers

PMID27351226
PMCPMC5216974
OpenAlexW2467988000

What OpenQuestion holds

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LicenceCC BY
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.