Evidence map›Paper›PMID 25114970›Full record

ArticleTheScientificWorldJournal2014

The p85 regulatory subunit of PI3K mediates cAMP-PKA and insulin biological effects on MCF-7 cell growth and motility.

E Di Zazzo, A Feola, C Zuchegna, A Romano, C F Donini, S Bartollino, C Costagliola, R Frunzio, P Laccetti, M Di Domenico and 1 more

Open access · goldAbstract read
In one paragraph

Article in TheScientificWorldJournal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

28 citing papers in PubMed, 42 citations in OpenAlex.

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  16. Adiponectin as Link Factor between Adipose Tissue and Cancer.International journal of molecular sciences · 2019
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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

11 authors at 4 institutions in 2 countries.

E Di ZazzoDepartment of Medicine and Health Sciences, University of Molise, Campobasso, Italy.
A FeolaDepartment of Biology, University Federico II of Naples, Naples, Italy ; Department of Biochemistry, Biophysics and General Pathology, Second University of Naples, Italy.
C ZuchegnaDepartment of Biology, University Federico II of Naples, Naples, Italy.
A RomanoDepartment of Biology, University Federico II of Naples, Naples, Italy.
C F DoniniDepartment of Experimental Medicine, Sapienza University of Rome, Rome, Italy.
S BartollinoDepartment of Medicine and Health Sciences, University of Molise, Campobasso, Italy.
C CostagliolaDepartment of Medicine and Health Sciences, University of Molise, Campobasso, Italy.
R FrunzioDepartment of Biology, University Federico II of Naples, Naples, Italy.
P LaccettiDepartment of Biology, University Federico II of Naples, Naples, Italy.
M Di DomenicoDepartment of Biochemistry, Biophysics and General Pathology, Second University of Naples, Italy ; Sbarro Institute for Cancer Research and Molecular Medicine, Center for Biotechnology, Temple University, Philadelphia, PA, USA.
A PorcelliniDepartment of Biology, University Federico II of Naples, Naples, Italy.
University of Naples Federico II · ITUniversity of Molise · ITSapienza University of Rome · ITTemple University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recent studies have shown that hyperinsulinemia may increase the cancer risk. Moreover, many tumors demonstrate an increased activation of IR signaling pathways. Phosphatidylinositol 3-kinase (PI3K) is necessary for insulin action. In epithelial cells, which do not express GLUT4 and gluconeogenic enzymes, insulin-mediated PI3K activation regulates cell survival, growth, and motility. Although the involvement of the regulatory subunit of PI3K (p85α (PI3K)) in insulin signal transduction has been extensively studied, the function of its N-terminus remains elusive. It has been identified as a serine (S83) in the p85α (PI3K) that is phosphorylated by protein kinase A (PKA). To determine the molecular mechanism linking PKA to insulin-mediated PI3K activation, we used p85α (PI3K) mutated forms to prevent phosphorylation (p85A) or to mimic the phosphorylated residue (p85D). We demonstrated that phosphorylation of p85α (PI3K)S83 modulates the formation of the p85α (PI3K)/IRS-1 complex and its subcellular localization influencing the kinetics of the insulin signaling both on MAPK-ERK and AKT pathways. Furthermore, the p85α (PI3K)S83 phosphorylation plays a central role in the control of insulin-mediated cell proliferation, cell migration, and adhesion. This study highlights the p85α (PI3K)S83 role as a key regulator of cell proliferation and motility induced by insulin in MCF-7 cells breast cancer model.

Indexed as

Cell MovementCell ProliferationCell SurvivalClass Ia Phosphatidylinositol 3-KinaseCyclic AMP-Dependent Protein KinasesHumansInsulinInsulin Receptor Substrate ProteinsIntracellular SpaceMCF-7 CellsPhosphorylationProtein BindingProtein TransportSignal TransductionClass Ia Phosphatidylinositol 3-KinaseCyclic AMP-Dependent Protein KinasesInsulinInsulin Receptor Substrate ProteinsIRS1 protein, human

Identifiers

PMID25114970
PMCPMC4119716
OpenAlexW2093089132

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.