Evidence map›Paper›PMID 20035555›Full record

ArticleJournal of proteome research2010

Inhibition of protein phosphorylation in MIA pancreatic cancer cells: confluence of metabolic and signaling pathways.

Hengwei Zhang, Rui Cao, Wai-Nang Paul Lee, Caishu Deng, Yingchun Zhao, Joan Lappe, Robert Recker, Yun Yen, Qi Wang, Ming-Ying Tsai and 2 more

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  3. Article
  4. Review
  5. The Warburg effect: a balance of flux analysis.Metabolomics : Official journal of the Metabolomic Society · 2015
    Article
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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

12 authors at 1 institution in 2 countries.

Hengwei ZhangGenomics and Functional Proteomics Laboratories, Osteoporosis Research Center and Department of Pathology, Creighton University Medical Center, 601 North 30th Street, Suite 6730, Omaha, Nebraska 68131, USA.
Rui Cao
Wai-Nang Paul Lee
Caishu Deng
Yingchun Zhao
Joan Lappe
Robert Recker
Yun Yen
Qi Wang
Ming-Ying Tsai
Vay Liang Go
Gary Guishan Xiao
Dalian Medical University · CN

Funding

ZONA-FREE HAMSTER OVA ASSAY AS AN INDICATOR OF MALE FERTILITYM01RR000425 · NCRR · LUNDQUIST INSTITUTE FOR BIOMEDICAL INNOVATION AT HARBOR-UCLA MEDICAL CENTER · PI ANDERSON, GAIL V · 1985 to 2011
$74.2M
UCLA Center for Excellence in Pancreatic DiseasesP01AT003960 · NCCIH · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI GO, VAY LIANG W · 2007 to 2011
$5.6M
NCCIH NIH HHS P01 AT003960NCCIH NIH HHS P01 AT003960-01NCRR NIH HHS M01 RR000425NCRR NIH HHS M01 RR00425
6 · The paper itself

Abstract

Oxythiamine (OT), a transketolase inhibitor, is known to inhibit pancreatic cancer cell proliferation. In this study, we investigated the effect of inhibition of the transketolase pathway on signaling pathways in MIA PaCa cancer cells using in-house proteomic techniques. We hypothesized that OT alter protein phosphorylation thus affecting cell cycle arrest and cell proliferation. MIA PaCa-2 cells were cultured in media containing an algal (15)N amino acid mixture at 50% enrichment, with and without OT, to determine protein expression and synthesis. Analysis of cell lysates using two-dimensional gel electrophoresis matrix assisted laser desorption and ionization time-of-flight and time-of-flight mass spectrometry (2-DE-MALDI-TOF/TOF MS) identified 12 phosphor proteins that were significantly suppressed by OT treatment. Many of these proteins are involved in regulation of cycle activities and apoptosis. Among the proteins identified, expression of the phosphor heat shock protein 27 (Hsp27) was dramatically inhibited by OT treatment while the level of its total protein remained unchanged. Hsp27 expression and phosphorylation is known to be associated with drug resistance and cancer cell survival. The changes in phosphorylation of key proteins of cancer proliferation and survival suggest that protein phosphorylation is the confluence of the effects of OT on metabolic and signaling pathways.

Indexed as

Signal TransductionBlotting, WesternCell CycleCell Line, TumorElectrophoresis, Gel, Two-DimensionalHSP27 Heat-Shock ProteinsHumansImmunohistochemistryMAP Kinase Signaling SystemOxythiaminePancreatic NeoplasmsPhosphorylationProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationHSP27 Heat-Shock ProteinsOxythiamineProteins

Identifiers

PMID20035555
PMCPMC2836017
OpenAlexW1987785670

What OpenQuestion holds

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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.