Evidence map›Paper›PMID 32040844›Full record

ArticlePharmacological reports : PR2020

The synthetic oleanane triterpenoid CDDO-Me binds and inhibits pyruvate kinase M2.

Iaci N Soares, Raiane Viana, Charles B Trelford, Eddie Chan, Boun Thai, Elio A Cino, Gianni M Di Guglielmo

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Article in Pharmacological reports : PR, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.9field-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

6 citing papers in PubMed, 14 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.

Iaci N SoaresDepartment of Physiology and Pharmacology, University of Western Ontario, London, ON, N6A 5C1, Canada.
Raiane VianaDepartment of Biochemistry and Immunology, Federal University of Minas Gerais, Belo Horizonte, Minas Gerais, 31270-901, Brazil.
Charles B TrelfordDepartment of Physiology and Pharmacology, University of Western Ontario, London, ON, N6A 5C1, Canada.
Eddie ChanDepartment of Physiology and Pharmacology, University of Western Ontario, London, ON, N6A 5C1, Canada.
Boun ThaiDepartment of Physiology and Pharmacology, University of Western Ontario, London, ON, N6A 5C1, Canada.
Elio A CinoDepartment of Biochemistry and Immunology, Federal University of Minas Gerais, Belo Horizonte, Minas Gerais, 31270-901, Brazil. eliocino@ufmg.br.
Gianni M Di GuglielmoDepartment of Physiology and Pharmacology, University of Western Ontario, London, ON, N6A 5C1, Canada. john.diguglielmo@schulich.uwo.ca.
Western University · CAUniversidade Federal de Minas Gerais · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe M2 isoform of the glycolytic enzyme pyruvate kinase (PKM2) is one of the key components in the Warburg effect, and an important regulator of cancer cell metabolism. Elevated PKM2 expression is a hallmark of numerous tumor types, making it a promising target for cancer therapy.

methodsMigration of H1299 lung tumor cells treated with synthetic oleanane triterpenoid derivatives CDDO-Me and CDDO-Im was monitored using scratch and transwell assays. Direct binding and inhibition of PKM2 activity by CDDO-Me was demonstrated by pull-down and activity assays. PKM2 localization in the absence and presence of CDDO-Me or CDDO-Im was determined by subcellular fractionation and immunofluorescence microscopy. Involvement of PKM2 in tumor cell migration was assessed using a stable PKM2 knockdown cell line.

resultsWe demonstrate that migration of H1299 lung tumor cells is inhibited by CDDO-Me and CDDO-Im in scratch and transwell assays. CDDO-Me binds directly and specifically to recombinant PKM2, leading to a reduction of its catalytic activity. PKM2 knockdown cells exhibit significantly lower migration compared to control cells when subjected to glucose and oxygen deprivation, but not under regular conditions.

conclusionsThe results suggest that PKM2 expression in a tumor-like environment contributes to cell migration, and that PKM2 activity can be down regulated by synthetic triterpenoid derivatives.

Indexed as

Carcinoma, Non-Small-Cell LungCell Line, TumorCell MovementGlucoseHumansHypoxiaOleanolic AcidPyruvate Kinasebardoxolone methylGlucoseOleanolic AcidPyruvate KinaseCancerCDDO-MeCell migrationPKM2TriterpenoidWarburg effect

Identifiers

PMID32040844
OpenAlexW3005943381

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Registered trials

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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.