Evidence map›Paper›PMID 27834734›Full record

ArticleMolecular & cellular proteomics : MCP2017

Nano-liquid Chromatography-orbitrap MS-based Quantitative Proteomics Reveals Differences Between the Mechanisms of Action of Carnosic Acid and Carnosol in Colon Cancer Cells.

Alberto Valdés, Virginia García-Cañas, Konstantin A Artemenko, Carolina Simó, Jonas Bergquist, Alejandro Cifuentes

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2017. 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
2.3field-weighted citation impact, top 12% 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, 37 citations in OpenAlex.

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  9. Anticancer Activity ofNutrients · 2020
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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

6 authors at 3 institutions in 2 countries.

Alberto ValdésFrom the ‡Laboratory of Foodomics, Institute of Food Science Research (CIAL, CSIC), Calle Nicolás Cabrera 9, 28049 Madrid, Spain.
Virginia García-CañasFrom the ‡Laboratory of Foodomics, Institute of Food Science Research (CIAL, CSIC), Calle Nicolás Cabrera 9, 28049 Madrid, Spain; virginia.garcia@csic.es.ORCID 0000-0001-6728-4325
Konstantin A Artemenko§Analytical Chemistry, Department of Chemistry-BMC and SciLifeLab, Uppsala University, Husargatan 3, 75124 Uppsala, Sweden.
Carolina SimóFrom the ‡Laboratory of Foodomics, Institute of Food Science Research (CIAL, CSIC), Calle Nicolás Cabrera 9, 28049 Madrid, Spain.
Jonas Bergquist§Analytical Chemistry, Department of Chemistry-BMC and SciLifeLab, Uppsala University, Husargatan 3, 75124 Uppsala, Sweden.
Alejandro CifuentesFrom the ‡Laboratory of Foodomics, Institute of Food Science Research (CIAL, CSIC), Calle Nicolás Cabrera 9, 28049 Madrid, Spain.
Instituto de Investigación en Ciencias de la Alimentación · ESScience for Life Laboratory · SEUppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carnosic acid (CA) and carnosol (CS) are two structurally related diterpenes present in rosemary herb (Rosmarinus officinalis). Although several studies have demonstrated that both diterpenes can scavenge free radicals and interfere in cellular processes such as cell proliferation, they may not necessarily exert the same effects at the molecular level. In this work, a shotgun proteomics study based on stable isotope dimethyl labeling (DML) and nano-liquid chromatography-tandem mass spectrometry (nano-LC-MS/MS) has been performed to identify the relative changes in proteins and to gain some light on the specific molecular targets and mechanisms of action of CA and CS in HT-29 colon cancer cells. Protein profiles revealed that CA and CS induce different Nrf2-mediated response. Furthermore, examination of our data revealed that each diterpene affects protein homeostasis by different mechanisms. CA treatment induces the expression of proteins involved in the unfolded protein response in a concentration dependent manner reflecting ER stress, whereas CS directly inhibits chymotrypsin-like activity of the 20S proteasome. In conclusion, the unbiased proteomics-wide method applied in the present study has demonstrated to be a powerful tool to reveal differences on the mechanisms of action of two related bioactive compounds in the same biological model.

Indexed as

AbietanesChromatography, LiquidColonic NeoplasmsEndoplasmic Reticulum StressGene Expression Regulation, NeoplasticHomeostasisHT29 CellsHumansIsotope LabelingProteasome Endopeptidase ComplexProteomicsSignal TransductionTandem Mass SpectrometryUnfolded Protein ResponseAbietanescarnosolProteasome Endopeptidase Complexsalvin

Identifiers

PMID27834734
PMCPMC5217784
OpenAlexW2550555570

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.