Evidence map›Paper›PMID 34324551›Full record

ArticlePloS one2021

A phenolic-rich extract from Ugni molinae berries reduces abnormal protein aggregation in a cellular model of Huntington's disease.

Rodrigo Pérez-Arancibia, Jose Luis Ordoñez, Alexis Rivas, Philippe Pihán, Alfredo Sagredo, Ulises Ahumada, Andrés Barriga, Ivette Seguel, César Cárdenas, Rene L Vidal and 2 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

10 citing papers in PubMed, 14 citations in OpenAlex.

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  4. Long noncoding RNAs in ubiquitination, protein degradation, and human diseases.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review
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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 4 institutions in 2 countries.

Rodrigo Pérez-ArancibiaLaboratorio de Productos Naturales, Departamento de Química Farmacológica y Toxicológica, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago, Chile.ORCID 0000-0002-7180-8547
Jose Luis OrdoñezLaboratorio de Productos Naturales, Departamento de Química Farmacológica y Toxicológica, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago, Chile.
Alexis RivasInstituto de Neurociencia Biomédica (BNI), Facultad de Medicina, Universidad de Chile, Santiago, Chile.
Philippe PihánInstituto de Neurociencia Biomédica (BNI), Facultad de Medicina, Universidad de Chile, Santiago, Chile.
Alfredo SagredoInstituto de Neurociencia Biomédica (BNI), Facultad de Medicina, Universidad de Chile, Santiago, Chile.
Ulises AhumadaCentro FONDAP de Gerociencia, Salud Mental y Metabolismo (GERO), Santiago, Chile.
Andrés BarrigaUnidad de Espectrometría de Masas, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago, Chile.
Ivette SeguelLaboratorio de Productos Naturales, Departamento de Química Farmacológica y Toxicológica, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago, Chile.
César CárdenasCentro FONDAP de Gerociencia, Salud Mental y Metabolismo (GERO), Santiago, Chile.
Rene L VidalInstituto de Neurociencia Biomédica (BNI), Facultad de Medicina, Universidad de Chile, Santiago, Chile.
Claudio HetzInstituto de Neurociencia Biomédica (BNI), Facultad de Medicina, Universidad de Chile, Santiago, Chile.
Carla DelporteLaboratorio de Productos Naturales, Departamento de Química Farmacológica y Toxicológica, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago, Chile.
Universidad Mayor · CLUniversity of Chile · CLInstituto de Neurociencia Biomédica · CLBuck Institute for Research on Aging · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Accumulation of misfolded proteins in the brain is a common hallmark of most age-related neurodegenerative diseases. Previous studies from our group identified the presence of anti-inflammatory and antioxidant compounds in leaves derived from the Chilean berry Ugni molinae (murtilla), in addition to show a potent anti-aggregation activity in models of Alzheimer´s disease. However, possible beneficial effects of berry extracts of murtilla was not investigated. Here we evaluated the efficacy of fruit extracts from different genotypes of Chilean-native U. molinae on reducing protein aggregation using cellular models of Huntington´s disease and assess the correlation with their chemical composition. Berry extraction was performed by exhaustive maceration with increasing-polarity solvents. An unbiased automatic microscopy platform was used for cytotoxicity and protein aggregation studies in HEK293 cells using polyglutamine-EGFP fusion proteins, followed by secondary validation using biochemical assays. Phenolic-rich extracts from murtilla berries of the 19-1 genotype (ETE 19-1) significantly reduced polyglutamine peptide aggregation levels, correlating with the modulation in the expression levels of autophagy-related proteins. Using LC-MS and molecular network analysis we correlated the presence of flavonoids, phenolic acids, and ellagitannins with the protective effects of ETE 19-1 effects on protein aggregation. Overall, our results indicate the presence of bioactive components in ethanolic extracts from U. molinae berries that reduce the load of protein aggregates in living cells.

Indexed as

FruitHuntington DiseasePlant ExtractsHEK293 CellsHumansMyrtaceaePeptidesPhenolsProtein AggregatesProtein Aggregation, PathologicalPeptidesPhenolsPlant ExtractspolyglutamineProtein Aggregates

Identifiers

PMID34324551
PMCPMC8320977
OpenAlexW3185819553

What OpenQuestion holds

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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.