Evidence map›Paper›PMID 31583572›Full record

ArticleMolecular biology reports2019

In vitro and in silico anticancer activity of amygdalin on the SK-BR-3 human breast cancer cell line.

Bahman Moradipoodeh, Mostafa Jamalan, Majid Zeinali, Masood Fereidoonnezhad, Ghorban Mohammadzadeh

Abstract read
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In one paragraph

Article in Molecular biology reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

15 citing papers in PubMed, 38 citations in OpenAlex.

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  8. Frontiers in pharmacology · 2024
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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

5 authors at 2 institutions in 1 country.

Bahman MoradipoodehDepartment of Clinical Biochemistry, Faculty of Medicine, Ahvaz Jundishapur University of Medical Science, Ahvaz, Iran.
Mostafa JamalanAbadan School of Medical Sciences, Abadan, Iran.
Majid ZeinaliBiotechnology Research Center, Research Institute of Petroleum Industry (RIPI), Tehran, Iran.
Masood FereidoonnezhadDepartment of Medicinal Chemistry, School of Pharmacy, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran.
Ghorban MohammadzadehHyperlipidemia Research Center, Department of Clinical Biochemistry, Faculty of Medicine, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran. mohammadzadeh@ajums.ac.ir.ORCID http://orcid.org/0000-0001-7921-4770
Ahvaz Jundishapur University of Medical Sciences · IRBiotechnology Research Center · IR

Funding

Hyperlipidemia Research Center, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran HLRC-9506
6 · The paper itself

Abstract

In spite of several studies that have shown the cytotoxic effects of amygdalin on the different cancer cell lines, however, the chemopreventive potential of amygdalin on the breast cancer cell line is not completely understood. We investigated the effect of amygdalin on the cell death and the level of pro-apoptotic Bax protein and anti-apoptotic Bcl-2 protein in SK-BR-3 human breast cancer cell line. The cell viability of SK-BR-3 cells was evaluated by MTT assay in different concentration of amygdalin. The level of Bax and Bcl-2 in SK-BR-3 cells were measured by western blot analysis. For statistical analysis, One-way ANOVA was used for the comparison of Bax and Bcl-2 protein level and percent of cell viability between groups. The molecular docking studies of amygdalin within the Bcl-2 (PDB ID: 4LVT) and HER2 (PDB ID: 3RCD) active site, were performed using AutoDock 4.2.5. Amygdalin induced a significant reduction of cell viability in SK-BR-3 after 24-h treatment in a dose-dependent manner. Also, amygdalin causes an increase in pro-apoptotic Bax protein and a decrease in anti-apoptotic Bcl-2 protein expression in the SK-BR-3 cells. Molecular docking studies showed that amygdalin interacts with the active site amino acids of Bcl-2 and HER2 through hydrogen bonding and some hydrophobic interactions. Amygdalin can induce apoptotic death in SK-BR-3 cells by increasing pro-apoptotic Bax protein and decreasing anti-apoptotic Bcl-2 protein expression. The results suggest that amygdalin may be a valuable candidate for the treatment of breast cancer, especially in HER2 positive cells.

Indexed as

Amygdalinbcl-2-Associated X ProteinBreast NeoplasmsCatalytic DomainCell Line, TumorCell ProliferationCell SurvivalErb-b2 Receptor Tyrosine KinasesFemaleGene Expression Regulation, NeoplasticHumansHydrogen BondingModels, MolecularMolecular Docking SimulationProto-Oncogene Proteins c-bcl-2Signal TransductionAmygdalinBAX protein, humanbcl-2-Associated X ProteinBCL2 protein, humanERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesProto-Oncogene Proteins c-bcl-2AmygdalinApoptosisBAXBcl-2Molecular dockingSK-BR-3 cells

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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.