Evidence map›Paper›PMID 32468000›Full record

ArticleMolecular medicine reports2020

Saikosaponin D inhibits autophagosome‑lysosome fusion and induces autophagy‑independent apoptosis in MDA‑MB‑231 breast cancer cells.

Ruoqiu Fu, Lin Zhang, Yuanyuan Li, Bin Li, Yue Ming, Zhiwei Li, Haiyan Xing, Jianhong Chen

Open access · hybridAbstract read
In one paragraph

Article in Molecular medicine reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed, 2 pooled it
2.9field-weighted citation impact, top 8% 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

26 citing papers in PubMed, 2 syntheses or guidelines pooled it, 39 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

8 authors at 2 institutions in 1 country.

Ruoqiu Fu *Department of Pharmacy, Daping Hospital, Army Medical University, Daping, Chongqing 400042, P.R. China.
Lin Zhang *Department of Pharmacy, Daping Hospital, Army Medical University, Daping, Chongqing 400042, P.R. China.
Yuanyuan LiDepartment of Pharmacy, Daping Hospital, Army Medical University, Daping, Chongqing 400042, P.R. China.
Bin LiDepartment of Pharmacy, Daping Hospital, Army Medical University, Daping, Chongqing 400042, P.R. China.
Yue MingDepartment of Pharmacy, Daping Hospital, Army Medical University, Daping, Chongqing 400042, P.R. China.
Zhiwei LiDepartment of Pharmacy, Daping Hospital, Army Medical University, Daping, Chongqing 400042, P.R. China.
Haiyan XingDepartment of Pharmacy, Daping Hospital, Army Medical University, Daping, Chongqing 400042, P.R. China.
Jianhong ChenDepartment of Pharmacy, Daping Hospital, Army Medical University, Daping, Chongqing 400042, P.R. China.
Army Medical University · CNDaping Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The present study aimed to explore the effect of Saikosaponin D (SSD) and its underlying mechanism on apoptosis and autophagy in human breast cancer MDA‑MB‑231 cells. MTT assay, flow cytometry, western blotting and confocal fluorescence microscopy detection were employed. SSD, a kind of triterpenoid saponins extracted from Radix bupleuri, has been demonstrated to have the effects of anti‑inflammatory, antioxidative and anticancer effects and can regulate autophagy. The present study revealed that SSD induced apoptosis through the activation of the p38 mitogen‑activated protein kinase (MAPK) signaling pathway in human breast cancer MDA‑MB‑231 cells. The administration of SSD promoted the phosphorylation/activation of p38 MAPK in MDA‑MB‑231 cells, whereas pretreatment with SB203580, an effective p38 MAPK inhibitor, attenuated SSD‑mediated apoptosis, the cleavage of PARP and the activation of caspase‑3. In addition, SSD blocked autophagic degradation by inhibiting autolysosome formation, resulting in the accumulation of autophagosomes. Mechanistically, the results of the present study revealed that SSD inhibited the formation of autophagosomes by inhibiting autophagosome‑lysosome fusion, rather than by damaging lysosome function. Furthermore, blocking autophagy degradation was not associated with SSD‑mediated apoptosis. The genetic knockdown of autophagy‑related protein 5 markedly reduced SSD‑mediated LC3B‑II accumulation; however, it did not affect the SSD‑mediated phosphorylation/activation of p38, cleavage of PARP, activation of caspase‑3 or apoptosis. In conclusion, the findings of the present study suggest that SSD may induce apoptosis and block autophagic degradation, which provides further evidence of the association between the inhibition of autophagic degradation and cell death.

Indexed as

ApoptosisAutophagosomesAutophagyAutophagy-Related Protein 5Breast NeoplasmsCaspase 3Cell Line, TumorGene Knockdown TechniquesHumansLysosomesMicrotubule-Associated ProteinsOleanolic Acidp38 Mitogen-Activated Protein KinasesPoly(ADP-ribose) PolymerasesSaponinsAutophagy-Related Protein 5CASP3 protein, humanCaspase 3MAP1LC3B protein, humanMicrotubule-Associated ProteinsOleanolic Acidp38 Mitogen-Activated Protein KinasesPoly(ADP-ribose) Polymerasessaikosaponin DSaponinsapoptosisautophagybreast cancer cellssaikosaponin d

Identifiers

PMID32468000
PMCPMC7339770
OpenAlexW3025403825

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.