Evidence map›Paper›PMID 32846884›Full record

ArticleInternational journal of molecular sciences2020

Characterizing the Relapse Potential in Different Luminal Subtypes of Breast Cancers with Functional Proteomics.

Tung-Yi Lin, Pei-Wen Wang, Chun-Hsun Huang, Pei-Ming Yang, Tai-Long Pan

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

25 citing papers in PubMed, 26 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

5 authors at 4 institutions in 1 country.

Tung-Yi LinDepartment of Traditional Chinese Medicine, Chang Gung Memorial Hospital at Keelung, Keelung 20401, Taiwan.ORCID 0000-0001-6495-7221
Pei-Wen WangDepartment of Medical Research, China Medical University Hospital, China Medical University, Taichung 40447, Taiwan.
Chun-Hsun HuangDepartment of Cosmetic Science, Research Center for Food and Cosmetic Safety, and Research Center for Chinese Herbal Medicine, College of Human Ecology, Chang Gung University of Science and Technology, Taoyuan 33303, Taiwan.
Pei-Ming YangTMU Research Center of Cancer Translational Medicine, Taipei 11042, Taiwan.ORCID 0000-0002-4004-2518
Tai-Long PanDepartment of Cosmetic Science, Research Center for Food and Cosmetic Safety, and Research Center for Chinese Herbal Medicine, College of Human Ecology, Chang Gung University of Science and Technology, Taoyuan 33303, Taiwan.ORCID 0000-0002-0187-8689
Chang Gung University of Science and Technology · TWChina Medical University · TWKeelung Chang Gung Memorial Hospital · TWTaipei Medical University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Poor prognosis due to the high relapse and metastasis rates of breast cancer has been particularly linked to the luminal B subtype. The current study utilized MCF-7 and ZR-75-1 to investigate various luminal subtypes of breast cancers that have discrepant expressions in the estrogen receptor (ER) and human epidermal growth factor receptor 2 (HER2). Understanding of the differential protein profiles and the associated pathways could help alleviate the malignance and promote the long-term survival rate of breast cancer patients. Functional proteome tools were applied to comprehensively delineate the global protein alterations that reflect the varieties of biological features between the two subtypes. In this study, a total of 11 proteins with significant and meaningful changes were identified. These protein targets including PRX2, CK19, nucleophosmin and cathepsin D were mostly involved in cell differentiation or proliferation. Particularly, cathepsin D was highly expressed in the luminal B subtype. Moreover, the level of cathepsin-D was also upregulated in the clinical metastatic tissues. Accordingly, the RNA interference-mediated silencing of cathepsin D stimulated ER expression but suppressed the level of HER2. The knockdown of cathepsin D enhanced the level of ZO-1 and a remarkable decrease in N-cadherin was also detected. Again, the matrix metalloproteinases (MMP) activity was impaired under the cathepsin D abolishment. Collectively, this study represented a modality to explore novel relationships in a proteome complex and highlighted the functional roles of cathepsin D in treatment options for different subtypes of breast cancer.

Indexed as

Biomarkers, TumorBreast NeoplasmsCathepsin DErb-b2 Receptor Tyrosine KinasesFemaleHumansLymphatic MetastasisMCF-7 CellsNeoplasm Recurrence, LocalPrognosisProteomeProteomicsReceptors, EstrogenTumor Cells, CulturedBiomarkers, TumorCathepsin DERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesProteomeReceptors, Estrogenbreast cancerestrogen receptorhuman epidermal growth factor receptor 2luminal B subtypenetwork analysisproteomics

Identifiers

PMID32846884
PMCPMC7504407
OpenAlexW3081303327

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.