Evidence map›Paper›PMID 30980596›Full record

ArticleMolecular oncology2019

Biochemical pathways mediated by KLK6 protease in breast cancer.

Georgios Pampalakis, Eleni Zingkou, Konstantinos Gus Sidiropoulos, Eleftherios P Diamandis, Vassilis Zoumpourlis, George M Yousef, Georgia Sotiropoulou

Open access · goldAbstract read
In one paragraph

Article in Molecular oncology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed, 1 pooled it
0.9field-weighted citation impact, top 26% 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

11 citing papers in PubMed, 1 synthesis or guideline pooled it, 17 citations in OpenAlex.

  1. Biomarkers of tumor invasiveness in proteomics (Review).International journal of oncology · 2020
    Pooled it
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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

7 authors at 4 institutions in 2 countries.

Georgios PampalakisDepartment of Pharmacy, School of Health Sciences, University of Patras, Rion-Patras, Greece.
Eleni ZingkouDepartment of Pharmacy, School of Health Sciences, University of Patras, Rion-Patras, Greece.
Konstantinos Gus SidiropoulosThe Keenan Research Center in the Li Ka Shing Knowledge Institute, Department of Laboratory Medicine, St. Michael's Hospital, Toronto, Canada.
Eleftherios P DiamandisDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Canada.ORCID 0000-0002-1589-820X
Vassilis ZoumpourlisNational Hellenic Research Foundation, Athens, Greece.
George M YousefThe Keenan Research Center in the Li Ka Shing Knowledge Institute, Department of Laboratory Medicine, St. Michael's Hospital, Toronto, Canada.
Georgia SotiropoulouDepartment of Pharmacy, School of Health Sciences, University of Patras, Rion-Patras, Greece.
University of Patras · GRSt. Michael's Hospital · CANational Hellenic Research Foundation · GRUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kallikrein-related peptidase 6 (KLK6) is a serine protease normally expressed in mammary tissue and aberrantly regulated in breast cancer. At physiological levels, KLK6 functions as a suppressor of breast cancer, while its aberrant overexpression (> 50-fold higher than normal) is characteristic of a subset of breast cancers and has been linked to accelerated growth of primary breast tumors in severe combined immunodeficiency mice (Pampalakis et al. Cancer Res 2009, 69, 3779). Here, we investigated the molecular mechanisms underlying the concentration-dependent functions of KLK6 by comparing MDA-MB-231 stable transfectants expressing increasing levels of KLK6 in in vitro and in vivo tumorigenicity assays (soft agar, xenograft growth, tail vein metastasis). Quantitative proteomics was applied to identify proteins that are altered upon re-expression of KLK6 in MDA-MB-231 at normal or constitutive levels. Overexpression of KLK6 is associated with increased metastatic ability of breast cancer cells into lungs, increased expression of certain S100 proteins (S100A4, S100A11) and keratins (KRT), and downregulation of the apoptosis-related proteases CASP7 and CASP8, and RABs. On the other hand, KLK6 re-expression at physiological levels leads to inhibition of lung metastases associated with suppression of S100 proteins (S100A4, S100A10, S100A13, S100A16) and induced CASP7 and CASP8 expression. As this is the first report that KLK6 expression is associated with S100 proteins, caspases, RABs, and KRTs, we validated this finding in clinical datasets. By integrating proteomics and microarray data from breast cancer patients, we generated two composite scores, KLK6 + S100B-S100A7 and KLK6 + S100B-S100A14-S100A16, to predict long-term survival of breast cancer patients. We present previously unknown pathways implicating KLK6 in breast cancer. The findings promise to aid our understanding of the functional roles of KLK6 in breast cancer and may yield new biomarkers for the cancer types in which KLK6 is known to be aberrantly upregulated.

Indexed as

Signal TransductionAnimalsApoptosisBreast NeoplasmsCarcinogenesisCell Line, TumorFemaleGene Expression Regulation, NeoplasticHumansKallikreinsMice, SCIDNeoplasm ProteinsPhenotypeS100 ProteinsSurvival AnalysisKallikreinsKLK6 protein, humanNeoplasm ProteinsS100 ProteinsapoptosisKLK6proteomicsS100Atriple-negative breast cancer

Identifiers

PMID30980596
PMCPMC6822253
OpenAlexW2935983171

What OpenQuestion holds

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LicenceCC BY
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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.