Evidence map›Paper›PMID 28160557›Full record

ArticleOncotarget2017

Cancer-associated oxidoreductase ERO1-α promotes immune escape through up-regulation of PD-L1 in human breast cancer.

Tsutomu Tanaka, Goro Kutomi, Toshimitsu Kajiwara, Kazuharu Kukita, Vitaly Kochin, Takayuki Kanaseki, Tomohide Tsukahara, Yoshihiko Hirohashi, Toshihiko Torigoe, Yoshiharu Okamoto and 3 more

Abstract read
In one paragraph

Article in Oncotarget, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed, 2 pooled it
–field-weighted citation impact
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

44 citing papers in PubMed, 2 syntheses or guidelines pooled it.

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  15. Endoplasmic reticulum stress targeted therapy for breast cancer.Cell communication and signaling : CCS · 2022
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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

13 authors.

Tsutomu TanakaDepartment of Pathology, Sapporo Medical University, Sapporo, Japan.
Goro KutomiDepartment of Surgery, Sapporo Medical University, Sapporo, Japan.
Toshimitsu KajiwaraDepartment of Pathology, Sapporo Medical University, Sapporo, Japan.
Kazuharu KukitaDepartment of Surgery, Sapporo Medical University, Sapporo, Japan.
Vitaly KochinDepartment of Pathology, Sapporo Medical University, Sapporo, Japan.
Takayuki KanasekiDepartment of Pathology, Sapporo Medical University, Sapporo, Japan.
Tomohide TsukaharaDepartment of Pathology, Sapporo Medical University, Sapporo, Japan.
Yoshihiko HirohashiDepartment of Pathology, Sapporo Medical University, Sapporo, Japan.
Toshihiko TorigoeDepartment of Pathology, Sapporo Medical University, Sapporo, Japan.
Yoshiharu OkamotoJoint Department of Veterinary Medicine, Tottori University, Tottori, Japan.
Koichi HirataDepartment of Surgery, Sapporo Medical University, Sapporo, Japan.
Noriyuki SatoDepartment of Pathology, Sapporo Medical University, Sapporo, Japan.
Yasuaki TamuraDepartment of Molecular Therapeutics, Institute for the Business-Regional Collaboration, Center for Food & Medical Innovation, Hokkaido University, Sapporo, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many human cancers have been reported to have enhanced expression of the immune checkpoint molecule programmed death-ligand 1 (PD-L1), which binds to programmed cell death-1 (PD-1) expressed on immune cells. PD-L1/PD-1 plays a role in inhibition of antitumor immunity by inducing T cell apoptosis and tolerance. Thus, it is crucial to elucidate mechanisms of PD-L1 expression on cancer cells. ERO1-α is an oxidase located in the endoplasmic reticulum. It is overexpressed in a variety of tumor types and it plays a role in disulfide bond formation in collaboration with PDI. Here, we investigated the influence of ERO1-α on expression of PD-L1 and immune escape. We demonstrated that ERO1-α augmented the expression of PD-L1 via facilitation of oxidative protein folding within PD-L1. In addition, we showed that overexpression of ERO1-α increased HIF-1α protein expression, resulting in an increase of PD-L1 mRNA as well as protein. In clinical cases, we observed that the expression of ERO1-α in triple negative breast cancer was related to the expression of PD-L1. Moreover, apoptosis of Jurkat leukemia T cells, which express PD-1, induced by tumor PD-L1 was inhibited when ERO1-α was depleted. The results suggest that targeting ERO1-α in tumor cells can be a novel approach for cancer immunotherapy. Therefore, the role of ERO1-α in tumor-mediated immunosuppression should be further explored.

Indexed as

ApoptosisB7-H1 AntigenBreast NeoplasmsCell Line, TumorFemaleHumansInterferon-gammaJurkat CellsLeukemia, T-CellMembrane GlycoproteinsOxidoreductasesProtein FoldingTransfectionTriple Negative Breast NeoplasmsTumor EscapeUp-RegulationB7-H1 AntigenCD274 protein, humanERO1A protein, humanInterferon-gammaMembrane GlycoproteinsOxidoreductasesdisulfide bondERO1-αoxidoreductasePD-L1triple negative breast cancer

Identifiers

PMID28160557
PMCPMC5421881

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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.