Evidence map›Paper›PMID 34784299›Full record

ArticleJCI insight2021

CPVL promotes glioma progression via STAT1 pathway inhibition through interactions with the BTK/p300 axis.

Hui Yang, Xiaocen Liu, Xiaolong Zhu, Xueqin Li, Lan Jiang, Min Zhong, Mengying Zhang, Tianbing Chen, Mingzhe Ma, Xiuming Liang and 1 more

Open access · goldAbstract read
In one paragraph

Article in JCI insight, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 21 citations in OpenAlex.

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  11. [Lactate-induced up-regulation of PLEKHA4 promotes proliferation and apoptosis of human glioma cells].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2023
    Article
  12. Article
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  14. Article
  15. Article
  16. Article
  17. BTK, the new kid on the (oncology) block?Frontiers in oncology · 2022
    Review
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

11 authors at 3 institutions in 2 countries.

Hui YangKey Laboratory of Non-coding RNA Transformation Research of Anhui Higher Education Institution.
Xiaocen LiuKey Laboratory of Non-coding RNA Transformation Research of Anhui Higher Education Institution.
Xiaolong ZhuKey Laboratory of Non-coding RNA Transformation Research of Anhui Higher Education Institution.
Xueqin LiKey Laboratory of Non-coding RNA Transformation Research of Anhui Higher Education Institution.
Lan JiangKey Laboratory of Non-coding RNA Transformation Research of Anhui Higher Education Institution.
Min ZhongKey Laboratory of Non-coding RNA Transformation Research of Anhui Higher Education Institution.
Mengying ZhangKey Laboratory of Non-coding RNA Transformation Research of Anhui Higher Education Institution.
Tianbing ChenKey Laboratory of Non-coding RNA Transformation Research of Anhui Higher Education Institution.
Mingzhe MaDepartment of Gastric Surgery, Fudan University Shanghai Cancer Center, Shanghai, PR China.
Xiuming LiangBiomolecular Medicine, Clinical Research Center, Department of Laboratory Medicine, Karolinska Institutet, Stockholm, Sweden.
Kun LvKey Laboratory of Non-coding RNA Transformation Research of Anhui Higher Education Institution.
Wannan Medical College · CNFudan University Shanghai Cancer Center · CNKarolinska Institutet · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CPVL (carboxypeptidase, vitellogenic-like) is a serine carboxypeptidase that was first characterized in human macrophages. However, the function of CPVL remains unclear in a variety of tumors. The quantitative PCR (qPCR), Western blotting, and IHC assays were utilized to measure the CPVL expression. CPVL was significantly upregulated in glioma cells and tissues compared with normal cells and tissues, respectively. Moreover, high CPVL expression was correlated with advanced clinical grade and poor prognosis. Silencing of CPVL promoted glioma cell apoptosis, and it inhibited cell proliferation and tumorigenicity in vitro and in vivo. Ingenuity Pathway Analysis (IPA) demonstrated that CPVL silencing activated the IFN-γ/STAT1 signaling pathway, thereby inducing glioma cell apoptosis. Mechanistically, immunopurification, mass spectrometry, IP, and glutathione S-transferase (GST) pull-down experiments elucidated that CPVL physically interacts with Bruton's tyrosine kinase (BTK) and downregulates the STAT1 phosphorylation through promoting p300-mediated STAT1 acetylation. Our findings reveal the crucial role of CPVL in promoting the progression of glioma through suppressing STAT1 phosphorylation. CPVL might serve as a potential prognostic biomarker and therapeutic target for the treatment of glioma.

Indexed as

CarboxypeptidasesCell Line, TumorDisease ProgressionE1A-Associated p300 ProteinGliomaHumansSTAT1 Transcription FactorCarboxypeptidasesCPVL protein, humanE1A-Associated p300 ProteinEP300 protein, humanSTAT1 protein, humanSTAT1 Transcription FactorOncogenesOncology

Identifiers

PMID34784299
PMCPMC8783677
OpenAlexW3212304172

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.