Evidence map›Paper›PMID 41399074›Full record

ArticleBeijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences2025

[Effect of dephosphorylation of tumor metastasis suppressor gene

Yanhua Liu, Min Lu, Xuyang Zhao, Kuan'gen Zhang, Rui Wu, Fang Mei, Zhihao Dai, Jiangfeng You, Fei Pei

Abstract readEnglish Abstract
In one paragraph

Article in Beijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Yanhua LiuDepartment of Pathology, School of Basic Medical Sciences Peking University / Peking University Third Hospital, Beijing 100191, China.
Min LuDepartment of Pathology, School of Basic Medical Sciences Peking University / Peking University Third Hospital, Beijing 100191, China.
Xuyang ZhaoPeking University Institute of Systems Biomedicine, Beijing 100191, China.
Kuan'gen ZhangDepartment of Pathology, School of Basic Medical Sciences Peking University / Peking University Third Hospital, Beijing 100191, China.
Rui WuDepartment of Pathology, School of Basic Medical Sciences Peking University / Peking University Third Hospital, Beijing 100191, China.
Fang MeiDepartment of Pathology, School of Basic Medical Sciences Peking University / Peking University Third Hospital, Beijing 100191, China.
Zhihao DaiDepartment of Pathology, School of Basic Medical Sciences Peking University / Peking University Third Hospital, Beijing 100191, China.
Jiangfeng YouDepartment of Pathology, School of Basic Medical Sciences Peking University / Peking University Third Hospital, Beijing 100191, China.
Fei PeiDepartment of Pathology, School of Basic Medical Sciences Peking University / Peking University Third Hospital, Beijing 100191, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectiveTo explore the effects and the molecular mechanisms of homo sapiens longevity assurance homolog 2 of yeast LAG1(LASS2) dephosphorylation on the biological functions of prostate cancer cells.

methodsFirstly, we examined the expression profiles of LASS2 by immunohistochemical staining using microarray sections from 90 human patients with prostate cancer; then FLAG-tagged

resultsLASS2 levels decreased with increasing Gleason scores of prostate cancer tissues by immunohistochemical staining; moreover, proteome analysis by mass spectrometry had identified that three residues in the C-terminal region of LASS2(Ser-341, Ser-348, and Ser-349) were phosphorylated. Dephosphorylation of LASS2 at serine residue 348 significantly enhanced growth, migration (from 49.11%±5.62% to 74.28%±8.77%,

conclusionPhosphorylation of LASS2 is essential for regulation of V-ATPase activity, and serine residue 348 of LASS2 is illustrated to be a key phosphorylation site. Phosphorylated LASS2 inhibits prostate cancer cell invasion

Indexed as

Cytoskeletal ProteinsMembrane ProteinsProstatic NeoplasmsSphingosine N-AcyltransferaseTumor Suppressor ProteinsVacuolar Proton-Translocating ATPasesCell Line, TumorCell MovementCell ProliferationHEK293 CellsHumansMaleMatrix Metalloproteinase 2Neoplasm InvasivenessPhosphorylationATP6V0C protein, humanCERS2 protein, humanCytoskeletal ProteinsMatrix Metalloproteinase 2Membrane ProteinsSphingosine N-AcyltransferaseTumor Suppressor ProteinsVacuolar Proton-Translocating ATPasesGene expression regulation, neoplasticLASS2 geneNeoplasm invasivenessProstatic neoplasmsVacuolar proton-translocating ATPases

Identifiers

PMID41399074
PMCPMC12711421

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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.