Evidence map›Paper›PMID 40918453›Full record

ArticleOncology research2025

Inhibition of Proteasome LMP2 Activity Suppresses

Tatiana M Astakhova, Nikita S Karpov, Nataliya O Dashenkova, Elena V Alpeeva, Mikhail V Nesterchuk, Sergey B Akopov, Arsen S Mikaelyan, Anfisa S Ryabchenko, Pavel A Erokhov, Natalia P Sharova

Abstract read
In one paragraph

Article in Oncology research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–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

3 citing papers in PubMed.

  1. Article
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  3. 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

10 authors.

Tatiana M AstakhovaKoltzov Institute of Developmental Biology, Russian Academy of Sciences, Moscow, 119334, Russia.
Nikita S KarpovKoltzov Institute of Developmental Biology, Russian Academy of Sciences, Moscow, 119334, Russia.
Nataliya O DashenkovaKoltzov Institute of Developmental Biology, Russian Academy of Sciences, Moscow, 119334, Russia.
Elena V AlpeevaKoltzov Institute of Developmental Biology, Russian Academy of Sciences, Moscow, 119334, Russia.
Mikhail V NesterchukKoltzov Institute of Developmental Biology, Russian Academy of Sciences, Moscow, 119334, Russia.
Sergey B AkopovKoltzov Institute of Developmental Biology, Russian Academy of Sciences, Moscow, 119334, Russia.
Arsen S MikaelyanKoltzov Institute of Developmental Biology, Russian Academy of Sciences, Moscow, 119334, Russia.
Anfisa S RyabchenkoKoltzov Institute of Developmental Biology, Russian Academy of Sciences, Moscow, 119334, Russia.
Pavel A ErokhovKoltzov Institute of Developmental Biology, Russian Academy of Sciences, Moscow, 119334, Russia.
Natalia P SharovaKoltzov Institute of Developmental Biology, Russian Academy of Sciences, Moscow, 119334, Russia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Objectives: Proteasomes, multi-subunit proteases, are key actors of cellular protein catabolism and a number of regulatory processes. The detection of subtle proteasome functioning in tumors may contribute to our understanding of the mechanisms of cancer development. The current study aimed to identify the role of low molecular mass protein 2 (LMP2), a proteasome immune subunit, in the development of mouse colon 26 (C26) adenocarcinoma. Methods: The functions of the LMP2 subunit in tumor development in Balb/c mice were studied using its irreversible inhibitor KZR-504. LMP2 activity was detected by the hydrolysis of the fluorogenic substrate Ac-Pro-Ala-Leu-AMC. Western blotting and Quantitative Reverse Transcription Polymerase Chain Reaction (qRT-PCR) were used. We applied fluorescent tests for cell proliferation and apoptosis. M2 macrophages were obtained by polarization of mouse bone marrow-derived macrophages using the corresponding cytokines. Results: KZR-504 showed high specificity only for the LMP2 subunit and had no negative effect on C26 cells in culture. However, KZR-504 suppressed the formation of tumor conglomerates (by 74%, Conclusion: We discovered earlier unknown functions of the proteasome LMP2 subunit to facilitate the formation of tumor conglomerates and maintain

Indexed as

AdenocarcinomaColonic NeoplasmsCysteine EndopeptidasesProteasome Endopeptidase ComplexAnimalsApoptosisCell Line, TumorCell ProliferationGene Expression Regulation, NeoplasticHumansLeupeptinsMacrophagesMiceMice, Inbred BALB CProteasome Inhibitorsbenzyloxycarbonylleucyl-leucyl-leucine aldehydeCysteine EndopeptidasesLeupeptinsLMP-2 proteinProteasome Endopeptidase ComplexProteasome Inhibitorschitinase-3-like protein 3KZR-504M2 macrophagesMouse colon 26 adenocarcinomaproteasome low molecular mass protein 2 subunit

Identifiers

PMID40918453
PMCPMC12408852

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