Evidence map›Paper›PMID 40420098›Full record

ArticleJournal of orthopaedic surgery and research2025

TRIM55 suppresses inflammatory response after spinal cord injury by accelerating the ubiquitination and degradation of TLR4.

Yang Li

Abstract read
In one paragraph

Article in Journal of orthopaedic surgery and research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

1 author.

Yang LiOrthopedics and Traumatology Department 3 (Spine), Changsha Hospital of Traditional Chinese Medicine Tianxin Campus, No.542, Shuyuan Road, Tianxin District, Changsha City, 410002, Hunan Province, China. 15211103675@163.com.

Funding

Scientific Research Fund of Changsha Municipal Health Commission KJ-B2023074
6 · The paper itself

Abstract

backgroundSpinal cord injury (SCI) is a neurological disorder characterized by severe and often irreversible damage to the spinal cord, for which no effective treatments currently exist. Ubiquitination, a reversible post-translational modification, plays a critical role in regulating protein degradation and stabilization. Tripartite motif-containing 55 (TRIM55), an E3 ubiquitin ligase, belongs to the TRIM protein family. This study aimed to explore the potential mechanism of TRIM55 in SCI.

methodsAn SCI rat model was established to investigate the effects of TRIM55 on SCI. LPS-stimulated PC12 cells were used to evaluate inflammation by measuring IL-1β, IL-6, and TNF-α levels using enzyme-linked immunosorbent assays. The proliferation and apoptosis of PC12 cells were assessed using the cell counting kit-8 assay and TUNEL staining. Quantitative real-time PCR, western blot analysis, co-immunoprecipitation, and cycloheximide chase experiments were performed to elucidate the underlying mechanism.

resultsThe findings revealed that TRIM55 was downregulated both in vitro and in vivo. Functionally, TRIM55 inhibited apoptosis and reduced the expression of pro-inflammatory cytokines in LPS-stimulated PC12 cells. Mechanistically, TRIM55 interacted with toll-like receptor 4 (TLR4) and promoted its degradation by modulating the ubiquitination process, thereby attenuating the inflammatory response. Furthermore, TRIM55 enhanced recovery from SCI and alleviated inflammation in vivo.

conclusionThis study not only provides robust theoretical evidence supporting TRIM55 as an anti-inflammatory factor but also offers a novel therapeutic approach for SCI research.

Indexed as

InflammationSpinal Cord InjuriesToll-Like Receptor 4UbiquitinationUbiquitin-Protein LigasesAnimalsApoptosisDisease Models, AnimalDown-RegulationMalePC12 CellsProteolysisRatsRats, Sprague-DawleyTripartite Motif ProteinsTlr4 protein, ratToll-Like Receptor 4Tripartite Motif ProteinsUbiquitin-Protein LigasesInflammationSpinal cord injuryTLR4TRIM55Ubiquitination

Identifiers

PMID40420098
PMCPMC12108013

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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 Socratic graph.