Ask about this productRelated genes to: TRIM72 Blocking Peptide
- Gene:
- TRIM72 NIH gene
- Name:
- tripartite motif containing 72
- Previous symbol:
- -
- Synonyms:
- MG53
- Chromosome:
- 16p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2006-03-30
- Date modifiied:
- 2016-03-22
Related products to: TRIM72 Blocking Peptide
Related articles to: TRIM72 Blocking Peptide
- Systemic lupus erythematosus (SLE) is a chronic autoimmune disease with diverse manifestations, including rash, arthritis, and nephritis. Although autoantibodies are a key feature of SLE, their levels often poorly reflect disease severity, suggesting the involvement of additional contributing factors. The tripartite motif-containing protein (TRIM) family, which regulates immunity, may play a role in SLE. Although TRIM21 is a known autoantigen, the roles of other TRIM family members remain unclear. The present study examined TRIM expression in SLE and evaluated the potential of TRIM proteins as biomarkers. TRIM expression in peripheral blood mononuclear cells was measured using reverse transcription quantitative polymerase chain reaction (PCR) and compared between patients with SLE (n = 33) and healthy controls (n = 20). Associations of TRIM expression with disease activity (active/inactive), renal involvement (nephritis/nonnephritis), clinical manifestations, and laboratory parameters were analyzed. The expression levels of several TRIM genes, specifically TRIM5, TRIM11, TRIM21, and TRIM72, were higher in patients with inactive SLE, nonnephritic disease, or low disease activity than in patients with active disease, nephritic disease, or relapsed SLE and healthy controls. The expression levels of these genes were considerably and negatively associated with clinical symptoms but not laboratory parameters. Hydroxychloroquine users exhibited higher levels of TRIM21 expression than did nonusers. Overall, specific TRIM proteins are inversely correlated with SLE disease activity and clinical phenotypes, which indicates their potential as biomarkers. Hydroxychloroquine may regulate TRIM21 expression. Further investigation into underlying mechanisms and continued TRIM monitoring are necessary to develop new SLE treatments and better assess disease progression. - Source: PubMed
Publication date: 2026/06/23
Lu Ling-YingYen Ling-JungHsia Hui-LingWeng Zi-XengChung Chi-HsiangHsu Paul Wei-CheChiu Chih-WeiChien Wu-ChienChang Tsung-Hsien - Idiopathic pulmonary fibrosis (IPF) is a severe and progressive disease with limited options for therapy. Mitsugumin 53 (MG53), a key factor involved in cell membrane repair, emerges as a protector in diverse disease models and cell injury. Although its role in pulmonary fibrosis is not well understood, this study focuses on exploring the function of MG53 in IPF and evaluating the therapeutic potential of recombinant MG53 protein. - Source: PubMed
Publication date: 2026/06/19
Miao JinruiWang HanFeng XiaoguoLiao LiweiDeng MingmingHou Gang - - Source: PubMed
Publication date: 2026/06/15
Berkel Caglar - Mitsugumin 53 (MG53, also TRIM72) is a muscle-enriched tripartite motif protein with a well-established role in acute membrane repair and cytoprotection in striated muscle and other stressed tissues. MG53 is a core component of cellular repair machinery, rapidly sensing membrane disruption and coordinating membrane resealing, mitochondrial preservation, and anti-inflammatory modulation. In contrast to its high expression in skeletal muscle, endogenous MG53 expression in the adult human heart is minimal, raising the question of how MG53 exerts cardioprotective effects in the human heart. Recent studies help address this by identifying MG53 as a circulating regenerative myokine. MG53 is secreted from skeletal muscle into the bloodstream and can reach distal organs, including the heart. These findings support a muscle-to-heart endocrine model in which MG53 mediates tissue crosstalk and helps provide repair capacity to the myocardium when intrinsic cardiac MG53 is low. Here, we summarize recent advances in MG53 biology, emphasizing molecular mechanisms and inter-organ communication underlying cardioprotection. We further highlight translational strategies leveraging recombinant MG53- and MG53-based therapeutics and discuss challenges that must be addressed for future clinical applications. Collectively, these insights support MG53 as an endocrine repair factor linking skeletal muscle to cardiac repair and a potential regenerative cardiovascular target. - Source: PubMed
Publication date: 2026/04/01
Chen YuchenLee Kyung EunKim JongsooKo Jae-KyunPark Ki Ho - The progression of acute kidney injury (AKI) to chronic kidney disease (CKD) remains a major clinical challenge. It is primarily triggered by renal tubular epithelial cell (RTEC) death that leads to persistent sterile inflammation, maladaptive repair and irreversible renal fibrosis. A pivotal event in RTEC death is plasma membrane rupture (PMR), which leads to the release of Damage-Associated Molecular Patterns (DAMPs). In this study, we identified Tripartite Motif-Containing 72 (TRIM72) as a critical regulator of Ninjurin-1 (NINJ1), a key mediator of PMR. Using tubule-specific knockout mice (Ninj1Ksp and Hmgb1Ksp) in a folic acid-induced AKI-CKD model, together with in vitro RTEC and immune cell assays, we delineated the TRIM72-NINJ1-HMGB1 signaling axis. We found that TRIM72 functions as an E3 ubiquitin ligase that targets NINJ1 at lysine 111 for proteasomal degradation, thereby restraining NINJ1-mediated PMR. Loss of TRIM72 stabilized NINJ1, exacerbated RTEC membrane rupture, and amplified the release of HMGB1. The resulting HMGB1 release propagated inflammation by promoting both macrophage-myofibroblast transition (MMT) and neutrophil extracellular trap (NET) formation, two major drivers of renal fibrosis. Consistently, tubule-specific deletion of either Ninj1 or Hmgb1 markedly attenuated the progression from AKI to CKD. Together, these findings establish the TRIM72-NINJ1-HMGB1 cascade as a central molecular pathway dictating the fate of injured RTECs and highlight TRIM72 as a promising therapeutic target for halting the transition from AKI to CKD. - Source: PubMed
Publication date: 2026/04/27
Ye KengLin SiyiChen CaimingChen ZhiminLin KongwenLi GuopingMa HuabinWu JianfengMak Tak WChen LiXu Yanfang