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
- 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 - Inflammatory bowel disease (IBD) involves dysregulated immune responses and chronic intestinal inflammation. The nod-like receptor pyrin domain-containing 3 (NLRP3) inflammasome plays a critical role in IBD pathogenesis, but regulatory mechanisms remain not fully understood. Mitsugumin 53 (MG53, also known as TRIM72), originally identified as a critical membrane repair protein, has emerged as a novel regulator of inflammatory processes. To investigate the protective role of MG53 in colitis and elucidate its mechanisms in regulating NLRP3 inflammasome activation in IBD. - Source: PubMed
Publication date: 2026/03/18
Li ZhongguangDawson Zachary DLi XiangGuangZhao SerenaliBu MattewJiang FeiChen YuchenZhang MinZeng XindiPark Ki HoLu JingHe JinshanLee KyungEunBoyaka Prosper NLi HaichangMa Jianjie - Skeletal muscle regeneration declines with age despite the persistence of satellite cells (muscle stem cells, MuSCs), suggesting that regenerative impairment reflects functional dysregulation rather than MuSC depletion. Increasing evidence identifies early MuSC activation during the immediate post-injury period as a stress-sensitive, rate-limiting transition that is particularly vulnerable in aged muscle. Aged MuSCs exhibit elevated stress responses and reduced membrane remodeling capacity, accompanied by weakened activation-associated transcriptional induction. In contrast, proliferative and differentiation programs remain largely intact once activation is successfully initiated. These findings underscore that impaired coordination during early activation contributes to long-term regenerative decline in aging. Within this framework, MG53 (tripartite motif-containing protein 72, ), a muscle-enriched TRIM family E3 ubiquitin ligase originally identified as a mediator of sarcolemmal membrane repair, may also function as a stress-responsive regulator that stabilizes the early activation environment. Rather than directly determining cell fate, MG53 is proposed to facilitate activation by mitigating stress-associated membrane disruption and maintaining programmatic coordination under age-related physiological constraints. Most mechanistic evidence derives from rodent models, and direct validation in human aging muscle remains limited. These observations suggest that targeting early activation, rather than simply increasing proliferation, may better preserve regenerative capacity in aging skeletal muscle. - Source: PubMed
Publication date: 2026/03/05
Xu YanpingZih-Shuo Jethro WangZhang ZhentaoChen PengAlizai UsmanSathish KeerthikaLilian SakaiYan ZhiyuWhitson Bryan APawlik Timothy MZhu Hua - Inflammatory bowel disease (IBD) involves dysregulated immune responses and chronic intestinal inflammation. The nod-like receptor pyrin domain-containing 3 (NLRP3) inflammasome plays a critical role in IBD pathogenesis, but regulatory mechanisms remain not fully understood. Mitsugumin 53 (MG53, also known as TRIM72), originally identified as a critical membrane repair protein, has emerged as a novel regulator of inflammatory processes. To investigate the protective role of MG53 in colitis and elucidate its mechanisms in regulating NLRP3 inflammasome activation in IBD. - Source: PubMed
Publication date: 2026/02/19
Li ZhongguangDawson ZachLi XiangguangZhao SerenaliBu MatthewJiang FeiChen YuchenZhang MinZeng XindiPark Ki HoLu JingHe JinshanLee KyungEunBoyaka ProsperLi HaichangMa Jianjie