SIRT3
- Known as:
- SIRT3
- Catalog number:
- Y213470
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- SIRT3
Related genes to: SIRT3
- Gene:
- SIRT3 NIH gene
- Name:
- sirtuin 3
- Previous symbol:
- -
- Synonyms:
- SIR2L3
- Chromosome:
- 11p15.5
- Locus Type:
- gene with protein product
- Date approved:
- 2001-03-20
- Date modifiied:
- 2014-11-18
Related products to: SIRT3
Related articles to: SIRT3
- Intestinal ischemia-reperfusion (I/R) injury constitutes a life-threatening condition with mortality approaching 50%, yet effective therapeutic interventions remain limited. Resveratrol, a natural polyphenolic compound, has demonstrated promising multi-targeted protective effects in preclinical models by simultaneously enhancing antioxidant defense, suppressing inflammatory cascades, inhibiting ferroptosis, stabilizing mast cells, and preserving intestinal barrier integrity through SIRT1/SIRT3-mediated pathways. Novel delivery systems, including exosome-based carriers and nanoformulations, have shown enhanced therapeutic efficacy in overcoming bioavailability limitations. However, a critical translational gap persists between experimental promise and clinical reality. Three interconnected obstacles impede progress: the complete absence of human clinical trials in intestinal I/R contexts, poor pharmacokinetics characterized by extensive first-pass metabolism that raises fundamental questions about achievable therapeutic tissue concentrations, and the lack of large animal validation studies bridging rodent models and human pathophysiology. This review provides critical analysis of evidence quality, identifies specific knowledge gaps, and proposes a structured translational roadmap prioritizing clinically relevant post-ischemic treatment paradigms, comprehensive pharmacokinetic characterization, biomarker development, and proof-of-concept clinical trials to advance resveratrol toward clinical benefit. - Source: PubMed
Publication date: 2026/03/23
Zhang Xue-FengHuang ZhiZeng YuanZhang YanLi PingWang Fei-XiangNie Liang - To study the effect and mechanism of geniposide (GE) on lipopolysaccharide (LPS)-induced inflammatory injury in human coronary artery endothelial cells (HCAECs). - Source: PubMed
Sun Wen-TingZhao Miao-MiaoShi Zhao-Ling - Mitochondrial transcription factor A (TFAM) plays a crucial role in mitochondrial fission beyond its canonical function in mtDNA maintenance. However, how TFAM regulates mitochondrial fission remains only partially understood. Fluorescence microscopy and TEM analyses showed that TFAM knockdown inhibited mitochondrial fission, whereas TFAM overexpression promoted mitochondrial fragmentation, and this mitochondrial morphology phenotype was supported by TEM-based ultrastructural observations in zebrafish embryos with tfam disruption. Depletion of Drp1 and MFF in TFAM-overexpressing cells led to elongated mitochondria, indicating that TFAM promotes Drp1- and MFF-dependent mitochondrial fission, which was further supported by the inhibitory effects of Mdivi-1 (Drp1 inhibitor) and Compound C (AMPK inhibitor) on TFAM-induced mitochondrial fission. Western blot and immunofluorescence analyses revealed that TFAM overexpression enhanced the mitochondrial localization and Sirt3-dependent mitochondrial protein deacetylation of Sirtuin 3 (Sirt3), increased phosphorylation of AMPK and MFF, and promoted mitochondrial recruitment of phosphorylated Drp1. Proteinase K protection and cycloheximide chase assays further supported intramitochondrial localization of Sirt3 and increased stability of mitochondrial Sirt3 upon TFAM overexpression. FRET imaging and co-immunoprecipitation demonstrated a direct TFAM-Sirt3 interaction mediated by TFAM's HMG-box A domain. Targeted mutagenesis or deletion of the HMG-box A domain disrupted the TFAM-Sirt3 interaction, impaired Sirt3 mitochondrial localization and Sirt3-dependent mitochondrial protein deacetylation, and abolished TFAM-mediated mitochondrial fission. Analysis of TCGA data showed that high TFAM-SIRT3 co-expression is associated with overall survival across cancers, particularly in Kidney Renal Clear Cell Carcinoma (KIRC), where TFAM is downregulated (whereas SIRT3 is not). Together, these findings demonstrate that TFAM promotes mitochondrial fission via direct interaction with Sirt3, thereby activating the AMPK/MFF/Drp1 pathway. - Source: PubMed
Publication date: 2026/04/21
Zhai ShixianHuang ZihongLuo ZeweiAn ChunchunGao LuChen Tongsheng - Cancer progression is tightly linked to metabolic reprogramming and persistent redox imbalance, which together sustain tumour growth while simultaneously creating exploitable vulnerabilities. Reactive oxygen species (ROS), once viewed solely as damaging metabolic by-products, are now recognized as dynamic signalling molecules that regulate energy homeostasis, mitochondrial function, and cell-fate decisions. Central to this regulation is the ROS-AMP-activated protein kinase (AMPK)-sirtuin axis, an evolutionarily conserved network that integrates redox signals with cellular energy sensing and NAD⁺ metabolism. AMPK responds to energetic and oxidative stress by suppressing anabolic pathways and promoting catabolic adaptation, whereas NAD⁺-dependent sirtuins-particularly SIRT1, SIRT3, and SIRT6-translate metabolic and redox cues into coordinated transcriptional, epigenetic, and mitochondrial responses. At moderate ROS levels, activation of this axis restores metabolic equilibrium, enhances antioxidant defences, and preserves genomic stability; in contrast, excessive or sustained oxidative stress overwhelms adaptive capacity, driving mitochondrial dysfunction and apoptosis in metabolically compromised tumour cells. This review provides a mechanistic and translational synthesis of how ROS regulate AMPK and sirtuin activity through both energy-dependent and redox-dependent mechanisms, thereby reshaping cancer metabolism and redox homeostasis. We examine the context-dependent roles of individual sirtuin isoforms across nuclear, cytosolic, and mitochondrial compartments and discuss emerging therapeutic strategies targeting this network, including pharmacological AMPK activators, NAD⁺ boosters, sirtuin modulators, and redox-active nutraceuticals. Finally, we highlight key translational challenges and future directions, emphasizing biomarker-guided precision, isoform-specific targeting, and controlled modulation of ROS signalling. Collectively, this framework positions the ROS-AMPK-Sirtuin axis as a foundation for redox-guided metabolic oncology. - Source: PubMed
Singh Fathe - Chikungunya virus (CHIKV) infection can induce acute kidney injury (AKI) and may be fatal in severe cases, yet effective therapeutic strategies remain unclear. This study integrated computational analysis (network pharmacology and molecular docking) with experiments to evaluate the protective potential of oxymatrine against CHIKV-induced AKI and to explore its underlying mechanisms. Network pharmacology analysis identified 605 overlapping targets between CHIKV- and AKI-related genes, with core targets including TNF, AKT1, IL6, IL1B, and TP53, which were primarily enriched in the PI3K/AKT signaling pathway. RT-qPCR analysis and molecular docking further indicated that oxymatrine may interact with 18 targets, such as BAX, BCL2, and TLR4, thereby modulating CHIKV-associated PI3K/AKT signaling. experiments showed that oxymatrine at concentrations of 250-2,000 μM significantly increased the viability of HEK293T cells infected with CHIKV at a MOI of 0.01 for 24 h, with an average increase of approximately 25.8%. At these concentrations, oxymatrine reduced the expression of the CHIKV entry factor and regulated the PI3K/AKT, NF-κB, and TNF signaling pathways, which may contribute to the inhibition of viral replication. Further analysis revealed that CHIKV-induced AKI involved 75 ferroptosis-related targets and was closely associated with inflammatory responses. Oxymatrine may attenuate these effects through the regulation of targets such as SIRT3, AR, and FURIN. Consistently, ELISA results demonstrated that 1,000 μM oxymatrine significantly decreased the levels of IL-1β, TNF-α, and IL-6 in HEK293T cells infected with CHIKV. In conclusion, these findings suggest that oxymatrine may protect against CHIKV-induced AKI by limiting viral replication, modulating PI3K/AKT and NF-κB/TNF signaling pathways, suppressing inflammation, and regulating ferroptosis-related processes. - Source: PubMed
Publication date: 2026/04/02
Xin JiaLiangLi FangJunKang LuLuYang JieWang HaiTongWang WeiFeng ShengLiao XinFeiLi WenJieZhang He