Rat Dihydrolipoyl Transacetylase ELISA , DLAT
- Known as:
- Rat Dihydrolipoyl Transacetylase Enzyme-linked immunosorbent assay test , DLAT
- Catalog number:
- E02D0021
- Category:
- -
- Supplier:
- Blue Gene Biotech
- Gene target:
- Rat Dihydrolipoyl Transacetylase ELISA DLAT
Related genes to: Rat Dihydrolipoyl Transacetylase ELISA , DLAT
- Gene:
- DLAT NIH gene
- Name:
- dihydrolipoamide S-acetyltransferase
- Previous symbol:
- DLTA
- Synonyms:
- PDC-E2, E2
- Chromosome:
- 11q23.1
- Locus Type:
- gene with protein product
- Date approved:
- 1989-06-30
- Date modifiied:
- 2018-12-14
Related products to: Rat Dihydrolipoyl Transacetylase ELISA , DLAT
Related articles to: Rat Dihydrolipoyl Transacetylase ELISA , DLAT
- Alzheimer's disease (AD) is a neurodegenerative disorder characterized primarily by progressive cognitive impairment, whose pathogenesis involves multiple pathological processes including protein deposition, metal homeostasis dysregulation, oxidative stress, mitochondrial dysfunction, and neuroinflammation. In recent years, metabolism-related cell death modalities such as ferroptosis, cuproptosis, and disulfidptosis have gradually been recognized as potentially involved in neuronal damage in Alzheimer's disease. This review summarizes the fundamental mechanisms of ferroptosis, cuproptosis, and disulfidptosis, along with their research evidence in AD. Ferroptosis is primarily driven by iron imbalance, lipid peroxidation buildup, and impaired GPX4 defense. This process exhibits a bidirectional amplification loop with Aβ and tau pathologies. Cuproptosis contributes to neuronal damage through abnormal copper accumulation, FDX1-related mitochondrial protein lipoylation dysfunction, loss of iron-sulfur cluster proteins, and proteotoxic stress. Disulfidptosis links glucose metabolism disorders, insufficient reducing power, and actin cytoskeleton vulnerability, providing novel insights into metabolic stress and structural damage in AD. Furthermore, the three modes of cell death can undergo cross-regulation through the SLC7A11-NADPH-GSH/GPX4 axis, the FDX1-DLAT/DLST-iron-sulfur cluster axis, as well as upstream factors such as p53, NRF2, and AMPK. Metabolic cell death may constitute a critical pathological network in AD. Targeting these death pathways and their shared hubs is expected to provide new directions for disease stratification, biomarker development, and disease-modifying therapies. - Source: PubMed
Publication date: 2026/07/30
Ding ShuyuGuo ZihanJi HengyuHe Jinting - To investigate the role and mechanism of METTL14-mediated regulation of cuproptosis in myocardial ischemia-reperfusion injury (MI/RI). An MI/RI rat model was established. H9C2 cells were cultured and subjected to hypoxia/reoxygenation (H/R) modeling. Cells were transfected with siRNAs targeting METTL14 and ATP7A. Cell viability was detected by CCK-8 assay. Intracellular Cu levels were measured using a biochemical kit. The interaction between METTL14 and ATP7A mRNA was verified by RNA immunoprecipitation (RIP) assay. Adenovirus containing si-METTL14 was constructed and injected into rats, followed by the induction of the MI/RI model. Cardiac function was evaluated by measuring ejection fraction (EF) and fractional shortening (FS) using echocardiography. Rat myocardial tissues were collected for Hematoxylin and Eosin (HE) staining. The mRNA expression of m6A regulatory enzymes was detected by quantitative PCR (qPCR). Cu levels in myocardial tissue were measured using a biochemical assay kit. The expression of cuproptosis-related proteins was assessed by Western blot. MI/RI rats showed significantly decreased FS and EF values, with necrosis and hemorrhage, increased Cu content, elevated mRNA levels of FTO, METTL3, ALKBH5, and METTL14, decreased ATP7A protein expression, and increased protein expression of FDX1, LIAS, and DLAT in the myocardial tissue. Intramyocardial injection of adenovirus containing si-METTL14 reversed the MI/RI-induced changes. In vitro, decreased cell viability, increased Cu content, decreased ATP7A protein expression, and increased FDX1, LIAS, and DLAT protein expression were observed in H/R stimulated H9C2 cells, which were remarkably rescued by si-METTL14. Moreover, co-transfection with both si-METTL14 and si-ATP7A reversed effects induced by si-METTL14 alone. METTL14 promotes cuproptosis-associated changes and exacerbates MI/RI. - Source: PubMed
Zeng ShengqiangHong DezhiYang LiuWu Yanqing - Cuproptosis is a novel form of programmed cell death characterized by the accumulation of copper ions in the mitochondria, the formation of DLAT oligomers, and the depletion of Fe-S cluster proteins. However, the alterations in mitochondrial morphology and function during cuproptosis and the potential role of mitophagy in cuproptosis remain insufficiently elucidated. In this study, we induced cuproptosis of breast cancer cells using Elesclomol (ES) and assessed changes in mitochondrial reactive oxygen species, mitochondrial membrane potential, and oxygen consumption rate. Stable cell lines with overexpression or knockdown of PINK1/Parkin genes were constructed to elucidate the impact of mitophagy on cuproptosis. Subcutaneous mouse xenograft models were employed to identify drugs that may synergize with ES and enhance antitumor effects. Our results demonstrated that ES induced cuproptosis of breast cancer cells, which was associated with the activation of PINK1/Parkin-mediated mitophagy. Both gene knockdown and pharmacological inhibition of mitophagy enhanced the sensitivity of breast cancer cells to cuproptosis in vitro and in vivo. The combination of dichloroacetate (DCA) and ES exhibited a synergistic antitumor effect without significant tissue damage on the brain, heart, liver, and kidneys in subcutaneous mouse xenograft models. Collectively, our findings reveal that inhibiting PINK1/Parkin-mediated mitophagy enhances the sensitivity of breast cancer to cuproptosis, offering a novel combined treatment strategy for breast cancer. - Source: PubMed
Publication date: 2026/08/13
Tang ChaoyiSu KaZhan ZexuHuang RongzhiLuo MingLi Jiehua - Parkinson's disease (PD), the second most prevalent neurodegenerative disorder, is characterized by progressive loss of dopaminergic neurons in the substantia nigra. Although the molecular mechanisms of PD remain incompletely understood, mitochondrial dysfunction has emerged as a central pathological driver, highlighting the urgent need for therapies targeting mitochondrial homeostasis. In this study, we demonstrate that rhynchophylline (Rhy), a bioactive alkaloid from species, exerts neuroprotective effects by restoring mitochondrial dynamics. Thermal proteome profiling identified dihydrolipoamide acetyltransferase (DLAT) as a direct target of Rhy. Genetic ablation of DLAT induced mitochondrial fragmentation and abolished Rhy-mediated beneficial effects on mitochondrial structure and function. Mechanically, Rhy binds to the N-terminal lipoyl domain of DLAT, allosterically disrupting its interaction with sirtuin 4 (SIRT4) and subsequently enhancing DLAT lipoylation, a critical post-translational modification for mitochondrial energy metabolism. , Rhy administration ameliorated motor deficits and dopaminergic neurodegeneration in both the 6-OHDA-induced and A53T -synuclein transgenic PD mouse models. Single-nucleus RNA sequencing further highlighted the clinical relevance of DLAT dysregulation in PD. Collectively, our findings establish Rhy as a promising PD therapeutic candidate and delineate DLAT as a pivotal node in therapeutic targets by promoting mitochondrial fusion and bioenergetics, offering a novel mechanistic avenue for neuroprotection. - Source: PubMed
Publication date: 2026/06/11
Liang XiaominYang XunfangWang ShuhuiZhuo FangfangHou XingziTu PengfeiLiu YangZeng KewuZhang Qingying - Cancer-related fatigue (CRF) remains difficult to manage, and the impact of metal ion-regulated cell death on peripheral fatigue during anticancer therapy is unclear. Here, we investigated whether ferroptosis inducers (FINs) potentiate copper ionophore (CIN)-triggered cuproptosis in skeletal muscle and aggravate lung cancer-related fatigue (LCaRF), and evaluated redox-based interventions. LCaRF cellular models were established using C2C12 exposed to LLC/M109 tumor-conditioned supernatants and treated with FINs (sorafenib/erastin) plus CIN + CuCl (CIN-Cu + FINs). Cell viability, lipid peroxidation, DLAT aggregation (cuproptosis hallmark), copper/glutathione (GSH), mitochondrial function, and FKBP5/Nrf2-HO-1 signaling were assessed with pharmacologic and genetic modulation. An orthotopic lung cancer mouse model underwent wheel-running, tail suspension, and open-field testing with tetrathiomolybdate (TTM) or hydrogen as interventions. FINs sensitized C2C12 cells to CIN-Cu cytotoxicity and increased DLAT aggregation; copper chelation with TTM attenuated these effects. FINs depleted GSH and amplified mitochondrial dysfunction/ROS; exogenous GSH or hydrogen reduced DLAT aggregation and restored mitochondrial indices. FKBP5 was markedly upregulated by CIN-Cu + FINs and linked to suppressed antioxidant defense (Nrf2/HO-1). In vivo, CIN-Cu + FIN treatment exacerbated fatigue-like behaviors, while TTM or hydrogen partially improved performance. FIN-CIN combinations may aggravate skeletal muscle injury and fatigue-like phenotypes in LCaRF models by promoting cuproptosis via GSH depletion and FKBP5/Nrf2-HO-1 dysregulation. - Source: PubMed
Publication date: 2026/07/31
Chen MingPang YingHe YiMa YunanTang Lili