mTFP1 Fluorescent Protein Reporter System
- Known as:
- mTFP1 Fluorescent Protein Reporter System
- Catalog number:
- ABP-FP-RPTFP01
- Product Quantity:
- 1 set
- Category:
- -
- Supplier:
- Allele
- Gene target:
- mTFP1 Fluorescent Protein Reporter System
Related genes to: mTFP1 Fluorescent Protein Reporter System
- Gene:
- MTFP1 NIH gene
- Name:
- mitochondrial fission process 1
- Previous symbol:
- -
- Synonyms:
- MTP18, HSPC242
- Chromosome:
- 22q12.2
- Locus Type:
- gene with protein product
- Date approved:
- 2010-09-02
- Date modifiied:
- 2016-10-05
Related products to: mTFP1 Fluorescent Protein Reporter System
Related articles to: mTFP1 Fluorescent Protein Reporter System
- The erythropoietin receptor (EPOR) is a single-pass transmembrane protein that homo-dimerizes upon binding with its renal ligand erythropoietin (EPO) to trigger downstream signaling. Its extracellular ectodomain mediates ligand binding. Therefore, a fusion protein of the EPOR ectodomain can be useful for various in vitro assays, such as a binding assay with an EPO-like peptide, if overexpressed in Escherichia coli (E.coli). In this study, we hypothesized that fusion proteins of the EPOR ectodomain with mCitrine or mTFP1, expressed in bacteria, could enable in vitro Förster resonance energy transfer experiments. Two fusion proteins, EPOR-mCitrine and EPOR-mTFP1, were overexpressed in E. coli but obtained as inclusion bodies. Urea solubilization and stepwise dialysis yielded soluble fusion proteins. Circular dichroism spectroscopy revealed that EPOR-mCitrine had greater secondary structure content than EPOR-mTFP1. When combined with recombinant human EPO, the hydrodynamic radius of EPOR-mCitrine changed, as measured using dynamic light scattering, confirming binding. This interaction was further validated using isothermal titration calorimetry. We propose that bacterially produced EPOR-mCitrine is a useful in vitro tool for measuring EPO binding. - Source: PubMed
Publication date: 2026/03/27
Kang EunhoAshim JanbolatJi SanghoHan Min AeYu WookyungKim Sung JaeHong EunmiMoon CheilLee Chang-Hun - Oocyte maturation is a complex process that is regulated by a variety of factors. Mitochondria are a key factor affecting oocyte maturation in vitro. Mitochondrial fission process 1 (MTFP1) is located on the inner mitochondrial membrane and mediates the fission of this membrane. However, the role and mechanism of MTFP1 in bovine oocyte maturation are still unclear. Therefore, we performed siRNA-mediated MTFP1 knockdown during in vitro maturation of bovine oocytes and assessed its effects on oocyte maturation as well as mitochondrial function and dynamics. We found that MTFP1 is expressed at all stages of bovine oocyte maturation. Moreover, MTFP1 knockdown decreased oocyte maturation efficiency. These observations, combined with our transcriptome sequencing results, showed that MTFP1 knockdown caused mitochondrial dysfunction, impaired nuclear and cytoplasmic maturation, promoted mitochondrial fusion, induced mitophagy and decreased oocyte apoptosis. In summary, the inner mitochondrial membrane protein MTFP1 plays a crucial role in bovine oocyte maturation. The results provide a reference and theoretical basis for improving the quality of in vitro oocyte maturation and breeding efficiency in beef cattle. - Source: PubMed
Publication date: 2026/03/28
Han TiancangZhao YuhanSun ZhaoyangJiao AnhuiWang BingbingGao Qingshan - : Mitochondrial dysfunction is central to the pathogenesis of acute myocardial infarction (AMI), but mitochondria-related molecular biomarkers and mechanisms remain incompletely defined. This study aimed to identify mitochondria-associated biomarkers in AMI and elucidate their functional roles in mitochondrial dynamics, extracellular matrix (ECM) remodeling, and cardiac protection. : Two GEO datasets (GSE19322, GSE71906) were analyzed to identify mitochondria-related differentially expressed genes (DE-MRGs) by intersecting DEGs with MitoCarta3.0 genes. Functional enrichment (GO/KEGG), LASSO regression, ROC curves, and nomogram modeling were employed to screen biomarkers. Immune infiltration profiling, GeneMANIA, GSEA, TF-mRNA and ceRNA network construction, and drug prediction analyses were performed. Expression validation was conducted via RT-qPCR, Western blot (WB), and immunohistochemistry (IHC) in murine AMI models and hypoxia-induced cardiomyocytes. Functional assays assessed cardiac performance (echocardiography), infarct size (TTC staining), fibrosis (Masson/Sirius red), oxidative stress (ROS), and ECM remodeling (MMP9/TIMP1 axis). : We identified 295 DE-MRGs, enriched in oxidative phosphorylation and mitochondrial metabolic pathways. Machine learning and validation analyses pinpointed MTFP1 and DNAJC28 as AMI biomarkers with strong diagnostic accuracy. In vivo and in vitro studies confirmed marked downregulation of MTFP1 post-AMI and under hypoxia. AAV9-mediated MTFP1 overexpression improved cardiac function, reduced infarct size, attenuated fibrosis, and decreased ROS levels. Mechanistically, MTFP1 upregulated phosphorylated DRP1 (Ser616) without altering total DRP1, balanced MMP9/TIMP1 activity, and suppressed fibrosis markers (COL1A1, α-SMA). Gelatin zymography indicated that MMP9 activation remained restrained despite elevated pro-MMP9, consistent with TIMP1-mediated regulation. Hypoxia-induced cardiomyocytes showed similar antifibrotic and antioxidative responses following MTFP1 overexpression. : Our study identified MTFP1 as a novel mitochondria-related biomarker and therapeutic modulator in AMI. MTFP1 exerts cardioprotective effects by restoring mitochondrial fission balance and ECM remodeling through the p-DRP1/MMP9/TIMP1 signaling axis, attenuating fibrosis and oxidative stress. These findings provide mechanistic insight into mitochondria-targeted cardioprotection and highlight MTFP1 as a promising diagnostic and therapeutic target for AMI. - Source: PubMed
Publication date: 2026/03/09
Hu XiBao HailongHuang YueCao ZhaoxingYang WeiHuang ChengChen XinChen YanbingChen BingxiuXia GuilingYang XiaoHuang RunzeChen Zhangrong - Liver metastasis is a common and fatal event for patients with pancreatic ductal adenocarcinoma (PDAC). Dysregulated mitochondrial dynamics reshape biological processes, including metabolism reprogramming, which disrupts immune cell function and promotes metastatic progression. - Source: PubMed
Publication date: 2026/02/20
Chen YangJin Gao-WeiHe Li-HongDong YuZhang Yan-NaGuo Han-XiangXu Yi-TingWei Zi-YangDang Bin-FeiMu Chun-YangCao Wan-YueZhang Yi-ZeWei Xiao-BaoFeng Yu-XiongLiu Yun-HuaZhang QiLiang Ting-Bo - Pancreatic β-cells are uniquely dependent on mitochondrial metabolism to couple glucose sensing to insulin secretion, a process impaired in diabetes. Mitochondrial fission process 1 (MTFP1) is an inner mitochondrial membrane protein that plays pleiotropic, tissue-specific roles in mitochondrial function and dynamics. Our previous work has identified Mtfp1 mRNA as a target for miR-125b, a microRNA that negatively regulates insulin secretion from β-cells. Nevertheless, the function of MTFP1 in these cells remained unexplored. Here, we show that MTFP1 is essential for normal glucose-stimulated insulin secretion (GSIS) in mouse and human cell lines and islets, and that mice with β-cell-specific elimination of MTFP1 develop glucose intolerance. Whereas β-cell survival and mitochondrial content were unaffected, oxidative phosphorylation and ATP production were sharply lowered. These changes were accompanied by disruption of mitochondrial cristae structure and a reduced contact surface with the endoplasmic reticulum, providing a mechanistic basis for defective stimulus-secretion coupling. Conversely, MTFP1 overexpression in mouse and human islets sufficed to improve mitochondrial respiration and GSIS. Finally, MTFP1 downregulation blocked the positive effects of miR-125b elimination in GSIS and mitochondrial respiration, unveiling MTFP1 as a downstream effector of miR-125b. Together, our findings identify MTFP1 as a critical regulator of β-cell mitochondrial architecture and function, necessary for efficient insulin secretion and glucose homeostasis, and a potential therapeutic target to enhance β-cell bioenergetic resilience in diabetes. - Source: PubMed
Publication date: 2026/02/03
Sarwat SuneheraAlen RosaWu ZhiyiZhang ChuyuePaszek MichaelYang MingMingOstinelli GiadaMihalovits AlinaBaker BellWai TimothyRutter Guy ARodriguez Tristan AMartinez-Sanchez Aida