Ask about this productRelated genes to: PTPMT1 antibody
- Gene:
- PTPMT1 NIH gene
- Name:
- protein tyrosine phosphatase mitochondrial 1
- Previous symbol:
- -
- Synonyms:
- PLIP, DUSP23, MOSP
- Chromosome:
- 11p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-03-15
- Date modifiied:
- 2019-02-14
Related products to: PTPMT1 antibody
Related articles to: PTPMT1 antibody
- Anxiety disorders are highly heritable, but their underlying genetic mechanisms remain poorly understood. This study aimed to identify and functionally characterize genes whose expression is causally linked to anxiety disorder risk by integrating the parallel single-tissue genetic data. - Source: PubMed
Publication date: 2026/04/21
Wang LeshengXu ZhipengLuo GaomengWei WeiGuo MeimeiYuan YunheShi BeiGuan HaowenLiu ShaLi Xiang - Targeting metabolic vulnerabilities, particularly mitochondrial dysfunction, has emerged as a promising therapeutic strategy for glioma. However, the precise induction of specific cell death pathways non-genetic nanotherapeutics remains a significant challenge. Here, we report a triple-targeted DNA nanozyme designed to eliminate aggressive glioma by precisely inducing disulfidptosis. - Source: PubMed
Publication date: 2026/03/30
Wu TiantianLi LeZhang ShunZhang GuannanLi ChenMei JiamingChen XiaoyuanCheng Junjie - To investigate the causal relationship between mitochondrial genes and the pathogenesis of carotid plaque (CP), a multiomics-integrated Mendelian randomization (MR) analysis was performed in this study. - Source: PubMed
Publication date: 2025/11/01
Yu ZhuyuanMeng XiangyuanZong ZiyuSong QiHuo YingchaoChen Hao - Molecular cloning and heterologous protein expression are essential for investigating protein function and interactions with ligands such as small molecules, drugs, and other proteins. Studies on the redox regulation, intermolecular interactions, structural determination, and structural dynamics of mitochondrial protein phosphatases require high-yield expression of soluble, catalytically active enzymes. Accordingly, the aim of this study was to optimize the cloning, expression, and soluble purification of mitochondrial protein phosphatases in their monomeric and active forms. We designed 22 expression constructs encoding the mitochondrial protein phosphatases PTPMT1, PP2Cm, PPTc7, and PGAM5, incorporating variations with or without the mitochondrial targeting sequence (MTS) and solubility-enhancing fusion tags. Our results demonstrate that, for matrix localized phosphatases, MTS removal combined with a soluble fusion tag is essential for obtaining soluble, structurally stable, properly folded, and catalytically active proteins. In contrast, intermembrane space phosphatase PGAM5 was well structured and active across constructs, thoug MTS presence reduced expression yields and increased protein instability. Overall, this work underscores the critical role of rational construct design for the successful production of mitochondrial protein phosphatases suitable for in vitro biochemical and structural studies. - Source: PubMed
Publication date: 2025/12/24
Gabas Mariana LOtvos Luca PAlmeida Naira B OFarias Sofia OVal Giovanna SMachado Luciana E S F - Renal cell carcinomas (RCC) have recently been shown to exhibit a high abundance of phosphatidylglycerols, which are products of the protein-tyrosine phosphatase mitochondrial 1 enzyme (PTPMT1) and precursors of cardiolipins. Effective treatments for RCC are still in need. This study evaluates the therapeutic effect of PTPMT1 inhibition using the poorly water-soluble inhibitor alexidine dihydrochloride, which has not previously been proposed for RCC treatment. Considering that this inhibitor is poorly water-soluble and has inconsistent antitumor activity in its pure form due to solubility limits, we incorporated it in nanocarriers composed of phosphatidylcholine and cholesterol. These solvent-free nanocarriers had an average size of 66 nm, a drug loading capacity of 21%, an encapsulation efficiency of 99%, a positive surface charge, and excellent storage stability. We assessed their safety and efficacy in two human RCC cell lines, 786O and A498, alongside the human non-neoplastic kidney cell line HEK293 as a control. Results revealed a marked antitumor activity of the nanocarriers and selectivity toward highly metabolically active RCC cells. Thus, after only 24 h of treatment, a significant decrease in the viability of 786O cells was recorded, while A498 and control cells exhibited only minimal reductions in viability. Advanced mass spectrometry imaging (DESI-MSI) revealed that untreated 786O cells had significantly higher levels of phosphatidylglycerols, cardiolipins, and 4-hydroxynonenal glutathione compared to A498 and HEK293. Treatment with nanocarriers markedly impacted the levels of these metabolites in RCC cells. In conclusion, RCC tumors with upregulated phosphatidylglycerol metabolism may be particularly sensitive to PTPMT1 inhibition by nanocarriers. - Source: PubMed
Publication date: 2025/09/02
Sultan AdanZoabi AmaniMorshin AnnaShalev OriLazarovici PhilipMargulis Katherine