MTCH1 antibody
- Known as:
- MTCH1 (anti-)
- Catalog number:
- orb100030
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- MTCH1 antibody
Related genes to: MTCH1 antibody
- Gene:
- MTCH1 NIH gene
- Name:
- mitochondrial carrier 1
- Previous symbol:
- -
- Synonyms:
- CGI-64, PSAP, SLC25A49
- Chromosome:
- 6p21.2
- Locus Type:
- gene with protein product
- Date approved:
- 2003-05-20
- Date modifiied:
- 2014-11-19
Related products to: MTCH1 antibody
Related articles to: MTCH1 antibody
- Ischemic heart failure (IHF) is a major cause of cardiovascular morbidity worldwide, characterized by complex tissue remodeling and inflammation. However, reliable molecular biomarkers for early diagnosis and a systematic understanding of the associated immune-stromal microenvironment remain limited. Identifying specific transcriptomic signatures may enhance diagnostic precision and reveal novel therapeutic targets. - Source: PubMed
Publication date: 2026/03/31
Sun YangChang YuFeng YezhiSong BinghuiZhou Yanan - : The exact pathogenesis of Alzheimer's disease (AD), a neurodegenerative disorder, remains unclear. Ferroptosis is a form of cell death characterized by intracellular iron accumulation, and has emerged as a potential contributor to the pathological cascade of AD. Therefore, this study aims to identify core genes that may function as reliable biomarkers for AD through an in-depth analysis of the genetic relationship between ferroptosis-related genes and AD. : This study first obtained the gene expression profiles (GSE140831, GSE63060 and GSE63061 expression profiles). The GSE140831 dataset served as the discovery cohort, and the GSE63060 and GSE63061 datasets were used as independent validation cohorts. R language 4.4.1 was used for standardizing and identifying differentially expressed genes (DEGs) in AD patients in all datasets. Secondly, the ferroptosis-related genes were obtained. By integrating the ferroptosis-related genes, ferroptosis-related DEGs (FRDEGs) were detected. Then, the FRDEGs were verified and evaluated, and the biological functions of the core genes were analyzed. Finally, miRNAs interacting with these core FRDEGs were explored. : The study identified nine FRDEGs (ACVR1B, BRPF1, G6PD, KLHDC3, LAMP2, MTCH1, P4HB, PTPN6, RBMS1), which are potentially related and may serve as biomarkers for AD. All nine genes demonstrated statistically significant differential expression (up-regulation) in both independent validation cohorts and in the combined analysis ( < 0.05). Although the area under the curve (AUC) values of these nine genes ranged from 0.61 to 0.71, indicating moderate discriminatory power, these findings suggest that they may be involved in pathways related to AD and are worthy of further investigation as potential auxiliary biomarkers. Finally, a network of hub FRDEGs-miRNAs interaction was constructed. There were 11 miRNAs that may regulate these hub FRDEGs simultaneously. : This study showed the significant association of the identified FRDEGs with AD. Also, a core ferroptosis-related biomarker network for miRNAs regulation of AD was constructed. The specific regulatory mechanism is worthy of further investigation. - Source: PubMed
Publication date: 2026/02/11
Liu WenjiaRao XinYu Liyang - Mitochondrial function relies heavily on the proper targeting and insertion of nuclear-encoded proteins into the outer mitochondrial membrane (OMM), a process mediated by specialised biogenesis factors known as insertases. These insertases are essential for the membrane integration of α-helical OMM proteins, which contain one or multiple hydrophobic transmembrane segments. While the general mechanisms of mitochondrial protein import are well established, recent research has shed light on the diversity and evolutionary conservation of OMM insertases across eukaryotic lineages. In , the mitochondrial import (MIM) complex, composed of Mim1 and Mim2, facilitates the integration of various α-helical OMM proteins, often in cooperation with import receptors such as Tom20 and Tom70. In , the functional MIM counterpart pATOM36 performs a similar role despite lacking sequence and structural homology, reflecting a case of convergent evolution. In mammals, MTCH2 has emerged as the principal OMM insertase, with MTCH1 playing a secondary, partially redundant role. This review provides a comparative analysis of these insertases, emphasising their conserved functionality, species-specific adaptations, and mechanistic nuances. - Source: PubMed
Publication date: 2025/08/11
Dimogkioka Anna RozaRapaport Doron - Prostate cancer is a heterogeneous malignancy with a complex tumor microenvironment (TME) composed of various cellular components, including fibroblasts. These fibroblasts, particularly cancer-associated fibroblasts (CAFs), are crucial in shaping the TME and influencing cancer progression. Catechol-O-methyltransferase (COMT), a key enzyme involved in the metabolism of catecholamines and oxidative stress regulation, has recently been implicated in cancer biology. This study aims to explore the molecular landscape of fibroblasts in prostate cancer and evaluate the prognostic significance of COMT expression in this context. We performed an integrated single-cell RNA sequencing (scRNA-seq) analysis on prostate cancer samples from Gene Expression Omnibus (GEO) databases. Fibroblast subpopulations were identified through clustering, and functional gene signatures for each subgroup were characterized. Prognostic analysis was carried out using univariate and multivariate Cox regression to identify genes associated with patient survival, culminating in a risk score model using data from the Cancer Genome Atlas (TCGA). Additionally, immunofluorescence assays were used to validate COMT expression in tumor-derived fibroblasts. Our single-cell sequencing analysis revealed three distinct fibroblast subpopulations, each with unique gene expression profiles linked to extracellular matrix remodeling, immune modulation, and cellular stress responses. COMT was identified as a key gene in tumor-derived fibroblasts, with its expression significantly higher in tumor samples compared to normal tissues. The risk score model, based on COMT and other fibroblast-associated genes (QSOX1, TAX1BP3, CCDC66, MTCH1, ARL2BP), successfully stratified patients into high-risk and low-risk groups, with higher risk scores correlating with poorer survival outcomes. Immunostaining confirmed the overexpression of COMT in tumor-derived fibroblasts, consistent with bioinformatics analysis. This study underscores the significant role of fibroblasts, particularly CAFs, in prostate cancer progression. Our findings highlight COMT as a critical regulator of the tumor microenvironment and a promising prognostic marker. The integration of single-cell RNA-seq with clinical data offers new insights into fibroblast heterogeneity and the potential for COMT as a therapeutic target in prostate cancer. Further research is needed to validate these findings and explore the mechanistic role of COMT in prostate cancer progression and therapeutic resistance. - Source: PubMed
Publication date: 2025/07/28
Shan WeiminGuan BoMa WeiweiFan RunzheCui DiHao Zongyao - The outer mitochondrial membrane (OMM) hosts a variety of proteins such as import machineries, enzymes, fission and fusion factors, and pore proteins. In Saccharomyces cerevisiae, the MIM complex, consisting of Mim1 and Mim2, mediates the insertion of α-helical proteins into the OMM. Until recently, it was unclear which proteins served this function in higher eukaryotes. Recent studies have identified MTCH2 as the insertase responsible for inserting α-helical proteins into the OMM in mammals. MTCH1 is a paralogue of MTCH2 but its general function and contribution to the biogenesis process are not clear. To better characterize MTCH1, we explored whether MTCH1 or MTCH2 could functionally replace Mim1 and/or Mim2 in yeast. Expression of MTCH1 and MTCH2 in yeast cells lacking Mim1, Mim2 or both revealed that MTCH1, but not MTCH2, could compensate for the growth defects upon deleting the MIM complex. Furthermore, MTCH1 could restore the biogenesis of MIM substrates, translocase of the outer membrane (TOM) complex stability and morphology of mitochondria. These findings indicate that MTCH1, by itself, has insertase activity and is a functional equivalent for the MIM complex, despite the absence of any evolutionary relation between the mammalian and yeast insertases. - Source: PubMed
Publication date: 2025/08/15
Dimogkioka Anna RozaElias AnniRapaport Doron