GPX6
- Known as:
- GPX6
- Catalog number:
- Y213576
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- GPX6
Related genes to: GPX6
- Gene:
- GPX6 NIH gene
- Name:
- glutathione peroxidase 6
- Previous symbol:
- GPXP3
- Synonyms:
- -
- Chromosome:
- 6p22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1994-11-23
- Date modifiied:
- 2015-09-11
- Gene:
- GPX7 NIH gene
- Name:
- glutathione peroxidase 7
- Previous symbol:
- -
- Synonyms:
- FLJ14777, GPX6, NPGPx
- Chromosome:
- 1p32.3
- Locus Type:
- gene with protein product
- Date approved:
- 1995-09-01
- Date modifiied:
- 2016-10-05
Related products to: GPX6
Related articles to: GPX6
- Glutathione peroxidases (GPXs) are key antioxidant enzymes that play a crucial role in maintaining cellular redox homeostasis and regulating cell fate across multiple organs. However, their involvement in tooth development remains unclear. In this study, we examined the expression patterns of GPX family members at various stages of mouse mandibular first molar development (E13.5, E14.5, E16.5, P0, P3, and P7) using qRT-PCR and immunohistochemical staining. GPX1, GPX2, GPX4, GPX7, and GPX8 were expressed with varying intensities in the dental epithelium and/or dental mesenchyme, while GPX3 was mainly detected in mesenchymal cells throughout all stages of tooth development. GPX5 and GPX6 were nearly undetectable. These findings indicate that GPX family members display distinct spatiotemporal expression patterns during tooth development. Notably, the sustained expression of GPX2, GPX4, and GPX8 in critical regions across multiple developmental stages suggests that these enzymes may be closely associated with the formation of dental tissues. - Source: PubMed
Publication date: 2026/02/20
Zhou KebingTian QingluZheng LiweiDu Wei - The study aimed to examine the hub genes and oxidative stress-related pathways in odontogenic keratocysts (OKCs) and predict transcription factors associated with the hub genes. - Source: PubMed
Publication date: 2025/06/10
Zhou HaoLi Rui-FangMan Qi-Wen - Extensive research efforts in the field of brain tumor studies have led to the reclassification of tumors by the World Health Organization (WHO) and the identification of various molecular subtypes, aimed at enhancing diagnosis and treatment strategies. However, the quest for biomarkers that can provide a deeper understanding of tumor development mechanisms, particularly in the case of gliomas, remains imperative due to their persistently incurable nature. Oxidative stress has been widely recognized as a key mechanism contributing to the formation and progression of malignant tumors, with imbalances in antioxidant defense systems being one of the underlying causes for the excess production of reactive oxygen species (ROS) implicated in tumor initiation. In this study, we investigated the gene expression patterns of the eight known isoforms of glutathione peroxidase (GPx) in brain tissue obtained from male and female control rats, as well as rats with transplacental ethyl nitrosourea (ENU)-induced brain tumors. Employing the delta-delta Ct method for RT-PCR, we observed minimal expression levels of , , , and in the brain tissue from the healthy control animals, while and exhibited moderate expression levels. Notably, and displayed the highest expression levels. Gender differences were not observed in the expression profiles of these isoforms in the control animals. Conversely, the tumor tissue exhibited elevated relative expression levels in all isoforms, except for , which remained unchanged, and , which exhibited alterations solely in female animals. Moreover, except for , which displayed no gender differences, the relative expression values of , , , , and were significantly higher in the male animals compared to their female counterparts. Hence, the analysis of glutathione peroxidase isoforms may serve as a valuable approach for discerning the behavior of brain tumors in clinical settings. - Source: PubMed
Publication date: 2023/08/24
Cueto-Ureña CristinaRamírez-Expósito María JesúsMayas María DoloresCarrera-González María PilarGodoy-Hurtado AliciaMartínez-Martos José Manuel - Maintaining the balance of a cell's redox function is key to determining cell fate. In the critical redox system of mammalian cells, glutathione peroxidase (GPX) is the most prominent family of proteins with a multifaceted function that affects almost all cellular processes. A total of eight members of the GPX family are currently found, namely GPX1-GPX8. They have long been used as antioxidant enzymes to play an important role in combating oxidative stress and maintaining redox balance. However, each member of the GPX family has a different mechanism of action and site of action in maintaining redox balance. GPX1-4 and GPX6 use selenocysteine as the active center to catalyze the reduction of HO or organic hydroperoxides to water or corresponding alcohols, thereby reducing their toxicity and maintaining redox balance. In addition to reducing HO and small molecule hydroperoxides, GPX4 is also capable of reducing complex lipid compounds. It is the only enzyme in the GPX family that directly reduces and destroys lipid hydroperoxides. The active sites of GPX5 and GPX7-GPX8 do not contain selenium cysteine (Secys), but instead, have cysteine residues (Cys) as their active sites. GPX5 is mainly expressed in epididymal tissue and plays a role in protecting sperm from oxidative stress. Both enzymes, GPX7 and GPX8, are located in the endoplasmic reticulum and are necessary enzymes involved in the oxidative folding of endoplasmic reticulum proteins, and GPX8 also plays an important role in the regulation of Ca in the endoplasmic reticulum. With an in-depth understanding of the role of the GPX family members in health and disease development, redox balance has become the functional core of GPX family, in order to further clarify the expression and regulatory mechanism of each member in the redox process, we reviewed GPX family members separately. - Source: PubMed
Publication date: 2023/03/02
Pei JunPan XingyuWei GuanghuiHua Yi - Mild impairment of mitochondrial function has been shown to increase lifespan in genetic model organisms including worms, flies and mice. To better understand the mechanisms involved, we analyzed RNA sequencing data and found that genes involved in the mitochondrial thioredoxin system, trx-2 and trxr-2, are specifically upregulated in long-lived mitochondrial mutants but not other non-mitochondrial, long-lived mutants. Upregulation of trx-2 and trxr-2 is mediated by activation of the mitochondrial unfolded protein response (mitoUPR). While we decided to focus on the genes of the mitochondrial thioredoxin system for this paper, we identified multiple other antioxidant genes that are upregulated by the mitoUPR in the long-lived mitochondrial mutants including sod-3, prdx-3, gpx-6, gpx-7, gpx-8 and glrx-5. In exploring the role of the mitochondrial thioredoxin system in the long-lived mitochondrial mutants, nuo-6 and isp-1, we found that disruption of either trx-2 or trxr-2 significantly decreases their long lifespan, but has no effect on wild-type lifespan, indicating that the mitochondrial thioredoxin system is specifically required for their longevity. In contrast, disruption of the cytoplasmic thioredoxin gene trx-1 decreases lifespan in nuo-6, isp-1 and wild-type worms, indicating a non-specific detrimental effect on longevity. Disruption of trx-2 or trxr-2 also decreases the enhanced resistance to stress in nuo-6 and isp-1 worms, indicating a role for the mitochondrial thioredoxin system in protecting against exogenous stressors. Overall, this work demonstrates an important role for the mitochondrial thioredoxin system in both stress resistance and lifespan resulting from mild impairment of mitochondrial function. - Source: PubMed
Publication date: 2022/05/13
Harris-Gauthier NamastheéTraa AnnikaAlOkda AbdelrahmanMoldakozhayev AlibekAnglas UlrichSoo Sonja KVan Raamsdonk Jeremy M