Ask about this productRelated genes to: PRDX6 Blocking Peptide
- Gene:
- PRDX5 NIH gene
- Name:
- peroxiredoxin 5
- Previous symbol:
- -
- Synonyms:
- ACR1, AOEB166, MGC142285, PRXV, PMP20, B166, PRDX6, PLP, SBBI10, MGC117264, MGC142283
- Chromosome:
- 11q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-07-31
- Date modifiied:
- 2016-10-05
- Gene:
- PRDX6 NIH gene
- Name:
- peroxiredoxin 6
- Previous symbol:
- -
- Synonyms:
- AOP2, KIAA0106, 1-Cys, NSGPx, PRX, aiPLA2, MGC46173, p29
- Chromosome:
- 1q25.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-04-03
- Date modifiied:
- 2016-10-05
Related products to: PRDX6 Blocking Peptide
Related articles to: PRDX6 Blocking Peptide
- Breast cancer is the most frequently diagnosed malignancy among women worldwide. Trace elements, such as selenium, play a crucial role in antioxidation and have gained interest in cancer research. This study aimed to assess the association between prediagnostic serum trace element concentrations and breast cancer risk, as well as their relationship with the expression of key antioxidant enzymes in leukocytes of ER-positive breast cancer patients. - Source: PubMed
Publication date: 2025/09/13
Argente Del Castillo PaulaMorla-Barcelo Pere MiquelMartinez-Bernabe ToniSánchez Asís SaraDelgado Rodríguez Jose AntonioNadal-Serrano MercedesLlompart Alabern IsabelRoca PilarCordoba OctaviSastre-Serra JorgeBauça Josep Miquel - Our study mainly focused on exploring the expression and mechanism of PRDXs family members in OSCC, as well as the diagnostic and prognostic monitoring value of PRDXs family members in OSCC. - Source: PubMed
Publication date: 2025/03/28
Zhang ZhouZheng QuanLi PingXu XiaopengZhou YanzhouQian Chen - Cryopreservation of bull sperm, crucial for breeding and assisted reproduction, often reduces sperm quality due to oxidative stress. This study examines how oxidative stress during cryopreservation affects peroxiredoxin 5 (PRDX5) and peroxiredoxin 6 (PRDX6) proteins, leading to their translocation and oligomerization in bull sperm. Increased reactive oxygen species (ROS) and nitric oxide (NO) levels were linked to reduced mitochondrial potential, higher DNA fragmentation, and increased membrane fluidity, prompting PRDX5 to move intracellularly and PRDX6 to the cell membrane. Under cryopreservation, these proteins formed high molecular weight oligomers, that may shift from peroxidase to chaperone roles. Their interaction with Toll-like receptor 4 (TLR4) may be key to their intracellular transport. On the other hand, the presence of PRDX5 and PRDX6 in exosomal vesicles suggested a potential mechanism for their transport into sperm cells. Using Imaging Flow Cytometry and various PAGE techniques, the study detected PRDX5 and PRDX6 in different sperm locations and analyzed their oligomer formation. These findings highlight the adaptive roles of PRDX5 and PRDX6 in protecting sperm cells, offering insights that could improve cryopreservation protocols in animal breeding and human reproductive medicine, and advance our understanding of the oxidative stress response in sperm cells. - Source: PubMed
Publication date: 2025/01/09
Agnieszka Mostek-MajewskaMagdalena Bossowska-NowickaMariola SłowińskaAndrzej Ciereszko - Non-alcoholic fatty liver disease or steatosis is an accumulation of fat in the liver. Increased amounts of non-esterified fatty acids, calcium deficiency, or insulin resistance may disturb endoplasmic reticulum (ER) homeostasis, which leads to the abnormal accumulation of misfolded proteins, activating the unfolded protein response. The ER is the primary location site for chaperones like thioredoxin domain-containing 5 (TXNDC5). Glutathione participates in cellular oxidative stress, and its interaction with TXNDC5 in the ER may decrease the disulfide bonds of this protein. In addition, glutathione is utilized by glutathione peroxidases to inactivate oxidized lipids. To characterize proteins interacting with TXNDC5, immunoprecipitation and liquid chromatography-mass spectrometry were used. Lipid peroxidation, reduced glutathione, inducible phospholipase A (iPLA) and hepatic transcriptome were assessed in the AML12 and TXNDC5-deficient AML12 cell lines. The results showed that HSPA9 and PRDX6 interact with TXNDC5 in AML12 cells. In addition, TXNDC5 deficiency reduced the protein levels of PRDX6 and HSPA9 in AML12. Moreover, lipid peroxidation, glutathione and iPLA activities were significantly decreased in TXNDC5-deficient cells, and to find the cause of the PRDX6 protein reduction, proteasome suppression revealed no considerable effect on it. Finally, hepatic transcripts connected to PRDX6 and HSPA9 indicated an increase in the , and and a decrease in , , , , , , , , and mRNA levels in AML12 KO cells. In conclusion, the lipid peroxidation system and glutathione mechanism in AML12 cells may be disrupted by the absence of TXNDC5, a novel protein-protein interacting partner of PRDX6 and HSPA9. - Source: PubMed
Publication date: 2023/12/05
Bidooki Seyed HesamoddinSánchez-Marco JavierMartínez-Beamonte RobertoHerrero-Continente TaniaNavarro María ARodríguez-Yoldi María JOsada Jesús - Gliomas are a histologically and molecularly heterogeneous group of neoplasms accounting for 80% of malignant primary brain tumors. Growing evidence suggests that production of reactive oxygen species (ROS) is linked to glioma pathogenesis, although it is still unclear whether it is a cause or an effect of this process. Peroxiredoxins (PRDXs), a family of six antioxidant proteins, may promote or inhibit carcinogenesis, depending on the tumor type and stage. The current knowledge on their expression, regulation and functions in glioma is scarce. In this study, a comprehensive analysis of PRDXs expression in distinct glioma subtypes and non-tumor brain tissues was conducted using gene expression data from The Cancer Genome Atlas (TCGA), REpository for Molecular BRAin NeoplasiaDaTa (REMBRANDT), The Chinese Glioma Atlas (CGGA) and Gene Expression Omnibus (GEO) datasets. The association between gene expression and patient survival was investigated. DNA methylation, mutations, copy number alterations of deregulated PRDXs as well as the correlation between gene expression and tumor-infiltrating immune cells were assessed. The analysis revealed overexpression of PRDX1, PRDX4, and PRDX6 in most histological glioma types compared to the non-tumor tissues, while PRDX2, PRDX3 and PRDX5 expression remained unaltered. The expression of PRDX4 and PRDX6 was higher in mesenchymal than proneural and classical glioma subtypes. Moreover, lower expression of PRDX1, PRDX4 and PRDX6 was observed in tumors with a glioma CpG island methylator phenotype (G-CIMP) compared to non-G-CIMP tumors, as well as in isocitrate dehydrogenase (IDH) mutant and 1p/19q co-deleted gliomas compared to the wild-type counterparts. High expression of PRDX1, PRDX4 or PRDX6 correlated with poor survival of glioma patients. PRDX1 and PRDX6 displayed a positive correlation with different immune cell population in low grade gliomas and, to a lesser extent, in glioblastoma. PRDX1 expression exhibited negative correlation with DNA methylation. These results indicate that high expression of PRDX1, PRDX4 and PRDX6 is associated with poor outcome in gliomas. - Source: PubMed
Publication date: 2021/12/28
Szeliga Monika