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
- To investigate the role of peroxiredoxin isoforms (Prdx) in the radioresistance of cancer cells, the expression of Prdx1-6, DNA repair genes, and apoptosis regulators was studied in human cancer cell lines with varying radiosensitivities (A549, Caco-2, and MCF-7) after exposure to ionizing radiation. A correlation was found between high constitutive Prdx1-6 expression levels and increased radioresistance. Predominantly cytosolic isoforms Prdx2 and Prdx6 demonstrated pronounced induction after irradiation, indicating their critical role in protecting against radiation-induced oxidative stress. Most radiosensitive A549 cells exhibited the lowest baseline Prdx expression and the most pronounced transcriptional changes after irradiation, whereas MCF-7 and Caco-2 cells had higher constitutive expression and a weaker response to radiation. Mitochondrial Prdx3 and Prdx5, as well as ER-localized Prdx4, exhibited relatively stable expression. A549 cells demonstrated the highest induction of DNA repair genes, which may indicate more severe DNA damage. In contrast, MCF-7 cells were characterized by high basal expression of repair genes and elevated γH2AX levels before irradiation, which may reflect their "readiness" for repair and explain their higher radioresistance. Furthermore, radioresistant MCF-7 cells had increased expression of anti-apoptotic genes (BCL2, MCL1, BIRC5), suppressing the mitochondrial apoptotic pathway. Meanwhile, A549 cells showed higher induction of pro-apoptotic genes (PUMA, NOXA, BAK1) and activation of caspase-3, which correlates with their increased radiosensitivity. Therefore, peroxiredoxins protect cells from radiation exposure, either by being constitutively expressed or by being highly inducible in response to radiation, and promote cell survival after irradiation. This makes them attractive targets for overcoming cancer cell radioresistance. - Source: PubMed
Publication date: 2026/05/27
Sharapov M GGoncharov R GKarmanova E EParfenyuk S BGlushkova O VLunin S M - 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