Ask about this productRelated genes to: PDIA6 antibody
- Gene:
- PDIA6 NIH gene
- Name:
- protein disulfide isomerase family A member 6
- Previous symbol:
- TXNDC7
- Synonyms:
- P5, ERp5
- Chromosome:
- 2p25.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-03-11
- Date modifiied:
- 2015-11-16
Related products to: PDIA6 antibody
Related articles to: PDIA6 antibody
- Heat stress causes severe oxidative damage and immune cell death in marine bivalves, but its upstream regulators remain unclear. This study identified regulators linking heat stress to oxidative damage in Pacific oyster haemocytes. Under 30 °C exposure, the apoptosis rate of oyster haemocytes increased from ~4.54% to 17.40% at 24 h, accompanied by elevated ROS, malondialdehyde, and lipid hydroperoxide and reduced SOD activity. GSEA and protein interaction analysis of the haemocyte transcriptome pinpointed protein disulfide isomerase A6 (PDIA6) as the hub gene linking endoplasmic reticulum stress, apoptosis, and oxidative stress. Single-cell in silico knockout placed at the head of a coupled SOD-peroxiredoxin relay (SOD1, SOD2, PRDX6) and shifted haemocytes toward a stress-activated state. This prediction was confirmed by RNAi knockdown, in which silencing aggravated heat-induced oxidative injury, reduced the expression of antioxidant-related genes (, , and ), and further suppressed SOD activity. Molecular dynamics simulations showed that heat destabilized its catalytic thioredoxin domains, compromising its protective function. These results demonstrate that PDIA6 protects haemocytes against heat-induced oxidative damage by sustaining antioxidant enzyme activity, providing insights into redox regulation and heat adaptation in mollusks. - Source: PubMed
Publication date: 2026/08/01
Sun PengchengLi MingLi PengMa YangGao LeiZhang XueshuWang LinglingSong Linsheng - Type I collagen is the most abundant form of collagen and forms the organic component of bone. Pathogenic variants in genes encoding its constituent polypeptide chains, and , can result in autosomal dominant osteogenesis imperfecta and other connective tissue disorders. Although osteogenesis imperfecta is clinically well-described, the molecular basis of clinical heterogeneity among patients is not well understood. We undertook a global proteomic approach to uncover alterations in osteogenesis imperfecta patient bone-derived stromal cells as well as their secretome. We performed multiplexed tandem mass tag (TMT)-based proteomics analysis of cells from three patients along with three controls to investigate global changes in the proteome of these cells as well as their secretome. This was combined with analysis of proline hydroxylation to catalog the modification of type I collagens in this disorder. We observed significant changes in both the cellular and secreted proteomes including the levels of proteins involved in osteoblast proliferation such as nitric oxide synthase-interacting protein (NOSIP), secreted frizzled-related protein 1 (SRFP1) and transforming growth factor beta-1-induced transcript 1 protein (TGFB1I1) as well as others involved in endoplasmic reticulum homeostasis such as protein disulfide isomerase A6 (PDIA6) and reticulophagy regulator 3 (RETREG3). Notably, a number of alterations were observed in proline hydroxylation in intracellular collagens - COL1A1 and COL1A2. These findings expand our current understanding of the cellular pathophysiology in osteogenesis imperfecta and could lead to the identification of novel therapeutic targets. - Source: PubMed
Publication date: 2026/07/22
Garapati KishoreMun Dong-GiDevasahayam Arokia Balaya RexSaraswat MayankRenuse SantoshTrahan GregoryKandasamy Richard KDeyle David RPandey Akhilesh - The continuously rising incidence and persistently high mortality of hepatocellular carcinoma (HCC) have created an urgent need for a deeper understanding of the molecular mechanisms underlying this disease. In the present study, leveraging multiple HCC transcriptome databases, we employed expression analysis, correlation analysis, Gene Set Variation Analysis (GSVA), and cox regression analysis to identify that aberrant upregulation of PDIA6 represents a promising prognostic biomarker associated with adverse clinical outcomes in HCC. Using a series of in vitro oncology research approaches, as well as nude mouse models of subcutaneous tumor formation and lung metastasis, we experimentally validated that PDIA6 promotes the proliferation and metastasis of HCC cells. Through transcriptome sequencing analysis and subsequent rescue experiments, we further confirmed that PDIA6 enhances HCC cell proliferation and migration by activating the Wnt signaling pathway. Combined analysis via immunoprecipitation-mass spectrometry and proteomics revealed that PDIA6 significantly downregulates the expression of the tumor suppressor gene AKAP12. Subsequent rescue experiments demonstrated that PDIA6 drives HCC progression in a manner dependent on the reduced expression of AKAP12. Utilizing protein half-life assays, ubiquitination assays, and co-IP experiments, we uncovered the underlying mechanism: PDIA6 competitively binds to the UCH domain of USP24, which impairs the deubiquitinating activity of USP24 towards AKAP12. This ultimately leads to enhanced K48-linked ubiquitination of AKAP12 and its subsequent proteasomal degradation. We further verified, using specific activators, that AKAP12 inhibits the Wnt signaling pathway in a PKA-dependent manner. In vivo, targeted inhibition of PDIA6 exhibited a more potent therapeutic effect on Wnt-positive HCC tumors.Conclusion Collectively, our study demonstrates the HCC-promoting mechanism of the PDIA6-AKAP12-Wnt signaling axis and highlights its great potential for the development of therapeutic targets in HCC. - Source: PubMed
Publication date: 2026/07/09
Yao RuchengYin YuhanLi XiaosongYang XinyuHe WenzhiYuan YufengHu Jun - Silver pomfret (), a highly valued marine fish, faces challenges in aquaculture due to its sensitivity to environmental conditions. Recirculating aquaculture system (RAS) is likely to become a primary indoor cultivation method for silver pomfret in the future, so studying hydrodynamic characteristics at varying flow rates in silver pomfret RAS is crucial and has far-reaching implications for both aquaculture practices and economic returns. This study investigated the effects of water flow rates (low: 400 L/h, moderate: 600 L/h, high: 800 L/h) on the growth performance, nutritional metabolism, and gut microbiota of silver pomfret over an 8-week period. Transcriptome and 16S rRNA sequencing revealed that the moderate-flow-rate group exhibited superior growth performance, with enhanced expression of genes related to protein synthesis (HYOU1, PDIA6, ITGA11) and redox regulation (GLUL, DUSP1, GST). Additionally, the moderate flow rate promoted gut microbial diversity and stability, with higher abundances of fermentation- and chemoheterotrophy-related functions, suggesting improved nutrient metabolism. In contrast, high flow rates induced anaerobic metabolism, leading to lactate accumulation and reduced growth. These findings demonstrate that a moderate flow rate of 600 L/h optimizes silver pomfret aquaculture by enhancing growth, metabolic efficiency, and microbial health, providing a foundation for sustainable large-scale farming practices. - Source: PubMed
Publication date: 2026/06/12
Hu JiabaoLi YuanboZhang YouyiZheng RongyueYan XiaojunZhang ManWang YajunJia Lingling - Protein-protein interactions (PPIs) are dynamic and critical to adaptive homeostasis. While there have been massive efforts to catalogue proteome-wide PPIs, global quantification of changes remains a challenge. Here, we integrate dynamic protein correlation profiling - mass spectrometry (PCP-MS) and quantitative cross linking-mass spectrometry (qXL-MS) using multiplexed stable isotope labelling to characterise global PPI remodelling following the development of chronic skeletal muscle insulin resistance (IR) with or without acute insulin stimulation. We quantify >7,000 unique PPIs amongst 5,346 proteins and show changes in the interactome network dominate the proteome response. Our data show the dysregulation of protein processing in the endoplasmic/sarcoplasmic reticulum involving changes in PPIs with protein chaperones and disulfide isomerases is a major hallmark of skeletal muscle IR. Mechanistically, we show the dysregulation of PPIs with Protein-Disulfide Isomerase 6 (PDIA6) regulates cysteine oxidation and insulin sensitivity. Taken together, we show in vivo quantitative interactome mapping is a powerful approach to understand disease mechanisms and provide new insights into protein network re-organisations with IR. - Source: PubMed
Publication date: 2026/06/23
Ng Yaan-KitBlazev RonnieWong Julian P HScott Nichollas EMolendijk JeffreyParker Benjamin L