Ask about this productRelated genes to: PCBD1 antibody
- Gene:
- PCBD1 NIH gene
- Name:
- pterin-4 alpha-carbinolamine dehydratase 1
- Previous symbol:
- DCOH, PCBD
- Synonyms:
- PCD
- Chromosome:
- 10q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1993-06-08
- Date modifiied:
- 2016-10-05
Related products to: PCBD1 antibody
Related articles to: PCBD1 antibody
- The production of complex biologics in Chinese hamster ovary (CHO) cells is constrained by the lack of selection systems capable of coordinating multiple transgenes. Conventional single-marker systems have low saturable thresholds that limit enrichment efficiency, while multi-auxotrophic platforms often impose metabolic burdens. Here, we present a rationally designed tyrosine-auxotrophic system that overcomes these limitations by establishing a high-threshold cooperative selection mechanism. This is achieved through the reconstruction of an essential pathway comprising pterin-4α carbinolamine dehydratase 1 (PCBD1), phenylalanine hydroxylase (PAH), and quinoid dihydropteridine reductase (QDPR). We generated a triple-knockout CHO host via CRISPR/Cas9, wherein survival under tyrosine deprivation became strictly dependent on the balanced co-expression of all three rescue genes. This architecture creates a selection pressure that is not saturable by any single gene, enabling efficient co-enrichment. Applied to monoclonal antibody (mAb) production, the system enriched triple-positive populations to 97.49%, resulting in significantly enhanced homogeneity and coordinated upregulation of antibody chain expression. Optimized pools achieved titers of 0.35 g/L in fed-batch and 1.60 g/L in perfusion cultures without tyrosine feeding. Consequently, pathway reconstitution rewired central metabolism, reducing byproducts and enhancing biosynthesis. This antibiotic-free multi-marker platform establishes a new paradigm for stringent multigene co-expression, advancing CHO cell engineering for next-generation biologics. - Source: PubMed
Publication date: 2026/03/09
Cao LeiNa DaoyuanCheng JunZhao LiangYe QianTan Wen-Song - Understanding the role of plasma proteins in the pathophysiology of epilepsy is crucial for uncovering novel biological mechanisms and therapeutic targets. Mendelian randomization (MR) provides a valuable tool for dissecting potentially causal associations between circulating proteins and disease risk. This study aimed to systematically assess potential causal relationships between the plasma proteome and epilepsy. - Source: PubMed
Publication date: 2025/10/30
Fu JingfengWu WeiShen Shangren - CHO cells dominate monoclonal antibody (mAb) production in fed-batch biomanufacturing, where tyrosine supply is limited by low solubility in neutral media and the complexities of alkaline tyrosine feeds. Existing studies confirm overexpressing pterin-4α-carbinolamine dehydratase 1 (PCBD1) and phenylalanine hydroxylase (PAH) restores tyrosine prototrophy and matches non-engineered cells' production in tyrosine-supplemented cultures. However, these studies focus on enzyme regulation without resolving feeding-phase supply challenges in high-density scenarios. To address this, this study verified that recombinant CHO (rCHO) cells rely strongly on exogenous tyrosine for growth and production. Multi-level expression analysis further confirmed low PCBD1/PAH levels restrict endogenous tyrosine synthesis, and identified quinoid dihydropteridine reductase (QDPR)-a key tetrahydrobiopterin (BH4) regeneration enzyme-as a previously unrecognized bottleneck, particularly in tyrosine-limited conditions. By co-overexpressing QDPR in high PCBD1/PAHexpressing cells to remodel the tyrosine biosynthesis pathway, a novel fed-batch strategy was established: basal medium with 3.0 mM tyrosine and tyrosine-free singlefeeding medium. Results showed this strategy, effective in high-density fed-batch settings, enabled rCHO cells to reach a final mAb titer of 4.24 g/L, representing a 32.50% increase compared to cells overexpressing only PCBD1 and PAH, and a 10.70 % increase compared to the conventional strategy. In summary, the strategy offers a simplified nutrient alternative by eliminating alkaline tyrosine feeds, highlighting holistic metabolic pathway optimization's importance in biomanufacturing and targeted value for high-density, tyrosine-limited CHO cell-based mAb production. - Source: PubMed
Publication date: 2025/10/10
Cao LeiZhao LiangYe QianTan Wen-Song - To investigate the targets and mechanisms of 7-hydroxyethyl chrysin (7-HEC) in prevention and treatment of high-altitude cerebral edema (HACE) in rats. - Source: PubMed
Zhang DongmeiLi XiaolinYang ChenyuJing LinlinHe LeiMa Huiping - Diabetic nephropathy (DN) is a common diabetes-related complication with unclear underlying pathological mechanisms. Although recent studies have linked glycolysis to various pathological states, its role in DN remains largely underexplored. - Source: PubMed
Publication date: 2025/01/21
Fan ChenglongYang GuanglinLi ChengCheng JiwenChen ShaohuaMi Hua