Ask about this productRelated genes to: BDH2 antibody
- Gene:
- BDH2 NIH gene
- Name:
- 3-hydroxybutyrate dehydrogenase 2
- Previous symbol:
- DHRS6
- Synonyms:
- UCPA-OR, FLJ13261, UNQ6308, PRO20933, SDR15C1
- Chromosome:
- 4q24
- Locus Type:
- gene with protein product
- Date approved:
- 2005-11-22
- Date modifiied:
- 2016-12-12
Related products to: BDH2 antibody
Related articles to: BDH2 antibody
- Cells possess intricate metabolic networks comprised of hundreds of enzymes. Despite extensive research, many of these enzymes remain uncharacterized. Identifying the function of these enzymes is crucial for advancing our understanding of cellular metabolism. However, multiple enzymes are not active in standard conditions, making them challenging to study. To overcome this challenge, we created a pipeline to track the upregulation of enzymes at the protein level during diverse growth conditions, suggesting a requirement for their activity in these conditions. To do this, we assembled a collection of ∼180 of yeast strains, each containing an uncharacterized putative enzyme fused to a fluorophore and under the regulation of its own promoter. By subjecting the collection to 42 diverse environments, we identified the biologically relevant conditions for the upregulation of 16 proteins. We focused on one such putative alcohol dehydrogenase, Bdh2, whose expression was upregulated during nutrient-limited conditions, and functionally characterized it. More broadly, our discovery pipeline lays the foundation for uncovering new stress-induced enzymes. This has implications in the cell biology of metabolism and biotechnology. - Source: PubMed
Publication date: 2026/05/07
Edilbi DunyaValenti RosarioDubreuil BenjaminAsraf YeynitPeleg YoavAlbeck ShiraMalitsky SergeyItkin MaximSchuldiner Maya - To investigate the role of 3-hydroxybutyrate dehydrogenase 2 (BDH2) in regulating ferroptosis and its impact on the metastasis of lung adenocarcinoma (LUAD). Expression levels of BDH2 were modulated in LUAD cell lines (A549, PC9) using pcDNA-BDH2 plasmid transfection. Cell motility was assessed by Transwell assays, while ferroptosis-associated markers, including Fe, malondialdehyde (MDA), lipid reactive oxygen species (ROS), ACSL4, and GPX4, were evaluated by biochemical assays, flow cytometry, and Western blotting. The involvement of the Nrf2/HO-1 signaling axis was analyzed by Western blotting and RT-qPCR. Furthermore, a xenograft mouse model was established to confirm the effect of BDH2 on tumor progression and metastasis . Overexpression of BDH2 significantly inhibited LUAD cell migration and invasion. BDH2 upregulation enhanced ferroptosis, effects that were reversed by the ferroptosis inhibitor Fer-1. Mechanistically, BDH2 suppressed the activation of the Nrf2/HO-1 pathway, thereby enhancing sensitivity to ferroptosis. , BDH2 overexpression markedly reduced tumor growth and metastasis in nude mice, while inhibition of ferroptosis attenuated these effects. BDH2 suppresses metastasis in LAUD by promoting ferroptosis via suppression of the Nrf2/HO-1 pathway, highlighting BDH2 as a potential therapeutic target for LUAD. - Source: PubMed
Publication date: 2026/04/09
Yang QiaoTian LinChen XiaodongMei XiongNie YongliChen Jun - Iron sustains cancer cell plasticity, yet it also sensitizes the mesenchymal, drug-tolerant phenotype to ferroptosis. This posits that iron compartmentalization must be tightly regulated. However, the molecular machinery governing organelle Fe(II) compartmentalization remains elusive. Here, we show that BDH2 is a key effector of inter-organelle Fe(II) redistribution and ferroptosis vulnerability during melanoma transition from a melanocytic (MEL) to a mesenchymal-like (MES) phenotype. In MEL cells, BDH2 localizes at the mitochondria-lysosome contacts (MLCs) to generate the siderophore 2,5-dihydroxybenzoic acid (2,5-DHBA), which ferries iron into the mitochondria. Fe(II) transfer by BDH2 supports mitochondrial bioenergetics, which is required to maintain lysosomal acidification and MLC formation. Loss of BDH2 alters lysosomal pH and MLC tethering dynamics, causing lysosomal iron sequestration, which primes MES cells for ferroptosis. Rescuing BDH2 expression, or supplementing 2,5-DHBA, rectifies lysosomal pH and MLCs, protecting MES cells from ferroptosis and enhancing their ability to metastasize. Thus, we unveil a BDH2-dependent mechanism that orchestrates inter-organelle Fe(II) transfer, linking metabolic regulation of lysosomal pH to the ferroptosis vulnerability of the mesenchymal, drug-tolerant cancer cells. - Source: PubMed
Publication date: 2025/09/16
Rizzollo FrancescaEscamilla-Ayala AbrilFattorelli NicolaLysiak Natalia BarbaraMore SanketHernández Varas PabloBarazzuol LuciaVan den Haute ChrisVan Asselberghs JorisNittner DavidCoene JonathanVenkataramani VivekMichalke BernhardGaillet ChristineCañeque TatianaDavidson IrwinVerhelst Steven H LVangheluwe PeterCalì TitoMarine Jean-ChristopheRodriguez RaphaëlBonnereau JulieAgostinis Patrizia - 5-Fluorouracil (5-FU) is an effective drug in the treatment of colorectal cancer (CRC); however, the development of acquired resistance to 5-FU poses a great challenge in clinical practice. Through the analysis of public datasets, we found that reduced 3-Hydroxybutyrate Dehydrogenase 2 (BDH2) expression in CRC tissues predicted poor survival in CRC patients. Low expression of BDH2 in clinical CRC tissue samples predicted a higher degree of malignancy. In addition, public dataset analysis showed that GLI Pathogenesis Related 1 (GLIPR1) expression was elevated in CRC patients following 5-FU treatment, contrasting with the expression pattern of BDH2. We reported that in 5-FU-resistant CRC cell lines (LOVO/5-FU and HCT15/5-FU), BDH2 was downregulated, while the expression of GLIPR1 was increased. To explore the regulatory relationship between BDH2 and GLIPR1 in 5-FU resistance, BDH2 and GLIPR1 overexpression plasmid vectors were constructed to transfect 5-FU resistant CRC cell lines. BDH2 led to enhanced 5-FU sensitivity in 5-FU-resistant CRC cell lines and inhibited the malignant behavior of CRC-resistant cells in vitro. In nude mice with subcutaneous tumors and intraperitoneal injections of 5-FU, tumor tissues formed by BDH2-overexpressing cells exhibited slower growth and increased apoptosis. Mechanistically, the upregulation of BDH2 increases GLIPR1 promoter methylation, mediated by DNA methyltransferases, thereby inhibiting GLIPR1 expression. High expression of GLIPR1 reduces 5-FU sensitivity in 5-FU-resistant CRC cell lines, which abolished the impact of BDH2 expression. These results suggest that BDH2 inhibits GLIPR1 expression by increasing GLIPR1 promoter methylation, thereby enhancing 5-FU sensitivity of 5-FU-resistant CRC cell lines and inhibiting CRC progression. - Source: PubMed
Publication date: 2025/07/12
Lu DapengMa LinZhang QingyueXing ChengzhongLi Yanke - This study aimed to identify potential susceptibility loci for testicular germ cell tumors (TGCT) through a comprehensive multi-omics analysis. - Source: PubMed
Publication date: 2025/06/03
Xu YuangaoShi HuaXiong JieyuWu YikunWu XiaoyuXu YuanboWang YuanlinXu Shuxiong