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
- Many age-related neurodegenerative disorders are marked by progressive defects in cellular energy metabolism and protein homeostasis that converge on mitochondrial and lysosomal dysfunction. TLDc domain-containing proteins, such as OXR1, NCOA7, and related family members, have emerged as crucial modulators of organellar physiology and cellular stress responses. Growing evidence indicates that TLDc proteins physically interact with vacuolar ATPases (V-ATPases) to modulate their assembly and catalytic activity, linking TLDc function directly to the maintenance of lysosomal and Golgi lumen pH. This organellar pH homeostasis, in turn, is fundamental to intracellular iron handling and metabolic regulation, processes essential for mitochondrial bioenergetics, lysosomal functions, and cellular viability. Lysosomes maintain an acidic lumen via V-ATPase proton pumping, counterbalanced by specific ion channels, including TMEM175. This acidic environment is required for ferric iron reduction and subsequent release into the cytosol; when acidification fails, cells develop cytosolic iron deficiency, mitochondrial defects, pseudohypoxia via HIF-1α activation, and inflammation. Conversely, iron flux from lysosomes to mitochondria depends on acidic conditions and direct organelle contact, as exemplified by BDH2-driven siderophore transport, a V-ATPase-dependent but not TLDc-regulated process, which supports mitochondrial bioenergetics and sustains lysosomal acidity. Iron and pH dysregulation synergize to drive ferroptosis, lipid peroxidation, and neurotoxicity. Emerging studies link lysosomal deacidification and iron dyshomeostasis to the pathogenesis of major neurodegenerative diseases. These mechanisms collectively shape neuronal resilience, survival, and aging trajectories. This review integrates recent insights into how TLDc proteins coordinate organellar pH regulation and iron homeostasis and discusses how disruption of these interconnected pathways contributes to age-related neurodegeneration. - Source: PubMed
Publication date: 2026/09/01
Ghufran Mohammad SajidSoni PriyankaThomas Bobby - Epidemiological studies suggest associations of asthma with the psychosis spectrum (psychotic experiences, bipolar disorder, schizophrenia), but the mechanisms underlying these associations remain unclear. - Source: PubMed
Publication date: 2026/08/06
Dardani ChristinaRobinson Jamie WHavdahl AlexandraDarrous LizaJones Hannah JZammit StanSullivan Sarah ARai DheerajStergiakouli EvieZhu ZhaozhongLiang LimingNava George WGardner ReneeGrove JakobRichardson Tom GSmith George DaveyDodd James WHemani GibranGaunt Tom RKhandaker Golam M - Camphor is a key quality determinant of lavender oil. Bornyl dehydrogenase (BDH) catalyzes the final camphor biosynthesis step, yet its gene family and mechanism in lavender remain uncharacterized. We phylogenetically classified 154 short-chain dehydrogenase/reductase () genes into six clades and screened 17 genes. Integrated transcriptomic and metabolomic analyses revealed that camphor biosynthesis primarily occurs via the plastidic 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway, with coordinated expression of geranyl diphosphate synthase (), bornyl diphosphate synthases (), bornyl-diphosphate diphosphatase (), and genes. Most biosynthetic genes, especially and , were significantly upregulated in "Xinxun 4", correlating with its highest camphor content. Subcellular localization showed BDH1 resides in the cytoplasm, suggesting plastid-cytoplasm collaboration. In vitro assays demonstrated that BDH1 and BDH2 both oxidize (+)- and (-)-borneol to camphor. Molecular dynamics simulations revealed that BDH1's active site exhibits conformational flexibility, accommodating both enantiomers with similar binding affinities, which was confirmed by enzyme kinetics. Asn90 was identified as a key catalytic residue. These findings reveal BDH family expansion, coordinated gene expression driving camphor accumulation, and BDH1's catalytic flexibility, offering key genetic resources and mechanistic insights for optimizing lavender camphor content via metabolic engineering and molecular breeding. - Source: PubMed
Publication date: 2026/06/07
Zeng YulingNie JingLan HaiyanZhang YichaoDai YufangCao XiaojieZhang LiangHu Jianjian - Adaptation is one of the key processes of animal domestication, environmental pressures will leave footprints in the genome. Geese are widely distributed across multiple geographical conditions with distinct adaptations. However, few reports have focused on the environmental adaptability of geese. Moreover, the key environmental drivers that trigger local adaptation and its genetic mechanisms are still unknown. To this end, 35 agro-climatic variables of 257 geese from 14 Chinese breeds were obtained, the key environmental drivers and its genetic mechanism were elucidated by combining the genome data. - Source: PubMed
Publication date: 2026/05/30
Zhou XiaoliXia JunliangChen WeidingZou JiajiaChen JiahuiZhang Xiquan - Emerging evidence has demonstrated the additional therapeutic benefits of ticagrelor in acute coronary syndrome (ACS) patients with diabetes. However, the underlying mechanisms of this association remain elusive. Mendelian randomization (MR) analysis using genome-wide association study (GWAS) data on ticagrelor, plasma proteomics and type 2 diabetes was employed to identify causal mediator proteins. RNA sequencing (RNA-seq) of ticagrelor-treated HepG2 cells revealed the molecular pathways regulating glucose metabolism. Genetically proxied ticagrelor was significantly associated with a reduced risk of diabetes (OR = 0.859, 95% CI: 0.783-0.934, P = 7.98E-05), and 24.41% of this effect was mediated by upregulation of BDH2 protein. In vitro experiments confirmed the enhanced effect of ticagrelor on glucose consumption. Transcriptome analysis revealed that mitochondrial respiratory chain transfer and oxidative phosphorylation (OXPHOS) were significantly enriched, and genes related to ATP biosynthesis were significantly upregulated. These findings highlight the non-platelet function of ticagrelor in maintaining glucose homeostasis, providing insights into potential drug repurposing in the future. - Source: PubMed
Publication date: 2026/05/20
Xie ZhipengMa HeshuoLiu YingjianLai Weihua