Ask about this productRelated genes to: ALDH1A1 antibody
- Gene:
- ALDH1A1 NIH gene
- Name:
- aldehyde dehydrogenase 1 family member A1
- Previous symbol:
- PUMB1, ALDH1
- Synonyms:
- RALDH1
- Chromosome:
- 9q21.13
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2015-11-18
Related products to: ALDH1A1 antibody
Related articles to: ALDH1A1 antibody
- Per- and polyfluoroalkyl substances (PFAS) are persistent environmental contaminants associated with adverse human health outcomes. However, experimental toxicity data remain unavailable for the vast majority of PFAS, limiting comprehensive risk assessment. In this study, ML-based classification Quantitative Structure Toxicity Relationship (QSTR) models were developed to predict PFAS toxicity across three biologically relevant high-throughput screening endpoints. These included AID-1030 (ALDH1A1 inhibition associated with reproductive toxicity), AID-504444 (Nrf2 pathway inhibition responsible for vascular disruption, hepatic steatosis, lung carcinogenesis, and infertility), and AID-588855 (inhibition of TGF-β/Smad3 signalling linked to developmental toxicity and tumour progression). To address pronounced class imbalance in these datasets, multiple data balancing techniques (ADASYN, SMOTE, Borderline-SMOTE, SVMSMOTE, and random oversampling) were applied. Fourteen ML classifiers were trained for each balanced dataset, yielding 70 models per endpoint. Sum-of-Ranking-Differences (SRD) analysis identified the most robust models with Gradient Boosting, Random Forest, and Support Vector Classifier models emerging as optimal for AID-1030, AID-504444, and AID-588855, respectively. SHAP and substructure analyses provided mechanistic interpretability, by linking PFAS structural features and AOP progression. The optimized models were further applied to an independent external dataset of 2,361 PFAS, and a Python-based screening tool, PERSIST, was developed to screen PFAS. - Source: PubMed
Publication date: 2026/06/29
Sarkar SPore SRoy K - Anecdotal accounts of inebriated elephants are widespread across elephant-inhabited regions, yet the molecular and mechanistic basis underlying these observations remains incompletely understood. Alcohol metabolism in mammals is primarily mediated by alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). We investigated elephant ADH and ALDH at the genomic, transcriptional, and enzymatic levels, comparing them with humans, hamsters, and rats. Elephant liver predominantly expressed three ADH1 genes, as in humans and hamsters that voluntarily consume ethanol, a feature otherwise reported mainly in primates. We measured hepatic ADH and cytosolic ALDH activities in elephants, despite challenges in sample collection. Elephant ADH exhibited high ethanol affinity, allowing enzymatic activity at low substrate concentrations, likely related to large body size. ADH catalytic efficiency was comparable to other species, and cytosolic ALDH showed relatively high efficiency. These results suggest that elephants are less likely to possess exceptionally low hepatic ethanol-metabolizing capacity, although the lack of data on mitochondrial ALDH2 activity should be taken into consideration. Elephants also exhibited unique features, including the absence of ADH4 gene expression, duplication of ALDH1A1, and pseudogenization of ALDH1B1, which appear to have arisen in association with diet and potential functional redundancy among paralogs. In addition to their ecological and evolutionary significance, these findings may contribute to the interpretation of drug metabolism and support evidence-based pharmacological management in elephants, given the role of ADH and ALDH in pharmaceutical metabolism. Together, this study provides a molecular and enzymatic basis for understanding ethanol metabolism in elephants. - Source: PubMed
Publication date: 2026/06/23
Morita AyukoWatanabe KanamiKondo MitsukiKhidkhan KraisiriSaengtienchai AksornSomgid ChaleamchatTowiboon PatcharapaAngkawanish TaweepokeLangkaphin WarangkhanaNamwongprom KittikulKittisirik NaruepornIkenaka YoshinoriNakayama Shouta M MIshizuka Mayumi - Delayed cerebral ischemia (DCI) is a major contributor to poor outcomes after aneurysmal subarachnoid hemorrhage (aSAH), yet its molecular correlates and early blood-based candidate biomarkers remain incompletely understood. This study aimed to characterize plasma proteomic changes associated with DCI and identify exploratory candidate protein signatures. - Source: PubMed
Publication date: 2026/06/20
Wang KeLin FaZheng GuanghaoLi RuntingZhao YuanliChen Xiaolin - Human midbrain organoids (hMOs) derived from induced pluripotent stem cells provide a powerful system to model disorders involving dopamine (DA) dysfunction, including Parkinson's disease (PD) and neuropsychiatric conditions. However, current differentiation protocols still fall short in recapitulating early specification, substantia nigra pars compacta (SNpc)-like identity, and the functional maturation of vulnerable DA neurons. Here, we established a differentiation strategy that combines tri-phasic WNT modulation with dynamic bioreactor culture to generate hMOs enriched in SNpc-like DA neurons. This approach significantly increases the yield of TH⁺/GIRK2⁺ and TH⁺/ALDH1A1⁺ DA neurons and promotes enhanced synaptic maturation, robust electrophysiological activity, and elevated DA release. Single-cell transcriptomics revealed that this strategy drives the emergence of SOX6/GIRK2 SNpc-like neurons, accompanied by upregulation of synaptic, metabolic, and maturation programs, alongside reduced cell stress and apoptotic signaling. Importantly, hMOs demonstrated vulnerability upon exposure to α-synuclein preformed fibrils, resulting in aggregate formation and DA neuron degeneration, supporting their use as a human model of PD-relevant pathology. Overall, this system provides a scalable and physiologically relevant approach to investigate molecular mechanisms underlying neurodegeneration and DA-related disorders. - Source: PubMed
Publication date: 2026/06/17
Raji HariamBertoli FedericoPerez Maria JoseLam AliciaVolpicelli-Daley LauraDeleidi Michela - Glioblastoma (GBM) invariably develops resistance to temozolomide (TMZ), the frontline chemotherapeutic agent, leading to treatment failure. The molecular mechanisms underlying this resistance remain incompletely understood. Here, we identify karyopherin subunit alpha 3 (KPNA3) as a potential contributor to TMZ resistance. Through integrated bioinformatics analysis of TMZ-resistant glioma cells (SF126R) and patient databases, we found KPNA3 expression is elevated in TMZ-resistant contexts and correlates with poor prognosis in TMZ-treated patients. Functional studies demonstrated that KPNA3 knockdown in resistant cells impaired malignant behaviors, re-sensitized cells to TMZ-induced apoptosis, and suppressed glioma stem cell (GSC) properties, including sphere formation and expression of stemness factors (OCT4, ALDH1A1). Mechanistically, KPNA3 was associated with a dual pathway: it correlated with increased expression of the DNA repair enzyme MGMT and was linked to activation of the STAT3 signaling pathway. KPNA3 knockdown reduced both MGMT levels and STAT3 phosphorylation (Tyr705). Furthermore, pharmacological inhibition of STAT3 mirrored the effect of KPNA3 knockdown by potently inhibiting GSC generation. Clinically, KPNA3 and p-STAT3 protein levels were positively correlated in high-grade glioma tissues. Collectively, our findings suggest that KPNA3 may play a role in concurrently enhances DNA repair and sustains the GSC population to foster TMZ resistance, identifying it as a candidate for further investigation for overcoming chemoresistance in GBM. - Source: PubMed
Gao YanruYuan HeZhou HoulingGao ChaoSun SulingHe ChuanjieFang ZhiyouChen Xueran