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
- The stamens of L., often discarded as floral waste, are rich in flavonoids and phenolics. This study investigated their toxicological safety, antigenotoxic potential, and molecular mechanisms of protection against cyclophosphamide (CP)-induced genotoxicity. Hydroethanolic and hydromethanolic extracts were prepared, and acute oral toxicity was assessed in mice following the Organization for Economic Co-operation and Development guideline 423. Genotoxicity and its amelioration were evaluated in rat and mouse leukocytes by employing the alkaline comet assay. Oxidative stress markers, including superoxide dismutase activity, as well as malondialdehyde and glutathione levels, in hepatic and renal tissues were quantified. In parallel, nine major metabolites were identified in the extracts and were molecularly docked with key enzymes involved in CP bioactivation (CYP2B6), aldehyde detoxification (ALDH1A1), DNA repair (OGG1), and oxidative stress regulation (Keap1-Kelch domain; Protein Data Bank ID: 7K2A). The extracts were non-toxic up to 4,000 mg/kg and did not exhibit any genotoxicity. Pre-treatment with extracts (200 mg/kg body weight) significantly attenuated CP-induced DNA damage and restored antioxidant enzyme levels. Docking results supported these observations: rutin demonstrated a high affinity for CYP2B6 (-11.2 kcal/mol) and favorable binding to 7K2A (-9.7 kcal/mol); catechin gallate bound tightly to ALDH1A1 (-10.0 kcal/mol) and OGG1 (-9.2 kcal/mol). These findings suggest reduced CP activation, but enhanced detoxification and DNA repair. In conclusion, the extracts of stamens are safe and possess robust antioxidant and antigenotoxic properties, confirmed by molecular docking. These findings highlight their potential as natural protective agents against chemotherapy-induced genotoxicity. - Source: PubMed
Publication date: 2026/04/13
Mamri SamiraBaddaoui SanaeKhibech OussamaOuahhoud SabirKhoulati AmineChoukri MohammedAsehraou AbdeslamSaalaoui Ennouamane - Fanconi anemia (FA) is a genetic disease characterized by congenital abnormalities and increased risk for bone marrow failure and cancer. FA is caused by mutation of 23 genes, the protein products of which function in the maintenance of genome stability. An important role for the FA proteins in the repair of DNA interstrand crosslinks (ICLs) has been established. While the endogenous sources of ICLs relevant to the pathophysiology of FA have yet to be determined, a role for the FA proteins in the detoxification of reactive metabolic aldehydes has been established. To discover new metabolic pathways linked to FA, we performed RNA-seq analysis on a previously established isogenic FA-D2 patient cell model. Multiple retinoic acid metabolism and signaling genes were differentially expressed in the FA-D2 patient cells, including ALDH1A1 and RDH10, two key enzymes in the retinoic acid pathway. Increased levels of ALDH1A1 and RDH10 were confirmed by immunoblotting. FA-D2 (FANCD2) patient cells displayed increased aldehyde dehydrogenase activity compared to the FANCD2-complemented cells. Following exposure to retinaldehyde, FA-D2 (FANCD2) patient cells exhibited increased DNA damage and checkpoint activation. Our findings provide an example of a novel link between retinoic acid metabolism and FA and suggest that retinaldehyde may be an additional reactive metabolic aldehyde relevant to the pathophysiology of FA. - Source: PubMed
Publication date: 2026/04/30
Blaize Justin LNoori Bahaa MHunter Kelsey PHenrikson Kathryn AAtoyan Janet AArdito Alan AChapdelaine Abygail GSun GongqinDonovan Frank XChandrasekharappa Settara CSchindler DetlevHowlett Niall G - Wilms tumor (WT) is the most common pediatric kidney cancer. Tolerogenic dendritic cells (TolDCs) promote tumor immune evasion in the tumor microenvironment. Therefore, establishing a TolDC-based prognostic model for WT holds significant clinical value. We analyzed WT-related genes from The Cancer Genome Atlas and TolDC-associated datasets to identify shared differentially expressed genes using Venn analysis. Protein-protein interaction network analysis and machine learning algorithms (Boruta and Support Vector Machine Recursive Feature Elimination, SVM-RFE) were performed to screen candidate hub genes. A prognostic risk model was constructed using univariate Cox proportional hazards regression, with predictive performance evaluated by Kaplan-Meier survival analysis and receiver operating characteristic curves. Immune infiltration analysis, gene set enrichment analysis, and BioGRID were conducted to elucidate biological functions. Drug-gene interaction analysis was performed using the Drug Signature Database. A total of 181 co-expressed genes were identified. Among these, MSH2, CDH2, ALDH1A1, AURKA, CD274, FOSL2, IL15RA, GADD45B, TGM2, CXCR4, SOD2, and MT1E were selected as TolDC-associated biomarkers for WT. The prognostic model ultimately pinpointed ALDH1A1, CXCR4, and FOSL2 as key diagnostic biomarkers, supported by Kaplan-Meier survival analysis and ROC curves, which confirmed the model's robust predictive capacity for survival risk. Drug-gene interaction analysis predicted 335 potential therapeutic compounds targeting ALDH1A1, CXCR4, and FOSL2. Comprehensive bioinformatics analysis identified the prognostic biomarkers of WT related to TolDCs, providing new insights for personalized WT treatment. - Source: PubMed
Publication date: 2026/04/30
Sun XiaolanGao YaqingMeng KexinWang YixuanWang Bei - Although exercise is the most effective strategy for increasing the skeletal muscle mass, the underlying molecular mechanisms remain poorly understood. We previously demonstrated that β-carotene, a provitamin A compound, enhances muscle mass through a retinoic acid receptor γ (RARγ)-dependent pathway. However, the involvement of vitamin A in exercise-induced muscle hypertrophy remains unclear. In this study, we used a mouse model of functional overload to mimic resistance exercise and investigated the role of vitamin A in overload-induced muscle growth. Overload increased the expression of Rdh10, Dhrs9 and Aldh1a2, an enzyme required for active vitamin A synthesis in the skeletal muscle. In contrast, the expression of Aldh1a1, Dhrs3, and Rarb was decreased by the overload. Vitamin A deficiency significantly suppressed overload-induced muscle hypertrophy and protein synthesis. Moreover, local administration of an RAR antagonist to the skeletal muscle reduced overload-induced protein synthesis. These findings suggest that vitamin A contributes to skeletal muscle hypertrophy during muscle overload by promoting protein synthesis via RAR-mediated signaling. - Source: PubMed
Kitakaze TomoyaNakatsuji AinoHarada NaokiYamaji Ryoichi - Although aldehyde dehydrogenases 1 family member A1 (ALDH1A1) has been extensively studied in cancer, its role in hepatocellular carcinoma (HCC) remains poorly understood. This study was designed to characterize the expression pattern and functional roles of ALDH1A1 in HCC, and to further investigate its underlying molecular mechanisms using integrated proteomic analysis. - Source: PubMed
Yue HanxunHu ZenanWu GuozhiLi RenpengJiang N AZheng Y AWang YupingZhou Yongning