Ask about this productRelated genes to: PPARA antibody
- Gene:
- PPARA NIH gene
- Name:
- peroxisome proliferator activated receptor alpha
- Previous symbol:
- PPAR
- Synonyms:
- hPPAR, NR1C1
- Chromosome:
- 22q13.31
- Locus Type:
- gene with protein product
- Date approved:
- 1993-11-01
- Date modifiied:
- 2016-10-05
Related products to: PPARA antibody
Related articles to: PPARA antibody
- To investigate the mechanism by which polydatin ameliorates neurological damage in Wilson disease (WD) based on bioinformatics analysis and experimental validation. - Source: PubMed
Publication date: 2026/06/08
Wang NiWu KaijianWei WangyunZhang WanqingFANGMingsheng Zhang Jing - Amid the growing demand for natural growth promoters in poultry production, phytobiotics are being extensively explored for their bioactive properties. Study aimed to evaluate the effects of Leontopodium alpinum extract on blood parameters, hepatic histopathological changes, and the expression of genes in broiler chickens. A total of 180 Ross broilers were divided into groups: control (C), E1 (0.5 g kg feed), E2 (1.0 g kg feed). Reductions in serum ALT and AST activities (p < 0.001), TCH (p = 0.001), and TG (p = 0.014) were observed in group E2. E1 showed the most favorable coagulation profile in the case of FIB (p = 0.038), TT (p = 0.041), and PT (p = 0.013), compared to groups E2 and C. Hematological analysis showed increased RBC (p = 0.007), hemoglobin (p = 0.037), WBC (p = 0.001), neutrophils (p = 0.022), and decreased monocytes (p = 0.039) in group E2. Expression of metabolic regulators FASN (E1, p = 0.018; E2, p = 0.007), NRF1 (E2 vs. C, p = 0.002; E2 vs. E1, p = 0.033), PPARA (E2 vs. C, p = 0.002; E2 vs. E1, p = 0.009), and UGT1A1 (E2 vs. C, p = 0.001) was reduced in a dose-dependent manner. HMOX1 (p = 0.003), NFE2L2 (E2 vs. C, p = 0.021), and NQO1 (E2 vs. C, p = 0.003) were downregulated in E2. L. alpinum (E2) enhances antioxidant capacity and metabolic performance in birds without histopathological or hemostatic side effects. - Source: PubMed
Publication date: 2026/06/03
Patrycja ReszkaKarolina StasiakAgata DankowiakowskaDorota Cygan-SzczegielniakElżbieta PietrzakMagdalena Stanek - Substantial improvements in lamb production have been achieved through genetic selection and advanced husbandry practices; however, whether flavour heterogeneity among different muscle anatomical regions is driven by region-specific metabolic and lipid regulatory patterns remains unclear. We hypothesised that distinct muscle cuts exhibit characteristic flavour profiles associated with differential amino acid composition, lipid molecules, and gene profiles. To verify this hypothesis, the muscle (LDM), front leg muscle (FLM), and hind leg muscle (HLM) of Sadumont lamb were systematically compared using integrated omics. Significant differences in amino acid composition were observed among muscles, with glycine and valine showing pronounced variation. The FLM exhibited higher levels of delicious amino acids than LDM and HLM. Volatile profiling revealed distinct aroma signatures, with hexanal predominating in LDM, 1-octen-3-ol and d-limonene characterising FLM, and octanal, nonanal, and benzaldehyde enriched in HLM. Lipidomic analysis showed that LDM was dominated by triacylglycerols, whereas FLM was enriched in phospholipids, particularly phosphatidylcholine and phosphatidylinositol, which are associated with lipid oxidation and flavour precursor generation. The HLM displayed an intermediate lipid profile with slightly elevated C22:6 and C20:5n3. Transcriptomic analysis identified 2595 differentially expressed genes, which were enriched in lipid-related pathways, including fatty acid elongation and metabolism. Notably, divergent expression of and supported differential regulation of fatty acid oxidation across muscle cuts. These findings support our hypothesis that flavour heterogeneity among muscle cuts is closely linked to cut-specific lipid components and gene expression. Additionally，these molecular markers could be utilised in precision breeding and meat quality optimisation. - Source: PubMed
Publication date: 2026/05/18
Guo TaoXing BaimingNie RuixueWang WenwenLiu NaAn XiaopingQi JingweiWang Yuan - The rising burden of antimicrobial resistance (AMR) necessitates new bioactive molecules that are both sustainable and therapeutically relevant. Endophytic actinomycetes, particularly , represent a valuable but underexplored source of secondary metabolites with pharmaceutical potential. - Source: PubMed
Publication date: 2026/05/14
Pattapulavar VeilumuthuSubburaj SaranyadeviRamanujam SathiyabamaShil RiyankaVelmurugan PriyankaGhatak TapasMuthusamy SanjivkumarSamrot Antony VChristopher John Godwin - Improving feed efficiency in dairy cattle requires a better understanding of tissue-specific mechanisms that support energy and nutrient utilization. Skeletal muscle represents a major proportion of body mass in dairy cows and plays a major role in post-absorptive metabolism. Our previous liver proteomics study highlighted that high-efficiency (HE) cows exhibit enhanced hepatic fatty acid oxidation, supporting lower feed intake without compromising productivity. This study aimed to identify muscle-based metabolic adaptations associated with feed efficiency. Skeletal muscle samples from 8 HE (low residual feed intake, RFI) and 8 low-efficiency (LE; high-RFI) mid-lactation (119 ± 33 DIM) Holstein cows, ranked at the top and bottom 10% of RFI, were analyzed using tandem mass tag proteomics and RT-qPCR to identify differences in skeletal muscle related to feed efficiency. HE cows had significantly greater muscle glycogen content and exhibited a coordinated metabolic shift favoring lipid utilization. RT-qPCR showed increased expression of β-oxidation (PPARA, ACADS, ACADVL, ACOX1) and triglyceride mobilization (ATGL) in HE cows. In contrast, proteomics revealed lower abundance of glycolytic and glycogenolytic enzymes (e.g., ALDOA, PFKM, PGAM2, PYGM, AGL) in HE muscle, indicating reduced glucose and glycogen catabolism. Proteins involved in the SLC2A4 (GLUT4) translocation pathway (ACTG1, YWHAH, YWHAZ) were more abundant in HE cows, suggesting an increased capacity for insulin-stimulated GLUT4 translocation, which may contribute to greater glycogen storage. Proteomics also showed enhanced redox regulation in HE cows, with greater abundance of GSR, CAT, GPX1, and PRDX2, and lower abundance of mitochondrial complexes I (NDUFB8) and III (UQCRC2), major sites of reactive oxygen species formation. These results indicate that skeletal muscle in HE cows adopts a metabolic phenotype characterized by increased reliance on lipid-derived fuels, glucose sparing, and improved oxidative homeostasis. Together with previously reported hepatic adaptations, these muscle-specific responses likely contribute to whole-animal feed efficiency in lactating dairy cows. - Source: PubMed
Publication date: 2026/05/30
Daddam Jayasimha RSura MounicaSarmikasoglou EfstathiosAhmad GhayyoorNaughton SarahMills MorganWhite Heather MVandeHaar MichaelZhou Zheng