Ask about this productRelated genes to: ACADS Blocking Peptide
- Gene:
- ACADS NIH gene
- Name:
- acyl-CoA dehydrogenase short chain
- Previous symbol:
- -
- Synonyms:
- SCAD, ACAD3
- Chromosome:
- 12q24.31
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2017-09-21
Related products to: ACADS Blocking Peptide
Related articles to: ACADS Blocking Peptide
- High ammonia nitrogen stress significantly compromises the survival of under low-salinity conditions. However, existing studies predominantly focus on ammonia nitrogen responses under single stressors or normal seawater salinity. The molecular regulatory mechanisms, metabolic remodeling patterns, and key pathway interactions in shrimp subjected to high ammonia nitrogen stress under low-salinity environment remain unclear. In this study, we employed integrated transcriptomic and metabolomic analyses to unveil the underlying molecular responses and metabolic biomarkers in the gills of to ammonia stress under low-salinity conditions. First, . underwent low-salinity acclimation from 30‱ to 5‱ salinity and was then reared for one week to acclimate to the experimental environment. Subsequently, shrimp were treated with 42.32 mg/L ammonia nitrogen for a consecutive 96 h period. Integrated transcriptomic and metabolomic analyses elucidated the stress response patterns in the gills of under low-salinity ammonia nitrogen exposure. Specifically, 352, 802, and 140 differentially expressed genes (DEGs) were identified at 12 h, 48 h, and 96 h post-exposure, respectively. GO and KEGG enrichment analyses revealed that the significant DEGs were primarily enriched in six major pathways: autophagy, immune-related pathway, ABC transporter, fatty acid degradation and metabolism, metabolic pathway, and PPAR signaling pathway. Metabolomic profiling identified numerous differentially accumulated metabolites (DAMs) in both positive and negative ion modes, with significantly altered DAMs mainly consisting of organic acids and their derivatives, phospholipids, and other related metabolites. Key DAMs included taurine, guanosine, 1-palmitoyl-sn-glycero-3-phosphocholine, pseudouridine, and betaine. Integrative multi-omics analysis revealed that mediates stress responses by modulating five core pathways under low-salinity/high-ammonia-nitrogen dual stress: fatty acid degradation and metabolism (e.g., acyl-CoA dehydrogenase short chain (), acetyl-CoA acetyltransferase 2 ()), autophagy (e.g., autophagy-related protein 101-like ()), immune regulation pathway (e.g., V-type proton ATPase subunit H-like (), actin-5C-like ()), metabolic pathway (e.g., molybdopterin synthase catalytic subunit-like (), cytochrome P450 2U1-like ()), and ABC transporter (e.g., ATP-binding cassette sub-family D member 3-like (), ATP-binding cassette sub-family B member 10 ()). Through characterization of these core pathways, this study reveals the fundamental mechanisms by which responds to high ammonia nitrogen stress following low-salinity acclimation, providing a theoretical foundation for estuarine shrimp farming. - Source: PubMed
Publication date: 2026/04/13
Zhao YutongDing YangyangZhou FalinHu XiaojuanYang QibinCao Yucheng - The Alzheimer's Disease Sequencing Project (ADSP) Release 5 provides whole-genome sequencing data from 58,507 individuals across diverse ancestries to discover rare coding variants and genes associated with Alzheimer's disease (AD) and AD-related traits. Gene-based aggregation tests identified 40 genes surpassing a Bonferroni-corrected gene-wide significance threshold, including established loci (TREM2, PSEN1) and putative novel candidates. In replication analyses, 21 genes showed nominal support in UK Biobank and Alzheimer's Disease Genetics Consortium (ADGC) cohorts, with eight genes (TREM2, ACADS, MFSD12, NUP210L, PIEZO2, PSEN1, SMURF2, AKAP13) supported under identical masks. Carrier-based analyses of AD-related traits linked rare variants to age at onset, neuropathology, cognition, and cerebrospinal fluid biomarkers (Aβ42, total tau, pTau181). Furthermore, we observed that AD-enriched variants were more likely to be ancestry-concentrated, and coalescent analyses indicated that AD risk alleles are younger than background variants. Together, these findings provide a multi-ancestry rare-variant resource for AD gene discovery. - Source: PubMed
Publication date: 2026/03/31
Lee Wan-PingWang HuiLeung Yuk YeeCheng Po-LiangZheng WendiValladares OttoChung Wei-HsuanKuzma AmandaNaj AdamVardarajan BadriGrsiwold AnthonyHaines JonathanWang Li-SanSchellenberg Gerard - To elucidate the epidemiological characteristics and genetic variant profile of Short-chain acyl-CoA dehydrogenase deficiency (SCADD) among newborns from Hainan Province and evaluate its significance within the local neonatal disease screening panel. - Source: PubMed
Zhao PeizhenZhao ZhendongXu Haizhu - Short-chain acyl-CoA dehydrogenase (SCAD) is a critical enzyme in mitochondrial fatty acid β-oxidation, catalyzing the initial dehydrogenation of short-chain acyl-CoAs. Mutations in the gene cause SCAD deficiency (SCADD), a disorder with remarkably heterogeneous clinical presentation. However, the molecular mechanisms underlying substrate specificity and the pathogenicity of most variants remain poorly understood. Here, we present high-resolution cryo-EM structures of human SCAD in complex with its physiological substrate butyryl-CoA (C) and the longer substrate hexanoyl-CoA (C). The butyryl-CoA-bound structure at 2.1 Å resolution details a pre-catalytic geometry ideal for hydride transfer, with Glu392 positioned as the catalytic base. We systematically characterized nineteen disease-associated mutations, which we classify into three functional categories: those disrupting FAD binding, those impairing substrate binding, and those compromising protein folding and stability. In addition, using the W177R mutant as a representative model, we demonstrate that folding-defective mutations provoke protein aggregation, leading to proteotoxicity, oxidative stress, and apoptosis, revealing a pathogenic mechanism beyond mere catalytic loss. In brief, our integrated findings elucidate the structural determinants of substrate specificity and catalytic mechanism in SCAD, and provide mechanistic insights into the functional impairments caused by mutations linked to SCADD. - Source: PubMed
Publication date: 2026/03/14
Bai FangLi XinruJu KaidePan XijiangJin YeYou ZhijingZhang LiliLiu ZhaoxiaZhang ShuyangLuan Xiaodong - Reprogramming of lipid metabolism and cyclic GMP‒AMP synthase (cGAS)-stimulator of interferon genes (STING) signaling is associated with cancer development. However, whether and how fatty acid metabolism regulates the cGAS‒STING pathway in colorectal cancer (CRC) remains to be elucidated. In this study, we found that short-chain acyl-CoA dehydrogenase (ACADS) is aberrantly deficient in CRC cells and is associated with cancer progression in human patients. We further revealed that ablation of ACADS promoted CRC progression by orchestrating the cGAS‒STING signaling-dependent immunosuppressive tumor microenvironment (TME) in mouse xenografts and AOM/DSS-induced CRC models. Mechanistically, ACADS deficiency suppressed cGAS‒STING signaling by inhibiting mtDNA leakage in a nonmetabolic manner. ACADS binds to and inhibits mitochondrial DNMT1 (mito-DNMT1)-dependent mtDNA methylation, thereby stabilizing mtDNA and inhibiting its leakage. Genetic and pharmacological modulation of mito-DNMT1 restored ACADS-regulated mtDNA leakage, cGAS‒STING signaling, and CRC progression. Importantly, strong correlations between ACADS, mito-DNMT1, and STING signaling and the immune TME were found in patients with CRC. Furthermore, we screened and identified an old drug, hypericin, as an ACADS-binding compound that upregulates ACADS expression. Hypericin treatment can mimic ACADS overexpression-regulated pathways, ultimately improving the immune TME and suppressing CRC growth. These findings highlight a previously undiscovered ACADS/mito-DNMT1 complex that links fatty acid metabolism reprogramming to mtDNA methylation and cGAS‒STING signaling-dependent antitumor immunity. - Source: PubMed
Publication date: 2026/03/26
Yang FangWang MengHu ShaofanGuan XuZhao KunZhou YongYao HuiZhang TianyingLi LiuliGao YuanZhao SijieLiu NanXiao WeidongXiang YuancaiMiao Hongming