COX5A Antibody
- Known as:
- COX5A Antibody
- Catalog number:
- csb-pa00414a0rb
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- CusAb
- Gene target:
- COX5A Antibody
Related genes to: COX5A Antibody
- Gene:
- COX5A NIH gene
- Name:
- cytochrome c oxidase subunit 5A
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 15q24.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-11
- Date modifiied:
- 2016-10-05
Related products to: COX5A Antibody
Related articles to: COX5A Antibody
- Snoring-related vibrations have been proposed as a pathogenic factor contributing to upper airway muscle dysfunction in patients with obstructive sleep apnea (OSA). To investigate whether exposure to snoring vibration is linked to muscle weakness, we used an in vitro vibration model to examine its effects on mitochondrial homeostasis in L6 muscle cells at 8, 12, 24, and 48 h. The findings were then compared with mitochondrial alterations in the upper airway muscles from snorers and patients with OSA. Proteomic analysis of L6 myoblasts revealed extensive remodeling of the mitochondrial proteome at 8 h, affecting pathways involved in oxidative phosphorylation, protein import, ribosome biogenesis, and RNA processing. Respiratory chain remodeling was subunit-specific, with increased abundance of selected components of Complexes I, IV, and V, including NDUFS4, COX5A, and ATP5PD. However, reductions in spliceosome-associated factors, such as SRSF2 and DDX46, along with alterations in mitochondrial ribosomal proteins, indicated impaired RNA processing and protein synthesis. Furthermore, both proteomic and transcriptomic analyses revealed activation of a mechanosensing-mechanotransduction axis, with early upregulation of integrin subunits and mechanosensitive ion channels, followed by transient activation of focal adhesion signaling. Despite transcriptional upregulation of selected Complex IV subunits Cox5a and Cox6a2, this response was accompanied by accumulation of unspliced pre-mRNA, indicating impaired RNA processing efficiency and a decoupling between transcript and protein levels. Real-time Seahorse assay revealed a collapse of mitochondrial respiration and glycolytic reserve at 8 h. Although mitochondrial oxygen consumption recovered after 48 h, the ability to dynamically upregulate glycolysis remained impaired. In patients, muscle capillarization was impaired, COX activity was reduced, and mitochondrial organization was disrupted. Moreover, transcription of Complex IV subunits COX5A and COX6A2 was, as in vibrated L6 cells, upregulated, suggesting a mismatch between transcript levels and protein expression. We conclude that snoring-induced vibrations are an unrecognized stressor that disrupts mitochondrial homeostasis in muscle by impairing RNA processing, protein synthesis, and mechanotransduction-driven mitochondrial remodeling, leading to transcript-protein uncoupling and likely muscle dysfunction. - Source: PubMed
Publication date: 2026/06/02
Stål PerEl-Habta RoineQian Yu-ChengZhu ShaochunWilliams ChloeMateus AndréGilthorpe Jonathan DShah Farhan - The leg muscles of poultry are an important source of high-quality protein and key trace elements. Most of the research on muscle development are focused on the embryonic or growth stage, there is relatively little research on the muscle development of chicken from embryonic stage to growth stages. Therefore, in this study, transcriptome sequencing was performed on leg muscle samples from female Huanglang chickens across embryonic (E13, E17) to growth stages (D1, D14, D35). A total of 7,691 differentially expressed genes (DEGs) were identified by comparison in pairs of the ten groups, and the highest number of DEGs was observed between E13 and D35, with 4,645 DEGs. Time-series expression analysis using STEM revealed three distinct expression clusters: cluster I (2,582 genes, downregulated genes), cluster II (1,666 genes, upregulated genes), and cluster III (614 genes, transient upregulation peaking at D1). GO and KEGG enrichment analyses showed that the DEGs were enriched in pathways such as cell cycle and DNA replication (cluster I), metabolic and muscle structure-related pathways (cluster II), oxidative phosphorylation and mitochondrial function (cluster III). Protein-protein interaction network analysis identified hub genes, including CDC45/MCM complex members in cluster I, mitochondrial genes such as CYTB and ND1 in cluster II, and oxidative phosphorylation genes including NDUFS3 and COX5A in cluster III. Transcription factor prediction highlighted KDM5A, KDM5B, PHF8, and SAP30 as key regulators. The RT-qPCR results of seven genes (ACTN2, PDK4, MYOG, MYOD1, MYH1F, MYH1B, and MYF6) were consistent with the RNA sequencing (RNA-seq) analysis. This study is the first to systematically analyzed the leg muscle development mechanisms of local chicken breeds from embryonic stage to early growth stage. It provides a comprehensive transcriptomic resource for understanding leg muscle development in chickens. - Source: PubMed
Publication date: 2026/05/28
Liu XuWang ZihanChen TingLiang HongniYang CanYang HaiDeng Yuying - Triploid turbot () exhibit superior growth and survival, yet the molecular basis of their sterility-a key trait for aquaculture-remains largely unexplored. This study investigated ovarian development and transcriptomic profiles in diploid and triploid at three key stages (6, 10, and 20 months post-hatch, mph) to elucidate the stage-specific molecular mechanisms underlying triploid sterility. Histological analysis revealed that diploid ovaries progressed through normal oogenesis to the early vitellogenic stage by 20 mph, whereas triploid ovaries were arrested at the oogonial stage, with only occasional primary oocytes and extensive connective tissue infiltration. Comparative transcriptomic analysis identified 13,305, 14,599, and 13,331 differentially expressed genes (DEGs) between triploid and diploid ovaries at 6, 10, and 20 mph, respectively. Functional enrichment analysis showed that DEGs were significantly associated with meiotic processes, cell cycle regulation, energy metabolism, and apoptosis. Key meiotic genes (, , ) were consistently upregulated in triploids across all stages, while the DNA repair gene was paradoxically downregulated, indicating attempted but aberrant meiotic initiation. Oogenesis regulators (, , ) and energy metabolism genes (, , ) were significantly downregulated, whereas apoptosis-related genes (, ) were upregulated. Notably, KEGG pathway analysis revealed stage-specific shifts from stress-induced apoptosis and p53 signaling at early stages to proteasome activation at later stages, suggesting a transition from active germ cell elimination to maintenance of cellular homeostasis in developmentally arrested ovaries. Collectively, these findings demonstrate that triploid sterility is associated with coordinated dysregulation of meiotic progression, metabolic, and apoptotic pathways, providing a high-resolution molecular framework for understanding reproductive failure in triploid fish and informing strategies for optimizing triploid production in aquaculture. - Source: PubMed
Publication date: 2026/04/28
Sun XiaoxuanLi LifangCheng LuyaoMeng ZhenXu WentengLiu Xinfu - Hematopoietic stem cells (HSCs) are essential for maintaining blood system homeostasis. Their aging leads to functional decline and increased susceptibility to blood disorders, largely driven by elevated reactive oxygen species (ROS). Here, we identify peanut procyanidin A (PPA) as a potent compound that delays HSC aging by targeting cytochrome c oxidase subunit 5a (Cox5a). Through screening of 234 FDA-approved natural compounds, we found that PPA significantly reduces mitochondrial ROS and improves the function of aged HSCs in mice. Transcriptomic analysis revealed that PPA induces a metabolic shift from oxidative phosphorylation toward glycolysis, reminiscent of a youthful HSC state. Moreover, PPA rescues aging phenotypes in human CD34+ hematopoietic progenitor cells. Our study establishes Cox5a as a druggable target for HSC rejuvenation and highlights PPA as a promising therapeutic candidate for age-related hematopoietic decline. - Source: PubMed
Publication date: 2026/04/29
Wang YingZhang BingzhengLu JunfeiLiu LinTang XiaoyuLi ChangzhengZeng XiFan ChuqingQiao YuncongChen ChengZhang YuChen JiajiaLi ZhiyiLuo YuchengYang GuizhiShen JuanLiu Bing - For chemical probe and drug discovery campaigns, the pairing of mass spectrometry-based chemoproteomics with photoaffinity labelling has emerged as a favoured approach for target discovery and mode of action assignment. However, photocrosslinked peptide-compound adducts raise analytic challenges for quantitative binding site discovery. Here, to address these challenges, we establish the Silyl Ether Enables Chemoproteomic Interaction and Target Engagement (SEE-CITE) method. SEE-CITE incorporates a fully functionalized chemically cleavable photocrosslinking handle that enables precise site-of-labelling identification and head-to-head comparisons of relative binding site engagement by chemically diverse compounds. To ensure high-confidence localization of labelled residues, we extended the MSFragger algorithm of the FragPipe computational platform to report localization scores customized for photoaffinity labelling and SEE-CITE data. When applied to scout fragments and analogues of select FDA-approved kinase inhibitors, SEE-CITE delineates known drug binding sites and uncovers small-molecule binding sites that affect the protein activity of RTN4 and COX5A. - Source: PubMed
Publication date: 2026/04/27
Ngo ChauTakechi ShoSivakumar AdityaVillanueva MirandaYu FengchaoBall Andréa BRubio JavierBiletch ElijahBurton Nikolas RBoatner Lisa MKim PhillipTurmon Alexandra CPerumal NitheshLiesa MarcDivakaruni Ajit SNesvizhskii Alexey IBackus Keriann M