MYH9 Antibody
- Known as:
- MYH9 Antibody
- Catalog number:
- csb-pa01405a0rb
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- CusAb
- Gene target:
- MYH9 Antibody
Related genes to: MYH9 Antibody
- Gene:
- MYH9 NIH gene
- Name:
- myosin heavy chain 9
- Previous symbol:
- DFNA17
- Synonyms:
- NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS
- Chromosome:
- 22q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 1990-03-12
- Date modifiied:
- 2019-04-23
Related products to: MYH9 Antibody
Related articles to: MYH9 Antibody
- Stanford type A aortic dissection (AAD) is a life-threatening cardiovascular disease characterized by tearing in the aortic wall. Using spatial transcriptomics and multiplex immunofluorescence, we comprehensively analyzed ascending aortas from eight AAD patients across different severities and segments. We demonstrate that SPP1-driven inflammatory signaling intensifies with AAD severity, identifying a nine-gene, layer-anchored severity scale: MYL6/CALD1/MYH9 (mild); CCL2/CP/COL4A1 (moderate); and TMSB4X/ATP5F1E/PKM (severe). Importantly, the collagen-remodeling triad COL1A1/COL3A1/MMP2 is concurrently up-regulated in the brachiocephalic, left subclavian, and left common carotid arteries, often before the ascending aorta meets surgical diameter thresholds. These molecular signatures provide a critical foundation for non-invasive biomarker discovery, risk stratification, and precision pharmacotherapy targeting the SPP1-inflammatory axis, ultimately offering new insights into AAD mechanisms and therapeutic targets. - Source: PubMed
Publication date: 2026/07/16
Li Yan-HongCao YingLiu FenWang Li-YingLiu Hai-ZhouZhao QianAdi DilareHuo QiangLiu ZhengLuo Jun-YiLi Xiao-MeiLiu DiYang Yi-Ning - This study aimed to analyze the active ingredients of the compound preparation of Yiqi Huoxue (YQHX) and evaluate the therapeutic effect of its nanoparticles (MM/YQHXF-NPs) on atherosclerosis (AS). First, the active ingredient in the YQHX formulation was identified by LC-MS analysis. Subsequently, transmission electron microscopy (TEM) tests particle size. Mapping tests nanoparticle surface elements. Dynamic light scattering (DLS) tests nanoparticle size and distribution. ZETA tests nanoparticle surface potential. HPLC tests drug release. The results showed that these nanoparticles were spherical, approximately 100 nm in size, and had good dispersion. The P element content of MM/YQHXF-NPs increased after cell membrane coating, and their hydrodynamic size also increased accordingly, but the Polymer dispersity index (PDI) value was low, indicating good monodispersity. In addition, the nanoparticle surface had a weak negative charge, the encapsulation efficiency of YQHXF was 59.4%, and the drug loading rate was 5.61%. In cell-based experiments, MM/YQHXF-NPs showed no cytotoxicity towards A7r5 cells at a concentration of 150 μg/mL. The study found that ox-LDL-induced A7r5 cell-to-foam cell transformation was significantly inhibited. Oil Red O staining revealed that MM/YQHXF-NPs reduced lipid accumulation. In addition, YQHXF and its active component, salvianolic acid B, can inhibit the foam cell formation of A7r5 cells. Furthermore, MM/YQHXF-NPs modulated the phenotype of smooth muscle cells, inhibiting the expression of genes such as Myh9, Icam-1, Vcam-1, Tnfrsf11b, Cd68, Lgals3, and Abca1, while promoting the expression of Myh11 and Smtn. Mechanistic studies revealed that MM/YQHXF-NPs exerted their effects by inhibiting the Krüppel-like factor 4 (KLF4) and NF-κB signaling pathways. In a high-fat diet, ApoE mice model of AS, MM/YQHXF-NPs demonstrated significant therapeutic efficacy. H&E and Oil Red O staining revealed that MM/YQHXF-NPs mitigated pathological changes, reduced plaque size, and lowered serum TC, TG, LDL, and HDL levels. They also stabilized atherosclerotic plaques by increasing fiber area and promoting SM22α and SM-MHC expression. Consistent with the results from cell-based experiments, MM/YQHXF-NPs effectively inhibited the transformation of arterial smooth muscle cells (SMCs) into foam cells in vivo and suppressed the activation of KLF4 and NF-κB signaling pathways. In summary, MM/YQHXF-NPs can effectively prevent the transformation of SMCs into foam cells by inhibiting the KLF4 and NF-κB signaling pathways, thereby alleviating AS. These results provide a theoretical basis for MM/YQHXF-NPs as a potential therapeutic drug for AS. - Source: PubMed
Publication date: 2026/07/27
Li YanqingWang HongyuanGuan YiZhuang JinliYang XiaohongChen YantingCun ShengyuLi JianfengQin YaXie Quan - Differentiating myosin heavy chain 9 (MYH9)-related disease (MYH9-RD) from immune thrombocytopenia (ITP) remains clinically challenging. This study utilized data-independent acquisition (DIA) plasma proteomics to identify distinguishing biomarker signatures. Profiling cohorts of MYH9-RD (n = 10), ITP (n = 10) and healthy controls (n = 14) quantified 2533 proteins, revealing distinct immune and metabolic remodelling. We identified 91 MYH9-RD-specific and 124 ITP-specific proteins, highlighting divergent organ involvement pathways. By integrating protein-protein interaction networks with Boruta and Random Forest machine-learning algorithms, we identified preliminary candidate biomarker panels (MYH9-RD panel: von Willebrand factor [VWF], cholesteryl ester transfer protein [CETP], apolipoprotein A-1 [APOA1], periostin [POSTN]; ITP panel: neutrophil gelatinase-associated lipocalin [NGAL], plasminogen activator inhibitor-1 [PAI-1], carboxypeptidase B2 [CPB2]) that demonstrated excellent apparent discrimination. This exploratory study provides a hypothesis-generating framework, revealing fundamentally distinct molecular landscapes between congenital and acquired macrothrombocytopenia. Pending rigorous future external validation, these preliminary candidate biomarkers offer novel biological insights into the divergent pathophysiologies of MYH9-RD and ITP. - Source: PubMed
Publication date: 2026/07/27
Luo XiaojuanCao KeWang RuizhiWu WeigenHuang TaoZhang YanFu XiaoyingLi DefaHe Meifang - This study investigated the impact of dietary alginate oligosaccharides (AOS) on the meat quality of breast muscle in broilers exposed to heat stress (HS). In broilers exposed to HS, dietary AOS enhanced pH and the activities of catalase (CAT), glutathione peroxidase (GSH-Px), and glutathione S-transferase (GST) (P < 0.05), while decreasing drip loss and malondialdehyde (MDA) concentration in breast muscle (P < 0.05). Non-targeted metabolomics analysis revealed that AOS regulates lipid metabolism of breast muscle. Furthermore, AOS upregulated the expression of antioxidant genes GSTA3, GPX3, CAT1, NQO1, and muscle fiber transformation regulators MyH1D, PGC-1α, MEF2C (P < 0.05), while downregulating lipogenic genes SREBP-1, ACC, FAS and FABP3, and the fast muscle marker MyH9 (P < 0.05). Concomitantly, AOS enhanced the phosphorylation modification level of Nrf2 and AMPK proteins (P < 0.05). Therefore, AOS improves the meat quality of breast muscle in broilers exposed to HS by improving the oxidative stability, promoting the transformation of fast muscle fibers into slow muscle fibers, and alleviating lipid metabolism disorders. - Source: PubMed
Publication date: 2026/07/17
Yao Qing-HuaWang Yao-YaoYe Xue-QingZhao Zhong-XiangLiu Hui-MeiLiu Wen-Chao - Hepatic stellate cell (HSC) activation can lead to liver fibrosis, for which there are no effective treatments. Aberrant cytoskeletal reorganization is a central driver of HSC activation. Non-muscle myosin II (NM II) is known to regulate cytoskeleton remodeling via its actin cross-linking and contractile properties. However, the molecular players controlling actomyosin assembly and contractility in HSCs during liver fibrosis remain poorly defined. Here, we identified integrin β-like 1 (ITGBL1) as a gatekeeper of HSC quiescence by negatively regulating actomyosin contractility-driven mechanotransduction in HSCs. ITGBL1 expression was markedly elevated in activated HSCs found in patient and mouse fibrotic livers. Unexpectedly, HSC-specific Itgbl1 deficiency worsened liver fibrosis, whereas ITGBL1 overexpression in HSCs limited it, suggesting a protective role for ITGBL1 against a pathogenic HSC activation. Multi-omics and functional analyses revealed that ITGBL1 impaired F-actin filament organization in HSCs by disrupting myosin heavy chain 9 (MYH9, also named NM II heavy chain A)-dependent actomyosin assembly. In line, HSC-specific Myh9 deficiency or silencing of Myh9 in HSCs alleviated liver fibrosis. Taken together, our findings unveil the ITGBL1-MYH9 interaction acts as a critical mechano-regulatory brake that maintains cytoskeletal equilibrium and mechanical homeostasis in HSCs, providing a promising therapeutic strategy to combat liver fibrosis. - Source: PubMed
Publication date: 2026/07/16
Li YixinWang YanTong ChenhaoFu XinghuanMa NingningHao YawenFeng ZianLing ShijiaYin ZequnLi HaodongGe ShujunYang SitingXiao PengDong SiyueGuillot AdrienDuan YajunHe Yong