Hsp90 Blocking Peptide
- Known as:
- Hsp90 Blocking Peptide
- Catalog number:
- 33r-10737
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- Hsp90 Blocking Peptide
Related genes to: Hsp90 Blocking Peptide
- Gene:
- HSP90AA1 NIH gene
- Name:
- heat shock protein 90 alpha family class A member 1
- Previous symbol:
- HSPC1, HSPCA
- Synonyms:
- Hsp89, Hsp90, FLJ31884, HSP90N
- Chromosome:
- 14q32.31
- Locus Type:
- gene with protein product
- Date approved:
- 1990-06-27
- Date modifiied:
- 2016-10-11
Related products to: Hsp90 Blocking Peptide
Related articles to: Hsp90 Blocking Peptide
- Imidacloprid (IMI), a widely used neonicotinoid insecticide, has been associated with neurotoxic effects; however, the system-level mechanisms underlying these effects remain incompletely understood. Here, we integrated network toxicology with multi-omics analyses to investigate IMI-induced neurotoxicity in SH-SY5Y cells and the whole-organism model, Caenorhabditis elegans (C. elegans). Network toxicology identified 284 potential IMI-related targets, and protein-protein interaction network analysis further prioritized 45 core targets, including HSP90AA1, ESR1, MAPK3, SRC, MAPK1, IL6, BCL2, PRKACA, and MAPK8. Molecular docking suggested potential binding interactions between IMI and several core targets, while qRT-PCR provided transcript-level support for a subset of hub genes. Transcriptomic profiling revealed pronounced model-specific responses. In SH-SY5Y cells, IMI primarily induced neuron-related molecular alterations, characterized by disruption of voltage-gated calcium channel activity and enrichment of multiple synaptic pathways. In contrast, C. elegans exhibited broader organism-level transcriptomic remodeling involving developmental processes, extracellular structure organization, and stress-adaptive pathways, including the MAPK and FoxO signaling pathways. Untargeted metabolomics in SH-SY5Y cells further revealed biochemical remodeling related to the neuroactive ligand-receptor interaction pathway, glutathione metabolism, oxidative phosphorylation, and ABC transporter pathways. In addition, IMI significantly increased intracellular ROS levels and disrupted glutathione redox homeostasis, as reflected by altered GSH and GSSG levels and the GSH/GSSG ratio. Integrated analysis identified neuroactive ligand-receptor interaction and glutathione metabolism as shared pathway-level features across datasets, supporting a mechanistic model in which disruption of receptor-mediated neurotransmission is accompanied by redox imbalance. Overall, this study provides a systems-level view of IMI-induced neurotoxicity and highlights both shared pathway-level features and pronounced model-specific biological responses. - Source: PubMed
Publication date: 2026/05/05
Hou XingangWang KaiHou ZhiguangWei LipingZhang ZhengZheng XiaojiaoWang YuzhenLv MengTian JiangxinWang ZhaoyangMa ChaoZhao FanrongHan Jiajun - GeXiaZhuYu Decoction (GXZYD) has long been used in the context of Colorectal Cancer (CRC), yet its active constituents and associated molecular features remain incompletely characterized at the systems level. - Source: PubMed
Publication date: 2026/04/23
Li JiawenXiao ZiyuWang LiPeng ZehaoLiu XinsenLiu LongfeiYi Liwei - Vision-threatening ocular diseases are impacted by aging-associated molecular changes, including mitochondrial dysfunction, cellular senescence, and chronic inflammation. Anti-VEGF therapies targeting VEGF-A/VEGFR2 signaling remain the frontline standard of care, but many patients exhibit suboptimal or nondurable responses, often due to compensatory and/or compromised antiangiogenic and anti-inflammatory pathways. We aimed to elucidate shared mechanisms underlying treatment failure and disease progression. - Source: PubMed
Piroozmand SomayehLatifi-Navid HamidSoheili Zahra-SoheilaHosseinkhani SamanSamiei ShahramBarzegar Behrooz AmirAhmadieh HamidLeonardi AndreaGhavami SaeidSheibani Nader - Pulmonary arterial hypertension (PAH) is a severe and progressive cardiopulmonary disorder with limited treatment options. (Merr.) Sealy (CP) contains multiple flavonoids and other phytochemicals, but its active compounds and molecular mechanisms in PAH remain unclear. Active compounds of CP were screened by comprehensive literature mining and absorption, distribution, metabolism, and excretion (ADME) evaluation. PAH-related hub targets were identified from transcriptomic data using weighted gene co-expression network analysis (WGCNA), machine learning, and external validation. Functional enrichment, immune infiltration, and single-cell RNA-sequencing analyses were performed to characterize their biological roles and cellular localization. Molecular docking and molecular dynamics simulations assessed compound-target interactions. The effects of CP were further evaluated in hypoxia-induced rat pulmonary artery smooth muscle cells (RPASMCs). Five core bioactive compounds were identified, among which luteolin and quercetin were prioritized for further analysis. and were screened as hub targets. Bioinformatic analyses suggested that these targets were mainly associated with the "Lipid and atherosclerosis" pathway, metabolic reprogramming, and modulation of the immune microenvironment. Single-cell analysis showed broad expression of and enrichment of in fibroblasts and endothelial cells. Molecular docking and molecular dynamics simulations supported stable binding of luteolin to HSP90AA1. In vitro, CP extract inhibited hypoxia-induced hyperproliferation of RPASMCs and reduced HSP90AA1 protein expression. HSP90AA1 may represent a candidate molecular mediator of CP in PAH, and CP inhibited hypoxia-induced RPASMC proliferation in association with downregulation of HSP90AA1. - Source: PubMed
Publication date: 2026/04/21
Chen XinyingZhou LipengZhu ChenghaoSun Zhirong - Chronic kidney disease (CKD) associated vascular calcification (VC) is a leading cause of cardiovascular mortality, partially driven by osteogenic transdifferentiation of vascular smooth muscle cells (VSMCs). Chaperone-mediated autophagy (CMA) is a selective lysosomal degradation cellular process. However, the precise role and mechanism of CMA in CKD-associated vascular calcification remain unknown. We studied calcified arteries from CKD patients and rats fed on a high-phosphate diet using histological and ultrastructural methods. VSMCs' calcification was induced by a calcification medium containing high phosphate and calcium. CMA activity was measured by a KFERQ reporter and lysosomal staining. The expression of LAMP2a and HSP90AA1 was knocked down by siRNA, overexpressed by plasmid, and activated by QX77.1. Bioinformatic analysis, protein interaction studies, immunofluorescence and co-immunoprecipitation were performed to investigate the potential mechanism of CMA in VC. The expression of LAMP2a was increased in human calcified radial artery tissues ( = 3, < 0.05) and rats' calcified aortic tissues ( = 3, < 0.01), accompanied by lysosomal abnormalities. The activity of CMA was increased during the osteogenic transdifferentiation of VSMCs, as indicated by increased expression of RUNX2 and reduced expression of SM22α ( < 0.05). LAMP2a knockdown attenuated VSMCs' calcification ( < 0.05), whereas pharmacological activation of CMA aggravated calcification in VSMCs ( < 0.01). Bioinformatic screening identified HSP90AA1 as a candidate involved in CMA in vascular calcification. Elevated HSP90AA1 expression was observed in human calcified radial artery tissues ( = 3, < 0.01) and rat calcified aortic tissues ( = 3, < 0.01), which promoted osteogenic transdifferentiation of VSMCs ( < 0.05). HSP90AA1 interacted with LAMP2a and positively regulated its expression ( < 0.01). These findings support an association between CMA activation and CKD vascular calcification. It suggests that HSP90AA1 facilitates vascular calcification in chronic kidney disease involving chaperone-mediated autophagy. - Source: PubMed
Publication date: 2026/04/12
Zhang YalingLi MingLuo YanwenHuang LimingChen SipeiLi GuisenLi YiWang Li