Ask about this productRelated genes to: HSP90AB1 antibody
- Gene:
- HSP90AB1 NIH gene
- Name:
- heat shock protein 90 alpha family class B member 1
- Previous symbol:
- HSPC2, HSPCB
- Synonyms:
- -
- Chromosome:
- 6p21.1
- Locus Type:
- gene with protein product
- Date approved:
- 1990-06-27
- Date modifiied:
- 2016-10-05
Related products to: HSP90AB1 antibody
Related articles to: HSP90AB1 antibody
- Oral squamous cell carcinoma (OSCC) has a poor prognosis and limited effective therapies. Anemarrhena asphodeloides exhibits anticancer activity, but its efficacy in OSCC treatment remains underexplored. Network and protein-protein interaction analysis identified 275 overlapping targets and 12 hub genes, with HSP90AA1, HSP90AB1, and CASP3 upregulated in OSCC, linked to poorer survival. QSAR modeling, molecular docking, and molecular dynamics simulations demonstrated stable binding of key bioactive compounds with HSP90 and AKT1, highlighting hippeastrine as a promising candidate. ADMET analysis indicated their favorable pharmacokinetic profiles. To validate the therapeutic potential of hippeastrine, in vitro experiments were conducted using the CAL27 and SCC-9 cell lines. CCK-8 assay demonstrated that hippeastrine exerted significant and dose-dependent cytotoxicity against OSCC cells. Furthermore, hippeastrine treatment significantly suppressed colony formation and attenuated cell migration and invasion capabilities. Gene set enrichment analysis of TCGA-HNSC data revealed a positive correlation between HSP90AA1/AB1 expression and PI3K/Akt/mTOR signaling. Western blot analysis confirmed inhibition of the HSP90-PI3K-Akt-mTOR axis by hippeastrine. Moreover, functional rescue experiments with the PI3K activator 740 Y-P successfully reversed the hippeastrine-induced suppression of cell viability and PI3K/Akt phosphorylation. These findings indicate that hippeastrine exerts anti-OSCC effects by targeting the HSP90/PI3K/Akt/mTOR pathway, highlighting it as a novel therapeutic agent against OSCC. - Source: PubMed
Lu YingHuang LanlanShen LiSingla Rajeev KZhu Xiaoming - Bisphenol A (BPA) is a pervasive environmental endocrine disruptor implicated in hormone-related cancers.However, its association with non-hormone-dependent malignancies such as Diffuse Large B-cell Lymphoma (DLBCL) remains poorly understood.This study aimed to predict the potential molecular mechanisms linking BPA exposure to DLBCL pathogenesis through an integrated approach combining network toxicology and molecular docking.We systematically identified 46 overlapping genes shared between BPA-associated targets and DLBCL-related genes. Protein-protein interaction network analysis indicate six hub genes(HSP90AB1, HSPA8, CCNA2, CDK1, LDHA, and HSPA14),with HSP90AB1 exhibiting the highest topological centrality.Functional enrichment analysis demonstrated that these genes are significantly enriched in key oncogenic signaling pathways, including the PI3K-Akt and MAPK pathways, as well as critical biological processes such as protein folding and cell cycle regulation. Molecular docking simulations further predicted the stable binding affinity between BPA and each of the six hub proteins, with binding energies below - 6.0 kcal/mol. Collectively, our computational findings suggest a putative mechanistic framework in which BPA may contribute to DLBCL development by directly interacting with and potentially dysregulating central regulatory nodes in cellular networks, particularly the molecular chaperone HSP90AB1. These predictions require experimental validation but provide a basis for future mechanistic studies. - Source: PubMed
Publication date: 2026/05/27
Zhang YueJin Li - Chronic kidney disease (CKD) is a progressive global health challenge. While empagliflozin, a selective SGLT2 inhibitor, is known to attenuate CKD progression through mechanisms beyond glycemic control, the precise molecular pathways remain incompletely characterized and warrant further investigation. This study employed an integrated network pharmacology and molecular docking approach to elucidate the multi-target mechanisms of empagliflozin in CKD. Initial evaluation demonstrated that empagliflozin exhibits favorable physicochemical properties, drug-likeness, and ADMET profiles, supporting its potential as an effective orally administered therapeutic option for CKD management. Network analysis identified 221 shared molecular targets between empagliflozin and CKD-associated genes. Topological analysis of the protein-protein interaction (PPI) network revealed ten critical hub proteins-GAPDH, IL6, EGFR, HSP90AA1, NFKB1, HSP90AB1, MTOR, MAPK3, IL2, and PIK3CA-which serve as key regulators in CKD pathophysiology. Gene Ontology and KEGG pathway enrichment analyses indicated that these shared targets are significantly involved in phosphorylation, signal transduction, and central signaling cascades associated with CKD progression, including the PI3K-Akt, FoxO, HIF-1, and AGE-RAGE pathways. Molecular docking simulations corroborated empagliflozin's multi-target affinity, demonstrating particularly strong binding energies toward HSP90AB1 (-10.85 kcal/mol), MAPK3 (-9.46 kcal/mol), and EGFR (-9.38 kcal/mol). Empagliflozin maintained stable hydrogen bonding throughout the 200-ns molecular dynamics simulation, primarily with GLN18, GLU42, SER45, ASN46, ASN101, GLY130, and TYR134, underscoring its persistent and well-anchored interaction with HSP90AB1. Collectively, these findings provide crucial mechanistic insights, suggesting that empagliflozin might exerts therapeutic effects by modulating interconnected pathways regulating inflammation, oxidative stress, and metabolic homeostasis, thereby reinforcing its role as a comprehensive, multi-target therapeutic strategy for CKD management. Nonetheless, validation through in vitro experiments remains necessary. - Source: PubMed
Publication date: 2026/04/23
Tedasen AmanChatatikun MoragotNetphakdee RatanaHuang Jason CPhongphithakchai Atthaphong - Inflammation plays a critical role in cancer cell proliferation; however, the specific role of inflammasomes, multiprotein complexes that regulate inflammation-associated signaling pathways, in prostate cancer (PCa) remains insufficiently explored. This study aims to characterize the expression of inflammasome-related genes in PCa and evaluate their association with clinical outcomes. - Source: PubMed
Publication date: 2026/05/26
Ghoreifi AlirezaAlshalalfa MohammedDavicioni ElaiSpratt Daniel EJeffrey Karnes RTodd Purves JHughes Francis MMoul Judd WAbern Michael R - Protein chaperones, such as heat shock protein 90 (HSP90), play essential roles in proteostasis by stabilizing client proteins and facilitating proper folding. Evidence for HSP90 function in vision is substantiated by reports of visual disturbances in patients treated with pan-HSP90 inhibitors. Among the cytosolic HSP90 paralogs, loss of HSP90α permits normal photoreceptor development, outer segment morphogenesis, and function, but rods subsequently undergo progressive degeneration despite upregulation of the closely related paralog HSP90β. In contrast, cone function is preserved in the absence of HSP90α, raising the question of whether cytosolic HSP90 paralogs have redundant functions or display functional specialization between rods and cones. To address this question, we generated a conditional knockout of HSP90β (Hsp90ab1), which revealed that loss of HSP90β alone does not disrupt photoreceptor development, morphology, or visual function. In contrast, cone-specific ablation of both cytosolic paralogs resulted in rapid loss of cone function, demonstrating a shared requirement for cytosolic HSP90 activity in cones. To examine potential redundancy during development, we generated mice with targeted deletion of both cytosolic HSP90 paralogs within the photoreceptor lineage. Although retinal lamination was preserved, photoreceptors failed to elaborate outer segments, and visual responses were abolished. The severe visual phenotype correlated with reduced levels of peripherin, a protein essential for outer segment morphogenesis. Together, the findings define stage- and cell type-specific requirements for cytosolic HSP90 paralogs in the retina and establish a central role for cytosolic HSP90 in photoreceptor outer segment development and function. - Source: PubMed
Publication date: 2026/05/24
Aliff Hunter LCrockett Alexis BMunezero DaniellaReid ChyanneBockius Hayley GKuzak Sierra GRhodes ScottSaravanan ThamaraiselviRamamurthy Visvanathan