Ask about this productRelated genes to: HSP90B1 antibody
- Gene:
- HSP90B1 NIH gene
- Name:
- heat shock protein 90 beta family member 1
- Previous symbol:
- TRA1
- Synonyms:
- GP96, GRP94
- Chromosome:
- 12q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-03
- Date modifiied:
- 2016-10-11
Related products to: HSP90B1 antibody
Related articles to: HSP90B1 antibody
- A strong crosstalk exists between endoplasmic reticulum (ER) stress and synovitis. Beyond their canonical role in protein folding, ER stress chaperones may promote inflammation, cell survival, and fibroblast activation under pathological conditions. This study aimed at localizing and quantifying 11 ER stress proteins (BiP, HYOU1, MANF, PDIA4, GANAB, HSP90B1, TXNDC5, DNAJB11, LMAN1, ERP29, CALR) in human inflamed synovial membranes and at investigating their expression in fibroblast-like synoviocytes (FLS) under ER stress, pro-inflammatory, or pro-fibrotic stimuli. By immunohistochemistry, on a first cohort of formalin-fixed paraffin-embedded (FFPE) biopsies obtained from patients with osteoarthritis (OA), chronic pyrophosphate arthropathy (CPPA), and rheumatoid arthritis (RA), these ER chaperones were primarily localized to the lining in low-grade inflammation (Tak <4) and expanded to the sublining under high inflammatory conditions (Tak ≥4), with a widespread distribution in RA. Imaging mass cytometry, applied to a second cohort of FFPE tissue samples collected from patients diagnosed with OA and RA, revealed the co-expression of ER stress proteins with CD55⁺ FLS in the lining and their progressive infiltration into the sublining along with CD34⁺CD31 FLS during inflammation. These observations were confirmed by immunofluorescence on a larger cohort of OA patients. As inflammation progresses, there is a loss of co-expression with CD55 in the lining, accompanied by a gradual shift towards co-expression with CD34 in the sublining. In vitro, ER stress proteins, particularly BiP, HYOU1, MANF, PDIA4, HSP90B1, LMAN1, CALR, and DNAJB11 are overexpressed in human OA FLS following ER stress, pro-inflammatory or pro-fibrotic stimulation, with BiP, PDIA4, HSP90B1, ERP29, and CALR also being secreted. PDIA4 emerged as a central player: its depletion significantly impaired FLS proliferation and migration, highlighting a direct role in driving synovitis. This study provides the first spatial and functional characterization of ER chaperones in human arthritic synovium, linking ER stress to fibroblast plasticity, inflammation, and fibrosis. - Source: PubMed
Publication date: 2026/08/12
Gendebien ZoéPoulet ChristopheDeroyer CélinePaulissen GenevièveSalpetier PaulineHego AlexandreLefèvre GaëtanCobraiville GaëlNeuville SophiePlener ZeldaDaniel ChristopheThirion ThierrySokolova TatianaDurez PatrickHemon PatriceDelarue YunaMarec NadègeBianchi ElettraDelvenne PhilippeRibbens Cliode Seny Dominique - Deer antler is the only mammalian organ capable of periodic complete regeneration. Its astonishing growth rate-reaching several centimeters per day-provides a unique model for research in tissue regeneration and developmental biology. This rapid growth relies on the protective and signaling functions of the skin, as well as the vigorous proliferation and differentiation capacity of mesenchymal cells. Although previous studies have identified some key factors involved in antler growth, systematically comparing the transcriptomic profiles of these two core tissues (skin and mesenchyme) to identify candidate genes regulating their synergistic growth is crucial for deciphering the molecular mechanisms underlying this "ultra-fast" growth. - Source: PubMed
Publication date: 2026/07/27
Bi XiaodanLiu BingLi BingZhao MeirongTian HuiminChen Jianxing - Poricoic acid A (PAA) is a bioactive triterpenoid from the fungus Poria cocos. Nevertheless, whether it exerts antidepressant-like effects and whether the gut microbiota and immune regulation are involved remain unknown. - Source: PubMed
Publication date: 2026/07/30
Yang JiangweiMa YunLiang ZixinWang ShuihongWang Heqiu - The Notch receptor, GLP-1 , is essential for germline proliferation and early embryonic development. While the cytosolic chaperone HSP-90 promotes GLP-1 signaling in the germline, it is unknown whether the endoplasmic reticulum-resident Hsp90, ENPL-1 (GRP94/endoplasmin), also promotes GLP-1 signaling. We used RNAi knockdown of in a sensitized background to investigate potential genetic interactions. RNAi-mediated knockdown of did not enhance reduced GLP-1 /Notch signaling, and it caused a similar degree of early larval arrest in both wildtype and backgrounds. Thus, we did not detect a role for ENPL-1 in promoting GLP-1 /Notch signaling. - Source: PubMed
Publication date: 2026/07/08
Lissemore James LPancake AmandaFang ShurongMaine Eleanor M - Heat shock proteins (HSPs) can be used as adjuvants to develop therapeutic vaccines, as they enhance the cross-presentation of related tumor antigens and stimulate T cells. In this study, the immunostimulatory properties of gp96 and calreticulin was evaluated to enhance HPV16 E7-based vaccines effectiveness. In silico evaluation was performed to select epitopes from HSPs based on high binding affinity to MHC-I/II, strong immunogenicity, and population coverage. Six novel multiepitope constructs harboring conserved epitopes of E7, gp96, and calreticulin were designed in different orientations. Molecular docking was performed between these constructs and signaling (TLRs) and endocytic (CD14, CD91, LOX-1, and SREC-1) receptors. After determination of an effective construct in molecular docking and MD simulation, prokaryotic expression plasmid containing eight (CTL/HTL) epitopes from HPV16 E7, gp96, and calreticulin in suitable orientation was prepared, and the recombinant multiepitope peptide was generated in E. coli system. Our data showed that the gp96-CRT-E7 construct had superior docking scores with receptors (especially TLR2 and LOX-1), suggesting stronger stimulation of both innate and adaptive immunity than other constructs. It was predicted to be non-toxic, non-allergenic, antigenic, immunogenic, and structurally stable. Moreover, the multiepitope gp96-CRT-E7 fusion peptide was expressed in the Rosetta strain under conditions of OD600: 0.6-0.7, 0.5 mM IPTG, temperature of 18ºC, and 24 hours after IPTG induction, and purified through affinity chromatography under native conditions. Generally, successful results of in silico and expression validation of the multiepitope gp96-CRT-E7 fusion peptide showed its strong potential as a novel candidate for HPV16 vaccine development. - Source: PubMed
Publication date: 2026/07/24
Esmail Nia GitiShahosseini ZahraAkbari ElaheBamehr HadiHeidarnejad FatemehMohsenzadegan MonirehBolhassani AzamFarajollahi Mohammadmorad