GRP78 Antibody (OASE00341)
- Known as:
- GRP78 Antibody (OASE00341)
- Catalog number:
- oase00341
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- GRP78 Antibody (OASE00341)
Related genes to: GRP78 Antibody (OASE00341)
- Gene:
- HSPA5 NIH gene
- Name:
- heat shock protein family A (Hsp70) member 5
- Previous symbol:
- GRP78
- Synonyms:
- BiP
- Chromosome:
- 9q33.3
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-26
- Date modifiied:
- 2015-11-19
Related products to: GRP78 Antibody (OASE00341)
Related articles to: GRP78 Antibody (OASE00341)
- HSPA5 is a member of the HSP70 family of heat shock proteins (HSPs) and functions as a chaperone protein within the endoplasmic reticulum (ER). It plays a role in maintaining ER homeostasis, assists in correct protein folding, and triggers the unfolded protein response. Environmental toxins-such as heavy metals, microplastics (MPs), and air pollutants-can cause cellular damage. These toxins can trigger ER stress, resulting in the buildup of proteins that are misfolded or not properly folded, which in turn upregulates HSPA5 expression. Moderate activation of HSPA5 serves as a protective mechanism aimed at restoring protein homeostasis and promoting cell survival; however, sustained and severe ER stress may cause HSPA5 to malfunction, ultimately leading to the activation of the apoptotic pathway and resulting in cell death. Furthermore, HSPA5-mediated mechanisms are closely associated with the prodromal initiation and subsequent escalation of neurodegenerative syndromes. This article focuses on the role of HSPA5 in environmental toxin-induced neurotoxicity and neurodegenerative diseases, with the aim of investigating changes in HSPA5 expression and its regulatory functions in neurotoxicity, thereby providing new strategies for the study of environment-related neurodegenerative diseases. - Source: PubMed
Publication date: 2026/09/21
Wang YurongLv YangZhao RuidongGuo XinGao JingWang TongYao DongmeiLi XinLiu BingchunYuan Jianlong - Deoxynivalenol (DON) is a prevalent mycotoxin that is highly toxic to animals, particularly pigs. Porcine reproductive and respiratory syndrome virus (PRRSV) is a major swine pathogen with high infectivity and severe clinical outcomes, but the mechanisms underlying the host cell responses to co-exposure of DON and PRRSV remain unclear. - Source: PubMed
Publication date: 2026/08/06
Zhang ShaosanMi JiahuiLi MengWang XinkeLi JiaxingZhang DingYang BoSun ZilongNiu Ruiyan - Tumors must adapt to high levels of endoplasmic reticulum (ER) stress to sustain tumor growth and metastases. The chaperone GRP78 (BiP/HSPA5) is a key component of the unfolded protein response (UPR) and essential for ER stress management and adaptive signaling supporting pro-survival UPR activities. Here, we report that oncofetal chondroitin sulfate (CS) glycosaminoglycans are required for ER stress adaptation in osteosarcoma. When osteosarcoma cells encounter ER stress, they upregulate 4-O-sulfated CS at the expense of other glycosaminoglycans leading to a reconfiguration of the glycocalyx in favor of an oncofetal CS subtype. Genetic ablation of the CS synthesis pathway impairs the UPR by preventing osteosarcoma cells from mounting GRP78 expression in response to ER stress. CS deficiency makes osteosarcoma cells hypersensitive to inhibition of GRP78 under both ambient and ER stress conditions, and acute ER stress drives CS-defective osteosarcoma cells into an apoptotic cell death that can be rescued by re-instating CS 4-O-sulfation capacity. This has direct implications for the metastatic progression of osteosarcoma, whereby oncofetal CS protects dissociated osteosarcoma cells from anoikis to allow pulmonary colonization in mice. Our data identify CS glycosaminoglycans as a critical component of the UPR that permits osteosarcoma cells to manage ER stress. - Source: PubMed
Publication date: 2026/08/01
Ørum-Madsen Maj SofiePihl JessicaClausen Thomas MSpliid CharlotteDhez Anne-ChloéZhang Hai-FengChen Yen-HsiVidal-Calvo Elena EthelGustavsson TobiasLizardo MichaelNelepcu IrinaLo JoeyEsko Jeffrey DOo Htoo ZarniDelaidelli AlbertoAgerbæk Mette ØrskovSteinø AnneAl Nakouzi NaderSalanti AliSorensen PoulDaugaard Mads - Intracerebral hemorrhage (ICH) is a devastating neurological disorder characterized by extensive neuronal death, in which ferroptosis has emerged as a central pathological mechanism. Yet, the role of mitophagy in regulating ferroptosis during ICH remains elusive. Herein, we identified a lactylation-mediated HSPA5 (heat shock protein family A (Hsp70) member 5)-VGLL3 (vestigial like family member 3) signaling axis that confers neuroprotection following ICH. We observed a marked upregulation of VGLL3 expression in ICH models, and loss-of-function experiments revealed that VGLL3 silencing exacerbated BNIP3 (BCL2/adenovirus E1B interacting protein 3)-BNIP3L/NIX (BCL2/adenovirus E1B interacting protein 3-like)-mediated, mitophagy-dependent ferroptosis. Mechanistically, VGLL3 enhanced EGLN3 (egl-9 family hypoxia-inducible factor 3) expression and reduced HIF1A/HIF-1α (hypoxia inducible factor 1, alpha subunit) stability, thereby suppressing BNIP3-BNIP3L-driven mitophagy. Upstream, HSPA5 activated VGLL3, and HSPA5 knockdown phenocopied the effects of VGLL3 silencing. Pharmacological activation of HSPA5 with the selective agonist BIP inducer X (BIX) suppressed mitophagy-dependent ferroptosis in cultured neurons, while BIX administration alleviated neuronal death and improved motor function in ICH mice. Epigenetic analyses further demonstrated that HSPA5 expression was transcriptionally modulated by histone H3-Lys18 (H3K18) lactylation, while its non-histone lactylation was catalyzed by the acetyltransferase EP300 (E1A binding protein p300) and removed by the NAD-dependent protein deacetylase SIRT1 (sirtuin 1). Collectively, our findings delineate a lactylation-driven HSPA5-VGLL3-EGLN3-HIF1A/HIF1-1α axis that represses BNIP3-BNIP3L-mediated, mitophagy-dependent ferroptosis. Targeting this pathway may provide a mechanistic rationale and therapeutic strategy for mitigating neuronal injury and functional deficits following ICH. BNIP3: BCL2/adenovirus E1B 19 kDa protein-interacting protein 3; BNIP3L/NIX: BCL2/adenovirus E1B interacting protein 3-like; EGLN3: egl-9 family hypoxia-inducible factor 3; GPX4: glutathione peroxidase 4; GSH: glutathione; GSSG: oxidized glutathione; HIF1A/HIF-1α: hypoxia inducible factor 1, alpha subunit; HSPA5: heat shock protein family A (Hsp70) member 5; IB: immunoblot; ICH: intracerebral hemorrhage; MDA: malondialdehyde; ROS: reactive oxygen species; SLC7A11: solute carrier family 7 member 11; VGLL3: vestigial like family member 3. - Source: PubMed
Publication date: 2026/09/28
QiXiang ZhangQiKai TangBaoFeng WangYiKui LiuYuXiao MaAoQian XuYuXiao XueSun YuHaoBian LiuGuan - Plexin-B1, Plexin-B2, and Plexin-B3 are members of the Plexin-B receptor family, which engage distinct class IV semaphorins as major ligands: Plexin-B1 binds , Plexin-B2 interacts with and , and Plexin-B3 has been reported to bind HSPA5, while all three may participate in non-redundant ligand-receptor networks. Researchers have found receptors associated with neurological and malignant, immune-mediated, and cardiovascular diseases. However, this study strives to provide a comprehensive, cross-disciplinary synthesis of the context-specific functions of Plexin-B family members and to critically evaluate their emerging therapeutic potential across multiple disease domains. In a tumor- and context-dependent manner, Plexin-B1 and Plexin-B2 promote metastasis in glioblastoma, colorectal cancer, and triple-negative breast cancer (TNBC) through RhoA/Rac1-dependent signaling, while Plexin-B3 exhibits dual roles, acting as a tumor suppressor in TNBC under hypoxic conditions yet promoting motility in pancreatic cancer. Plexin-B regulates neuroinflammation in Alzheimer's disease and T-cell regulation in asthma and other cardiovascular diseases via signals. This review positions the Plexin-B family as a promising yet functionally complex target for future precision medicine. - Source: PubMed
Publication date: 2026/09/14
Xu JianliWang NannanLao JunZhang Renwen