ATF6 antibody - N-terminal region (ARP31688_P050)
- Known as:
- ATF6 (anti-) - N-terminal region (ARP31688_P050)
- Catalog number:
- arp31688_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- ATF6 antibody - N-terminal region (ARP31688_P050)
Related genes to: ATF6 antibody - N-terminal region (ARP31688_P050)
- Gene:
- ATF6 NIH gene
- Name:
- activating transcription factor 6
- Previous symbol:
- -
- Synonyms:
- ATF6A
- Chromosome:
- 1q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-12-15
- Date modifiied:
- 2015-09-11
Related products to: ATF6 antibody - N-terminal region (ARP31688_P050)
Related articles to: ATF6 antibody - N-terminal region (ARP31688_P050)
- Tramadol (TRM) is a commonly prescribed opioid analgesic; however, accumulating evidence suggests that it may exert toxic effects on vital organs, including the lungs. This study aimed to elucidate the mechanisms underlying TRM-induced lung injury and to investigate the potential protective role of rutin (RUT), a bioactive flavonoid with potent antioxidant and anti-inflammatory properties. In a rat model, lung tissues were analyzed using histopathological examination, biochemical assays for oxidative stress parameters, RT-qPCR for gene expression analysis [nuclear factor E2-related factor 2 (Nrf2), heme oxygenase-1 (HO-1), NAD(P)H:quinone acceptor oxidoreductase 1 (NQO1), nuclear factor kappa B (NF-κB), tumor necrosis factor alpha (TNF-α), inducible nitric oxide synthase (iNOS), Bax, Bcl-2, and Caspase-3], and immunohistochemical (IHC) evaluation of Beclin-1 and 3-nitrotyrosine (3-NT) expression. TRM administration caused severe pulmonary structural alterations, including alveolar collapse, interalveolar septal thickening, inflammatory infiltration, edema, and hemorrhage. These histopathological changes were associated with pronounced oxidative stress, as evidenced by suppressed superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GPx) activities, depletion of glutathione (GSH), increased lipid peroxidation, and disruption of the Nrf2/HO-1/NQO1 antioxidant signaling axis. Furthermore, TRM markedly activated endoplasmic reticulum (ER) stress responses (PERK and ATF-6), upregulated apoptotic markers (Bax and Caspase-3), downregulated Bcl-2 expression, and enhanced autophagy-related Beclin-1 immunoreactivity. In parallel, significant activation of inflammatory and nitrosative pathways was observed, characterized by elevated NF-κB, TNF-α, and iNOS expression and increased nitrotyrosine accumulation. In contrast, RUT treatment substantially ameliorated TRM-induced lung injury by restoring antioxidant capacity, suppressing ER stress-mediated apoptosis and autophagy, and attenuating inflammatory and nitrosative responses. Overall, these findings demonstrate that RUT confers significant protection against TRM-induced pulmonary toxicity through coordinated modulation of oxidative stress, ER stress, apoptosis, autophagy, and inflammation. - Source: PubMed
Publication date: 2026/04/18
Gönen Mustafa ÖnderAkaras NurhanŞimşek HasanKandemir ÖzgeCaglayan CuneytMutlu HüseyinKandemir Fatih Mehmet - The transcription factor ATF6α has a central role in adapting mammalian cells to ER stress via the unfolded protein response (UPR), prompting efforts to identify ATF6α modulators. Here, an unbiased genome-wide CRISPR-Cas9 screen performed in Chinese Hamster Ovary cells revealed that proteolytic processing of the ATF6α precursor to its active form was impaired in cells lacking the ER-resident solute carrier SLC33A1, a transporter previously implicated in acetyl-CoA import, sialylation, and Nε-lysine protein acetylation. Cells lacking SLC33A1 constitutively trafficked the ATF6α to the Golgi but exhibited impaired Golgi processing and activating proteolysis. IRE1α signalling was derepressed by SLC33A1 deficiency consistent with selective loss of ATF6α-mediated negative feedback in the UPR. -deleted cells accumulated unmodified sialylated N-glycans, precursors to acetylated glycans, likely reflecting impaired glycan processing. Deletion of ER-localised acetyltransferases NAT8 and NAT8B, which catalyse protein Nε-lysine acetylation in the secretory pathway, did not replicate the ATF6α processing defects observed in -deficient cells. Together, our findings highlight a role of SLC33A1-mediated metabolite transport in the post-ER ATF6α maturation, linking small-molecule metabolism to branch-specific signalling in the UPR. - Source: PubMed
Publication date: 2026/04/17
George GintoHarding Heather PKay RichardRon DavidOrdoñez Adriana - OPA is an infectious viral disease of sheep. JSRV, which causes the disease, is a slow virus and has oncogenic properties. There are two recognized forms of the disease, classical and atypical. These forms are very important in the prognosis and pathogenicity of the tumor. Although there are many diagnostic, prevalence and pathogenesis studies on the disease, these studies are not enough to explain the ER stress and apoptosis caused by the agent in cells. Therefore, in this study, we investigated the pathogenesis of ER stress and apoptosis in OPA-induced lung tissue. In addition, the differences of these findings between atypical and classical forms of the disease were also determined. For this purpose, 18 lung specimens were used in the study, which were detected by histopathologic, RT-PCR, immunohistochemical (IHC) and immunofluorescence (IF) methods. GRP78, ATF6, ATF4, CHOP, Bcl-2, BAX, and Caspase 3 in all 18 samples by IHC, IF, and Western Blot analysis methods. The atypical form exhibited elevated marker expression, accompanied by reduced Bcl-2 levels compared to the classical form. With these results, it was observed that apoptosis occurred in cells due to the formation of ER stress in OPA infections. In addition, it was determined that the atypical form of the disease caused ER stress more than the classical form and caused more severe apoptosis in cells. - Source: PubMed
Publication date: 2026/04/12
Bolat İsmailBeytut EnverSağlam Yavuz SelimKarakurt EminÇomakli SelimCoşkun NüvitBolat MerveGözegir BerrahIşik Recep - Endoplasmic reticulum (ER) stress is a key cellular mechanism that is important in the development of many diseases, including cancer. Since the discovery of the unfolded protein response (UPR), research has greatly improved our understanding of how ER stress affects cellular functions, especially protein folding and adaptation to stress. The UPR consists of three main branches: IRE1, ATF6, and PERK, each of which is crucial for regulating stress responses, protein homeostasis, and apoptosis. These pathways normally help cells handle stress effectively; however, excessive or prolonged activation can lead to cell death and disease progression. In cancer, ER stress not only shapes the tumor environment but also supports immune evasion, making treatment more challenging. Moreover, ER stress is linked to a wide range of other diseases, including cardiovascular diseases, neurodegenerative disorders, metabolic issues, and autoimmune diseases. ER stress can cause inflammation, protein buildup, and disrupted immune responses in these cases. Targeting the pathways involved in ER stress is a promising therapeutic approach with the potential to reduce disease severity and improve treatment outcomes by restoring cellular balance. The current review systematically integrates current findings on the signaling pathways and regulatory mechanisms of ER stress, examines its role in a wide range of diseases, and explores potential therapeutic strategies aimed at modulating this response. By focusing on the complex relationship between ER stress and different diseases, this investigation aims to guide future research and clinical efforts targeting ER stress-related pathways. - Source: PubMed
Publication date: 2026/04/16
Wei SiyuZhang NanZhang HaoChen ZiguiLi ShuyuWu WantaoLiu ZaoquXia ZhiweiLuo PengCheng Quan - Isoniazid (INZ) is an effective antituberculosis drug; however, its use is associated with nephrotoxicity due to the induction of oxidative stress, inflammation, and apoptosis. This study investigated whether chrysin (CHR), a natural flavonoid with antioxidant and anti-inflammatory properties, could protect against INZ-induced nephrotoxicity in rats. Male Sprague Dawley rats were divided into five groups: Control, INZ, CHR, INZ+CHR25 and INZ+CHR50. Biochemical assays, ELISA, RT-qPCR, Western blot and immunohistochemistry were used to evaluate renal function markers, oxidative stress parameters, inflammatory mediators, survival genes, apoptosis, autophagy and endoplasmic reticulum (ER) stress-associated genes. INZ treatment was found to significantly increase serum urea and creatinine levels, cause glomerular and tubular damage, raise MDA levels, lower antioxidant enzymes (SOD, CAT and GPx) and GSH levels, and suppress Nrf-2, HO-1, SIRT1 and PGC1α. Furthermore, INZ treatment was found to upregulate inflammatory markers (NFκB, STAT3, TNF-α, IL-1β, MAPK and JNK), apoptotic markers (Bax, Bcl2, P53, and P62), components of the PI3K/AKT/mTOR pathway and ER stress/autophagy genes (GRP78, ATF6, PERK, IRE-1α, CHOP and Beclin-1). Co-administration of CHR reversed these alterations in a dose-dependent manner, enhancing antioxidant defenses, attenuating inflammation, apoptosis, autophagy, and ER stress. CHR also reduced kidney injury by increasing nephrin expression and decreasing KIM-1 expression immunohistochemically. These findings suggest that CHR has a nephroprotective effect against INZ-induced renal injury through multi-target molecular mechanisms and demonstrate its potential as an adjunctive therapy to reduce drug-induced nephrotoxicity. - Source: PubMed
Publication date: 2026/04/09
Kandemir ÖzgeKandemir Fatih MehmetKüçükler SefaÇomaklı SelimCaglayan CuneytDalkılınç Elif