BAG3 antibody
- Known as:
- BAG3 (anti-)
- Catalog number:
- orb101835
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- BAG3 antibody
Related genes to: BAG3 antibody
- Gene:
- BAG3 NIH gene
- Name:
- BCL2 associated athanogene 3
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 10q26.11
- Locus Type:
- gene with protein product
- Date approved:
- 1999-04-23
- Date modifiied:
- 2019-04-23
Related products to: BAG3 antibody
Related articles to: BAG3 antibody
- Microglia are the resident immune cells of the brain and serve as key regulators of innate immune responses within the central nervous system (CNS). The NOD-like receptor family pyrin domain-containing 3 (NLRP3) inflammasome is a multiprotein complex that plays a central role in innate immunity, and its excessive activation contributes to the pathogenesis of neurodegenerative diseases. Nilotinib, a second-generation tyrosine kinase inhibitor, has recently attracted attention due to its neuroprotective and immunomodulatory properties in the CNS. In the present study, we investigated the effects of nilotinib on NLRP3 inflammasome activation, GSDMD/NINJ1-mediated pyroptosis, NF-κB signaling, BAG3-dependent aggrephagy, and ESCRT-III-mediated plasma membrane repair in LPS plus ATP-induced murine N9 microglial cells. Our findings demonstrated that nilotinib significantly attenuated NLRP3 inflammasome activation, as evidenced by reduced NLRP3 expression, decreased caspase-1 activation, and suppressed secretion of proinflammatory cytokines IL-1β and IL-18 through modulation of the IκBα/NF-κB signaling axis. Furthermore, nilotinib markedly inhibited pyroptotic cell death by reducing GSDMD-N and NINJ1 expression, thereby preserving membrane integrity. In parallel, nilotinib enhanced BAG3-dependent selective autophagy and increased LC3B expression, suggesting activation of aggrephagy pathways involved in the clearance of inflammasome-associated components. Notably, nilotinib also restored VPS4A expression, indicating activation of ESCRT-III-mediated plasma membrane repair mechanisms. Collectively, our results reveal that nilotinib exerts a multi-layered regulatory effect on microglial inflammatory responses by suppressing inflammasome activation and pyroptosis while promoting autophagy-dependent clearance and membrane repair pathways. These findings highlight a novel integrative mechanism linking autophagy, pyroptosis, and membrane repair in the neuroprotective actions of nilotinib. - Source: PubMed
Publication date: 2026/08/31
Erdem MehmetErdem ŞenizKarahan Süleyman Caner - Heart failure (HF) has multiple etiologies, but genetic testing remains mainly recommended for selected subgroups with suspected inherited cardiomyopathy. - Source: PubMed
Publication date: 2026/08/26
Lima Isabella RamosLacerda Pires Lucas VieiraCastro E Silva Marcos AraújoMansur Alfredo JPereira Lygia VHünemeier TábitaKrieger José EduardoPereira Alexandre C - Heat shock proteins of the HSP70 family and their BAG co-chaperones regulate responses to oxidative stress, inflammation, apoptosis, and ischemia, all central to coronary artery disease (CAD) pathogenesis. The contribution of genetic variants within HSP70-family and BAG co-chaperone genes to CAD susceptibility remains unclear. Thus, we sought to evaluate associations of HSP70- and BAG-related SNPs with CAD risk and to characterize their potential regulatory effects using comprehensive bioinformatic analyses. A case-control cohort of 834 CAD patients and 1328 controls of Russian ethnicity was genotyped for 13 SNPs. Associations with CAD susceptibility and traits were tested using log-additive regression with adaptive permutation. Loci underwent functional annotation. The C allele of BAG1 rs706121 was associated with increased CAD risk overall (OR = 1.24, p = 0.019), in males (OR = 1.39, p = 0.002), and in smokers (OR = 1.39, p = 0.020). BAG3 rs196329 was associated with lower risk in males (A allele: OR = 0.82, p = 0.040), whereas HSPA6 rs753856 was associated with reduced risk in physically active individuals (G allele: OR = 0.61, p = 0.008). Additional associations involved clinical or biochemical traits. Functional annotation identified potential regulatory effects, including eQTL associations, overlap with histone marks, and allele-dependent changes in transcription factor binding. HSP70 and BAG variants may contribute to CAD susceptibility and support sex- and lifestyle-informed risk assessment. - Source: PubMed
Publication date: 2026/08/15
Polshvedkina OlgaKobzeva KseniaOrlov Yuriy LBushueva Olga - Protein quality control is critical for maintaining sarcomere structure and function in cardiomyocytes. Mutations in protein quality control pathway proteins, namely, CRYAB-R120G (arginine to glycine at position 120) and BAG3-P209L (proline to lysine at position 209), induce protein aggregates and cardiomyopathy in humans. Novel observations in yeast demonstrate mitochondrial uptake of cytosolic protein aggregates. We hypothesized that mitochondrial uptake of cytosolic protein aggregates, and their removal by mitophagy, a lysosomal degradative pathway, facilitates cytosolic protein quality control in cardiomyocytes. - Source: PubMed
Publication date: 2026/08/26
Rawnsley David RIslam MoydulZhao ChenGuan XuminKargar Gaz Kooh YasamanMendoza AdelitaNavid HonoraKumari MinuPandi PhalgunMurphy John TNigro JessKovacs AttilaGreenberg LinaMani KartikGreenberg MichaelHuebsch NathanielMa XiucuiDiwan Abhinav - Heat shock protein family B member 8 (HSPB8) is a chaperone involved in the chaperone-assisted selective autophagy (CASA) complex. HSPB8 in conjunction with cochaperone BAG3, promotes autophagy-mediated removal of misfolded proteins associated with various neurodegenerative diseases. Mutations in , previously associated with Charcot Marie Tooth disease type 2L, have recently been linked to an autosomal dominant rimmed vacuolar myopathy (MFM13), and is considered a multisystem proteinopathy. Patients have distal and proximal limb girdle myopathy with muscle biopsy showing fatty replacement, endomysial fibrosis, and rimmed vacuoles leading to muscle atrophy and early demise. We have demonstrated reduced expression of HSPB8, altered autophagy and TDP-43 accumulation in patient fibroblasts. Using CRISPR technology, we generated a knock-in 8 mouse model of the c.515dupC hot spot frameshift variant to study disease pathology. Overexpressed murine frameshift mutant (c.515dupC, fs) displays insolubility and aggregation propensity in Murine Neuroblastoma X Spinal Cord 34 (NSC-34) cells. Mutant mice developed late-onset muscle weakness beginning at 15 months. Muscle biochemical analyses revealed reduced HSPB8 levels, increased TDP-43, and altered autophagy markers, partially recapitulating the human phenotype. Fiber type analysis, neuromuscular junction integrity, and motor neurons show mild myopathy without neurodegeneration. Given the lack of available treatments, we evaluated trehalose, a natural disaccharide that induces HSPB8 and enhances autophagy. Administration of 2% trehalose in drinking water improves motor performance, restores HSPB8 expression, and ameliorates autophagic and TDP-43 pathology in mutant mice. These findings support the value of our preclinical models for translational studies, and autophagy enhancement as a potential therapeutic strategy for HSPB8-related myopathy. - Source: PubMed
Publication date: 2026/08/09
Shmara AlyaaWeiss LanGromova AnastasiaTedesco BarbaraPal PallabiKostalnick GenieBoock VictoriaBassett ElizabethParera SebastianCheng ChengTa LacLee JonathanPanchagatti ArjunMohanty EshaneeVu JillianLa Spada Albert RPoletti AngeloKimonis Virginia