HSPB8 antibody
- Known as:
- HSPB8 (anti-)
- Catalog number:
- orb73838
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- HSPB8 antibody
Related genes to: HSPB8 antibody
- Gene:
- HSPB8 NIH gene
- Name:
- heat shock protein family B (small) member 8
- Previous symbol:
- -
- Synonyms:
- H11, E2IG1, HSP22, HspB8, CMT2L
- Chromosome:
- 12q24.23
- Locus Type:
- gene with protein product
- Date approved:
- 2004-01-29
- Date modifiied:
- 2019-04-23
Related products to: HSPB8 antibody
Related articles to: HSPB8 antibody
- Bcl-2-associated athanogene 3 (BAG3) is a mediator of chaperone-assisted selective autophagy, and in the brain, is most highly expressed in astrocytes. However, its role in astrocytes remains poorly defined. Given the genetic and pathological links of BAG3 to proteostasis and neurodegenerative diseases, we investigated how BAG3 contributes to astrocyte function and Alzheimer's disease (AD). To define its function and relevance, we used single-nucleus RNA sequencing to confirm BAG3 enrichment in astrocytes and employed CRISPR/Cas9 editing of human induced pluripotent stem cells followed by proteomic and transcriptomic profiling, which revealed that BAG3 loss caused greater disruption in astrocytes than in neurons. BAG3-deficient astrocytes displayed reduced autophagy, lysosomal abundance and activity, and proteasome function. Coimmunoprecipitation identified BAG3 known binding partners (e.g., HSPB8, proteasome regulators), as well as an interactor in the retromer complex, VPS35. BAG3 deficiency resulted in altered retromer activity as measured by amyloid precursor protein (APP) localization in endosomes. In addition to validating these binding partners, integrative -omics analyses showed that BAG3 regulates AD-relevant proteins (GFAP, BIN1), as well as HSPB8. Functionally, BAG3 knockout astrocytes exhibited impaired amyloid-β proteostasis when cocultured with APP/PSEN1 mutant neurons, directly linking BAG3 to a disease-relevant astrocyte phenotype. Finally, analysis of postmortem human brain revealed that BAG3 expression marks a stress-responsive astrocyte subtype in aged individuals. Together, these findings demonstrate that BAG3 coordinates astrocyte proteostasis through interactions with regulators of autophagy, proteasome activity, and retromer function, positioning it as a potential therapeutic target and central node of astrocytic protein quality control in neurodegeneration. - Source: PubMed
Publication date: 2026/09/28
Augur Zachary MFogo Garrett MBenoit Courtney RKearney Masin ATerzioglu GizemMurphy Zachary RArbery Mason RComandante-Lou NatachaDuong Duc MSeyfried Nicholas TDe Jager Philip LYoung-Pearse Tracy L - Chaperone-assisted selective autophagy (CASA) is a crucial process aimed at maintaining proteostasis in several neurodegenerative diseases associated with protein misfolding, including polyglutamine (polyQ) diseases. Autophagy is a critical lysosome-mediated degradation pathway, particularly essential in neurons, which are highly susceptible to proteotoxic stress due to their post-mitotic nature. Selective autophagy pathways, including CASA, ensure the targeted removal of misfolded proteins and damaged organelles, thereby preserving cellular homeostasis. CASA is based on the intersection of chaperones and autophagy, where HSPB8 and BAG3 interact with HSPA and STUB1 forming a complex that identifies, ubiquitinates, and directs aberrant proteins toward autophagosomes for subsequent lysosomal degradation. In polyQ diseases, such as spinal and bul muscular atrophy (SBMA) and Huntington's disease (HD), mutant proteins accumulate, overwhelming the protein quality control systems. The CASA components are upregulated as a compensatory response, promoting toxic aggregates clearance and cellular damage mitigation. However, chronic proteotoxic stress and progressive impairment of autophagic and lysosomal pathways eventually limit CASA efficiency, contributing to disease progression. The review highlights how CASA exerts its protective activities in polyQ diseases and reports therapeutic strategies aimed at enhancing CASA activity, including pharmacological inducers and combinatorial approaches targeting autophagy and the ubiquitin-proteasome system. Overall, CASA emerges as a crucial adaptive mechanism and a promising therapeutic target in polyQ-related neurodegeneration. - Source: PubMed
Publication date: 2026/09/03
Tedesco BarbaraChierichetti MartaCristofani RiccardoPoletti Angelo - 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 - In the diabetic heart, hyperglycemia can augment the covalent modification of Ca2+-calmodulin-dependent protein kinase II (CaMKII) by O-linked N-acetylglucosamine (O-GlcNAc). Concurrently, mitophagy serves as a crucial link in diabetic myocardial injury. The association between these two processes in diabetic cardiomyopathy remains to be elucidated. - Source: PubMed
Jiang YanjuanHu KaiboLuo ZhaoweiDuan HuiwenQi XinruiZheng XuehongZhang JingZou FangCai XiaNiu LiyanYu PengLai Xiaoyang - Acute ischemic stroke is a major cause of death and disability, yet many patients cannot engage in early rehabilitation due to severe motor deficits. Resulting immobility accelerates muscle atrophy and systemic inflammation, highlighting muscle-brain interactions as potential therapeutic targets. Electrical muscle stimulation (EMS) provides a non-volitional means of activating skeletal muscle and may mimic key neuroprotective features of exercise. We tested whether hyperacute EMS modulates muscle-to-brain signaling to improve stroke outcomes. Transient middle cerebral artery occlusion was induced in male and female C57BL/6 mice, followed by daily neurological assessments and 4 Hz lower-limb EMS for three days. Myofiber morphology, infarct size, blood lactate, and muscle and brain gene expression were subsequently analyzed. EMS preserved myofiber size and reduced stress-response gene expression (Hsp25, Hspb8, Atf4) in skeletal muscle. In the brain, EMS decreased infarct volume, limited necrosis, and improved neurological function. Stroke-associated inflammation was attenuated, evidenced by reduced Tnf, Nlrp3 and Aif1 expression. EMS elevated circulating lactate, while stroke groups showed increased expression of the monocarboxylate transporter Mct-1, supporting a lactate-dependent metabolic coupling mechanism. These findings identify hyperacute EMS as a feasible, noninvasive intervention that confers neuroprotective and anti-inflammatory benefits after stroke, potentially via lactate-mediated muscle-to-brain signaling. EMS may represent a valuable adjunct for patients unable to mobilize during the critical early phase of stroke recovery. - Source: PubMed
Publication date: 2026/06/02
Törteli AnnaKozák PéterUno HiroyukiHősi RajmundRuppert ZsófiaGáspár EszterBari FerencTörök ZsoltFarkas EszterTóth Melinda EMenyhárt Ákos