HSPB8 _ HSP22
- Known as:
- HSPB8 _ HSP22
- Catalog number:
- GTX104815
- Product Quantity:
- 100 µg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- HSPB8 _ HSP22
Related genes to: HSPB8 _ HSP22
- 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 _ HSP22
Related articles to: HSPB8 _ HSP22
- 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 - This study aims to investigate the role of the lncRNA LUCAT1 in cerebral infarction-induced neurological damage. In vitro experiments employed N2a cells to establish an OGD/R model, while in vivo experiments utilized male C57BL/6 mice to construct a MCAO model. Cell viability and apoptosis were assessed via the CCK-8 assay and flow cytometry, respectively. RT-qPCR measured mRNA expression of LUCAT1, miR-337-3p, and HSPB8. The molecular targeting relationship was validated using dual luciferase reporter assays and RNA pull-down experiments. ELISA was used to measure the levels of IL-6, IL-1β, and TNF-α. DCFH-DA fluorescent probes and commercial kits were employed to measure ROS levels, MDA and SOD activity. Neurological function assessment included Longa score, Bederson score, adhesive removal test, and modified neurological severity score. In both OGD/R and MCAO models, LUCAT1 expression was downregulated while miR-337-3p expression was upregulated. LUCAT1 was found to directly bind to miR-337-3p. Under OGD/R conditions, LUCAT1 overexpression enhanced cell viability, inhibited apoptosis, and alleviated inflammation and oxidative stress, with these protective effects being reversed by miR-337-3p overexpression. Animal experiments further confirmed that LUCAT1 overexpression improved neuroinflammation, oxidative stress, and neurological deficits in MCAO mice, an effect that was attenuated by co-expression of miR-337-3p. HSPB8 was identified as a direct target gene of miR-337-3p; inhibition of miR-337-3p exerted protective effects by upregulating HSPB8, whereas HSPB8 knockdown counteracted this protective effect. The long noncoding RNA LUCAT1 exerts neuroprotective effects in cerebral infarction by sponging miR-337-3p and relieving its inhibitory action on HSPB8. - Source: PubMed
Publication date: 2026/05/20
Lei LeiGuo MengnanZou Qixin