Ask about this productRelated genes to: CRYAB antibody
- Gene:
- CRYAB NIH gene
- Name:
- crystallin alpha B
- Previous symbol:
- CRYA2
- Synonyms:
- HSPB5
- Chromosome:
- 11q23.1
- Locus Type:
- gene with protein product
- Date approved:
- 1987-09-11
- Date modifiied:
- 2019-04-23
Related products to: CRYAB antibody
Related articles to: CRYAB antibody
- This study investigates the molecular mechanism by which SPI1 inhibits ferroptosis and immune escape in bladder cancer (BC) through upregulation of CRYAB expression. Bioinformatics was utilized to screen BC-related prognostic genes and their upstream regulators. RT-qPCR and Western blot (WB) were conducted to assess SPI1 and CRYAB expression in BC cells. CRYAB knockdown and SPI1/CRYAB overexpression were performed to explore their effects on cellular behaviors. Malignant phenotypes were evaluated through CCK-8, colony formation, scratch assays, and Annexin V-FITC/PI staining. Ferroptosis was assessed using Fe²⁺ and JC-1 staining, alongside biochemical analysis. THP-1 monocytes were differentiated into macrophages and co-cultured with BC cells; WB was performed to measure M2 macrophage polarization markers (CD86/CD206). T cell cytotoxicity assays were performed using activated CD3 T cells from healthy donors co-cultured with BC cells to directly assess immune evasion. Dual-luciferase and ChIP-qPCR assays were used to explore the transcriptional regulation of CRYAB by SPI1. A xenograft mouse model was established to examine BC cell growth and immune escape in vivo. Bioinformatics identified CRYAB and SPI1 as key regulators in BC. Both were highly expressed in BC cells. CRYAB knockdown promoted ferroptosis and inhibited malignant behaviors of BC cells, and suppressed epithelial-mesenchymal transition (EMT) and M2 macrophage polarization in co-culture systems. Furthermore, CRYAB or SPI1 knockdown sensitized BC cells to T cell-mediated killing and enhanced T cell effector molecule production (IFN-γ, TNF-α, Granzyme B), whereas CRYAB overexpression reversed the effect of SPI1 knockdown. Dual-luciferase and ChIP-qPCR assays confirmed that SPI1 directly transcriptionally regulates CRYAB. SPI1 knockdown enhanced ferroptosis, inhibited EMT, and suppressed immune escape in BC cells, effects that were reversed by CRYAB overexpression. SPI1 inhibits ferroptosis and immune escape in BC by promoting CRYAB expression, thereby facilitating BC progression. These findings provide new theoretical insights and potential therapeutic strategies to improve the prognosis of BC patients. - Source: PubMed
Publication date: 2026/04/22
Chen HaoYang GuanglinWei LiweiCui ZelinZhao QiyueMo QizhouWen JianhuaYang ShuboYu JiayinHuang YichenTan ShutingQin MinCheng Jiwen - This study used proteomic analysis to evaluate how four cooking methods impact the quality of beef from Rikaze humped cattle. Conventional boiling, high-pressure boiling, roasting and frying produced varying numbers of differentially abundant proteins (DAPs) in and hind leg beef samples compared to the raw meat. Principal component analysis, hierarchical clustering and correlation analysis revealed 11 and 18 proteins significantly associated with meat tenderness and colour, respectively. Myosin heavy chain 7 (MYH7), myosin light chain 2 (MYL2) and myosin light chain 6B (MYL6B), involved in the sarcomere (GO:0030017) and cardiac muscle contraction (map04260) pathways were negatively correlated with tenderness, indicating that their decreased abundance contributes to improved tenderness after cooking. The cytoskeletal protein α-crystallin B chain (CRYAB) showed a positive correlation with shear force, suggesting a role in toughness. PGAM2, ALDOA and PKM, participating in ADP metabolism (GO:0046031) and glycolysis (map00010), influenced meat texture, while glycolytic enzymes ALDOA, CKM and PKM promoted changes in lightness (*). MYBPC2 and VDAC2 were negatively correlated with *. EEF1G, PGP, PPIA and PRDX2 were negatively correlated with redness (*), and DES was positively correlated with yellowness (*). Overall, wet-heat cooking altered mainly skeletal, heat-shock and cytoskeletal proteins and enhanced tenderness, while proteins related to energy metabolism and oxidative stress were closely linked to colour development. These key proteins could serve as potential biomarkers for predicting the eating quality of humped cattle beef and provide a basis for the development of high-value beef products. - Source: PubMed
Publication date: 2026/04/15
Zheng HaoZhao XiaolongLi JingWang PingLi SiminLi LiangLiu Zhendong - Benzo(a)pyrene (BaP), an environmental carcinogen, contributes to colon cancer pathogenesis through incompletely elucidated mechanisms. This study integrated network toxicology and multi-omics analyses to decipher BaP-associated molecular signatures and clinical relevance in colon cancer. Using TCGA-COAD data, 113 differentially expressed BaP-related targets were identified via CTD and Super-PRED databases. PPI networks, functional enrichment, and Cox/Lasso regression revealed key pathways (xenobiotic metabolism, p53 signaling, cell cycle) and six prognostic genes (CLK2, CRYAB, RPS6KA1, DPP7, CDC25C, GAST). A BaP-related risk model stratified patients into distinct survival groups. A nomogram accurately predicted 1-, 3-, and 5-year overall survival. High-risk scores correlated with advanced tumor stage, metastasis, and immunosuppressive microenvironments. Molecular docking demonstrated strong BaP binding to CLK2 and CRYAB. External validation (GSE39582, TNMplot) confirmed tumor-specific gene expression patterns. These findings delineate BaP-driven networks connecting xenobiotic stress, immune dysregulation, and tumor progression. The risk model provides a prognostic biomarker for personalized management and therapeutic targeting in colon cancer. - Source: PubMed
Publication date: 2026/04/22
Yang XueyingYang ZhendongSui Bowen - Mutations in the small heat shock protein α-crystallin B (CryAB) result in cataracts, cardiomyopathies, and myofibrillar myopathies (MFMs), all of which are marked by protein aggregation. To investigate pathological mechanisms, we expressed four human CryAB disease alleles in skeletal muscle. All variants resulted in the accumulation of protein aggregates. Mutations within the conserved α-crystallin domain (ACD) caused CryAB-positive structures that colocalized with an amyloidogenic form of human Desmin. The amyloid-like nature of these CryAB variants was further supported by thioflavin T spectroscopy and Congo red staining, the latter of which was also evident in other MFM-causing genes in zebrafish muscles and human biopsies. Muscle-enriched CryAB amyloid-like structures co-localized with extracellular vesicle (EV) markers and were detected in the hemolymph, suggesting an EV-mediated export mechanism. This is the first report of CryAB amyloid formation in skeletal muscle and broadens amyloid dynamics beyond the nervous system. - Source: PubMed
Publication date: 2026/03/21
Zhao ZiweiLim Hui-YingCannone ElenaMarchetto GiuliaSchiavone MarcoVattemi GaetanoGuo YunguiWang Zong-HengGlancy BrianGeisbrecht Erika R - Polyhydramnios, Megalencephaly, and Symptomatic Epilepsy syndrome (PMSE/STRADA-related disorder) is a rare neurodevelopmental disorder characterized by megalencephaly (ME), early-onset drug-resistant epilepsy, neurocognitive impairment, and high early mortality, often due to status epilepticus. PMSE is caused by a multi-exon deletion in , encoding STRADA, which regulates the mechanistic target of rapamycin (mTOR) pathway. GABAergic inhibitory interneurons (INs) critically modulate the excitatory:inhibitory balance in cortical and hippocampal networks, and IN deficits contribute to epileptogenesis in several epileptic encephalopathies. However, no studies have investigated INs in PMSE. We used a multimodal approach to study INs in a mouse model engineered with the same causative 5-exon deletion identified in human PMSE. We demonstrate that / loss causes a reduction of INs in the somatosensory cortex and a corresponding increase in the striatum, representative of remnant ganglionic eminence progenitor origin, in -/- mice and a single PMSE brain tissue specimen. RNA sequencing comparing wildtype to -/- cortex and striatum corroborated these findings, revealing increased IN-related gene expression (e.g., ) in the striatum and decreased IN-related gene expression (e.g., ) in the developing cortex. Cytoskeletal (e.g., , , ) and mTOR-associated genes (e.g., , ) are differentially expressed in the developing cortex, mature striatum, and mature cortex of mice. Functional validation confirmed enlarged INs in mouse and human / -deficient brain and enhanced S6 phosphorylation in striatum. Together, these findings suggest / loss contributes to failed IN migration - the first such report in a developmental, mTOR-associated megalencephaly syndrome - highlighting INs as a therapeutic target for seizure prevention in PMSE. - Source: PubMed
Publication date: 2026/04/01
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