Ask about this productRelated genes to: CRYAB protein
- 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 protein
Related articles to: CRYAB protein
- Dilated cardiomyopathy (DCM) is a major cause of heart failure in young patients, with a genetic aetiology identified in up to 40% of cases. Variants in **, encoding the small heat shock protein αB-crystallin, are rare but increasingly recognized in inherited cardiomyopathies. - Source: PubMed
Publication date: 2026/04/29
Tran Vy Le - Pathological cardiac hypertrophy is manifested by downregulated PPARα driven metabolic dysregulation which culminates into cardiomyocyte apoptosis. Emerging evidences indicate that additional regulated cell death mechanisms also operate during cardiac pathophysiology. Arjunolic acid (AA) has shown antifibrotic effect via tinkering PPARα. The study investigates the underlying noncanonical role of PPARα agonism by AA in amelioration of cardiomyocyte PANoptosis process during pathological hypertrophy. An integrative approach combining in silico, in vitro and in vivo studies using Wistar rat model to uncover the role of AA driven cardio-protection by regression of PANoptosis signaling mechanism via PPARα agonism. AA driven PPARα agonism does not perturb its canonical function of being a transcription factor as it forms a stable structure with RXR. PPARα agonism in hypertrophied cardiomyocytes by AA, drives a molecular rearrangement within cells in two major ways; by interacting with a molecular chaperon CRYAB to repress IKKα mediated activation of pyroptosis and its sequestration of p300 mediated repression of p53 acetylation driven apoptosis in hypertrophied cardiomyocytes. Additionally, repressed activation of NFκB-p65 by PPARα augmentation effectively reduces ROS accumulation that in turn downregulates activation of MLKL driven necroptotic prowess in diseased cardiomyocytes. The present study provides novel mechanistic insights into the existence of PANoptosis during hypertrophic pathophysiology, that drives the diseased cardiomyocytes in unison towards imminent cell death, which could be mitigated by AA driven PPARα agonism leading to improved cardiac function. - Source: PubMed
Publication date: 2026/05/20
Kar AbhikGupta SoumyadeepSingh GagandeepMatilal ArkapravoRoy SoumikaBag Braja GopalAsthana ShailendraSarkar Sagartirtha - Lumbar spinal stenosis (LSS) caused by hypertrophy of the ligamentum flavum (HLF) is a major cause of lower limb dysfunction; however, its underlying pathogenesis remains unclear. Here we show that metabolic reprogramming and epigenetic modifications synergistically drive HLF progression through a glycolysis-lactylation-fibrosis axis. We demonstrate that HLF tissues exhibit enhanced glycolysis, characterized by elevated extracellular acidification rate, increased ATP production, and upregulated glycolytic enzymes, along with lactate accumulation that positively correlates with tissue thickness. Mass spectrometry identifies CRYAB lysine 92 lactylation (CRYAB_K92la) as a significantly upregulated modification in HLF. Lactylation at CRYAB_K92 promotes fibrosis in human ligamentum flavum cells, whereas the lactylation-blocking mutation CRYAB_K92R attenuates lactate-induced fibrosis and proliferation. Mechanistically, CRYAB_K92 enhances S100A16 transcription, stabilizes S100A16 protein by inhibiting its degradation, and strengthens CRYAB-S100A16 binding, collectively upregulating S100A16 expression. Upregulated S100A16 activates the RAGE signaling pathway, further promoting lactate release and ATP production, thereby forming a positive feedback loop that perpetuates glycolysis, lactate generation, and fibrosis. These findings reveal a novel regulatory axis in HLF pathogenesis and identify CRYAB lactylation, S100A16, and the RAGE pathway as potential therapeutic targets for LSS. - Source: PubMed
Publication date: 2026/05/08
Li JianjunYu ChengCheng JunjieCao YanlinLin TaoNi SongjiaHu KongheDuan Yang - Myocardial fibrosis, a hallmark of heart failure, is driven by pathological crosstalk between stressed cardiomyocytes and activated fibroblasts, yet the initiating signals from cardiomyocytes remain poorly defined. Here, we identify downregulation of casein kinase 2α (CK2α) in cardiomyocytes as a conserved and early trigger of fibrotic remodeling. Cardiomyocyte-specific CK2α loss induces progressive mitochondrial proteome collapse, metabolic reprogramming, and bioenergetic failure. This mitochondrial impairment induces oxidative stress and sterile inflammation, subsequently activating cardiac fibroblasts via paracrine mediators, such as IL-6, thereby establishing a direct mechanistic link between a cardiomyocyte-intrinsic defect and fibroblast activation. Mechanistically, CK2α preserves mitochondrial-cytoskeletal integrity by directly phosphorylating the intermediate filament Desmin at threonine 452 (Thr452). This phosphorylation recruits the chaperone protein αB-crystallin (Cryab) to prevent pathological Desmin aggregation. Disruption of this quality control checkpoint, suffices to recapitulate the full spectrum of mitochondrial dysfunction and pro-fibrotic signaling. Notably, AAV9-mediated restoration of CK2α specifically in cardiomyocytes preserves mitochondrial structure, rescues bioenergetic function, and attenuates fibrosis. Our findings uncover a CK2α-Desmin-mitochondrial quality control axis as a critical metabolic-structural checkpoint in cardiomyocytes and establish that cardiomyocyte-initiated paracrine signaling drives fibroblast activation, highlighting new therapeutic strategies for fibrotic heart disease. - Source: PubMed
Publication date: 2026/05/07
Ma CanjieJia JialiLan JuncongWang JingRao DanRao LanlanZhang WeibinWu DongpengZhang JieWang GangLiu BaohuaAo YingWang Zimei - Gene curation is the analysis of clinical and experimental evidence to determine the strength of relationship between specific genes and diseases. Gene curations allow for improved genetic testing analysis and downstream clinical outcomes. Although variants in crystallin genes are believed to cause about half of all non-syndromic inherited pediatric cataracts, formal gene curations have not been performed. Established and publicly available ClinGen protocols were utilized to perform curations for thirteen crystallin genes to evaluate strength of their associations with pediatric cataracts using published clinical and experimental evidence. Seven genes () scored as Definitively associated with autosomal dominant (AD) inherited pediatric cataracts. Two genes () as Moderate; and four genes have Limited support ( and ). Experimental evidence, when added to clinical evidence, increased the strength of gene-disease relationship for five genes ( from Limited to Definitive, from Moderate to Definitive, CRYGA and from Limited to Moderate and from No Known Disease Relationship (given absence of clinical evidence) to Limited). Optimization and clarification of these gene-disease relationships will improve harmonization of genetic test options (i.e., inclusion on cataract gene panels) and variant interpretation, ultimately allowing for improved clinical care. - Source: PubMed
Publication date: 2026/05/06
Ing AlexanderWeisman Allison GoetschDrackley AndyMcMullen PatrickSkol AndrewLewis FrankEvans BradyYap Kai LeeRathbun PamelaGordon AdamRalay Ranaivo HantaBohnsack Brenda LRossen Jennifer Landau