Ask about this productRelated genes to: TUBB3 antibody
- Gene:
- TUBB3 NIH gene
- Name:
- tubulin beta 3 class III
- Previous symbol:
- FEOM3
- Synonyms:
- beta-4, CFEOM3, CFEOM3A
- Chromosome:
- 16q24.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-11-22
- Date modifiied:
- 2015-12-17
Related products to: TUBB3 antibody
Related articles to: TUBB3 antibody
- The aim of this research was to use Mebendazole as an anticancer candidate to reduce the dose of Flutamide and reduce its side effects. - Source: PubMed
Fattahi Mohammad RezaTaheri DianaInanloo Seyed HassanMirzaei AkramAzodian Ghajar HeliaReis Leonardo OliveiraAghamir Seyed Mohammad Kazem - 2,4,6-Tribromophenol (TBP) is the most environmentally prevalent bromophenol pollutant. Although TBP tends to accumulate in the brain, its neurotoxic effects and underlying mechanisms remain poorly understood. In the present study, the neurodevelopmental toxicity of TBP was investigated using an in vitro neural differentiation model of mouse embryonic stem cells (mESCs). Results showed that during differentiation, TBP exposure suppressed the expression of the ectoderm marker Tfap2α on day 6. Moreover, after 12 days of exposure, TBP significantly reduced the protein expression levels of PAX6 (neural precursor marker) and TUBB3 (neuronal marker) and inhibited acetylcholinesterase (AChE) activity. TBP exhibited limited effects on canonical developmental signaling pathways, such as BMP, WNT, and Notch-Hes, suggesting that its inhibitory effect on neural differentiation may not depend on these pathways. Transcriptomic analysis revealed TBP-induced alterations in both lipid metabolism-related pathways and genes involved in the mitochondrial respiratory chain. Further biochemical validation experiments demonstrated that TBP upregulated the expression of the lipid uptake gene Cd36, leading to increased total cholesterol (TC) and triglyceride (TG) levels. Concurrently, mitochondrial oxidative stress was elevated, whereas mitochondrial membrane potential, complex I activity, and ATP content were markedly decreased. Therefore, TBP likely impaired neural differentiation by disrupting lipid homeostasis and mitochondrial function. This study enhances the understanding of the neurotoxic mechanisms of bromophenol pollutants and provides crucial scientific evidence for their health risk assessment. - Source: PubMed
Publication date: 2026/08/22
Sun YumiaoPei YaoLiu HuinanGao YurouYang XiaoxiLiu Qian SXu LiFaiola FrancescoZhou QunfangJiang Guibin - Duchenne muscular dystrophy (DMD) cardiomyopathy is characterized by progressive microtubule remodeling, connexin-43 (Cx43) dysregulation, and ventricular arrhythmias. We previously demonstrated phospho-mimic knock-in of βIII-tubulin S172E preserves microtubule organization and attenuates cardiac pathology in mdx mice. However, whether these protective effects can be reproduced using a clinically relevant gene-delivery strategy remains unknown. - Source: PubMed
Publication date: 2026/08/06
Zhou DelongYegneshwaran VasishtAli Nehal KamalGeukgeuzian GeovanniMesa ElamXie Lai-HuaFraidenraich Diego - How aging of human neurons affects dynamics of essential organelle such as mitochondria and autophagosomes remains largely unknown. MicroRNA-induced directly reprogrammed neurons (miNs) derived from adult fibroblasts retain age-associated signatures of the donor, enabling the study of age-dependent features in human neurons, including longitudinal isogenic samples. Transcriptomic analysis revealed that neurons derived from elderly individuals are characterized by gene expression changes associated with the regulation of autophagosomes, lysosomes, and mitochondria, compared to young counterparts. To clarify these changes at the cellular level, we performed live-cell imaging of cellular organelles in miNs from donors of different ages. Older donor miNs exhibit decreased mitochondrial membrane potential, which surprisingly co-occurs with a significant increase in mitochondrial fission and fusion events. We posit that the increased fission and fusion of mitochondria may reflect age-dependent compensation for impaired mitochondrial turnover, perhaps due to changes in macroautophagy/autophagy. We subsequently identified a significant decrease in autophagosome acidification in neurons derived from individuals > 65 years compared to younger donors, and a corresponding age-dependent reduction in neuritic lysosomes resulting in fewer lysosomes available to acidify autophagosomes. This age-dependent deficit in autolysosome flux was rescued by promoting autophagosome generation through TFEB, which also reversed the age-dependent increase in mitochondrial fission and fusion and improved mitochondrial health. Partial organelle recovery occurred after inducing mitophagy or inhibiting mitochondrial fission. Together, this work reveals a mechanism by which aging reduces autophagic flux secondary to a loss of neuritic lysosomes, resulting in mitochondria-intrinsic mechanisms to avoid loss of energy production.: DEG: differentially expressed gene; DMSO: dimethyl sulfoxide; Dox: doxycycline; iPSC: induced pluripotent stem cell; LAMP1: lysosome associated membrane protein 1; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MAPT/tau: microtubule associated protein tau; miNs: microRNA induced neurons; miRNA: microRNA; MMP: mitochondrial membrane potential; PID: post-infection day; RCAN1: regulator of calcineurin 1; TFEB: transcription factor EB; TUBB3: tubulin beta 3 class III; UA: urolithin A. - Source: PubMed
Publication date: 2026/08/23
Klinman EvaKwon Ji-SunDolle Roland EPak Stephen CSilverman Gary APerlmutter David HYoo Andrew S - Following the publication of the above article, a concerned author drew to the authors' attention that, regarding the data showing caspase-3 activity as measured by a colorimetric assay in Fig. 7 on p. 1015, given the use of the MCF‑7 cell line in this study, it was unexpected that the authors would have identified changes in caspase‑3 activity, since it has been demonstrated that MCF‑7 cells do not express caspase‑3 [for example, see the paper by Jänicke and colleagues entitled 'MCF‑7 breast carcinoma cells do not express caspase‑3'. Breast Cancer Res. Treat., vol. 117.1 (2009); p. 219‑221]. In addition, the reader noted that, in the Materials and methods section, it was stated that an Ac-DEVD-pNA-based assay had been used, which has been reported not to be specific for caspase-3, since this assay also reacts to caspase-7 ['Preparation of the caspase-3/-7 substrate Ac-DEVD-pNA via solution-phase peptide synthesis'. Nat Protoc., vol. 5(2) (2010); p. 294-302]. The reader also noted that it was surprising that none of the western blot experiments included in this study actually probed for the presence of the caspase-3 protein, given that the caspase-3 signaling pathway represented one of the principal foci of the study. The authors have been contacted by the Editorial Office to offer an explanation for these apparent anomalies or curiosities in the presentation of the data in this paper, and we are awaiting their response. Owing to the fact that the Editorial Office has been made aware of potential issues surrounding the scientific integrity of this paper, we are issuing an Expression of Concern to notify readers of this potential problem while the Editorial Office continues to investigate this matter further. [Oncology Reports 37: 1011-1019, 2017; DOI: 10.3892/or.2017.5358]. - Source: PubMed
Publication date: 2026/08/14
Yang ZhenhuaLiu YingShi ChangzhengZhang YuqinLv RongzhaoZhang RongWang QianWang Yiming