Ask about this productRelated genes to: PTBP1 Blocking Peptide
- Gene:
- PTBP1 NIH gene
- Name:
- polypyrimidine tract binding protein 1
- Previous symbol:
- PTB
- Synonyms:
- HNRPI, HNRNP-I, PTB2, PTB3, PTB-1, PTB4, pPTB
- Chromosome:
- 19p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1992-06-29
- Date modifiied:
- 2015-03-26
Related products to: PTBP1 Blocking Peptide
Related articles to: PTBP1 Blocking Peptide
- Osteoporosis is characterized by disrupted bone homeostasis while dysregulated autophagy contributes to impaired bone remodeling and bone loss. This study investigates the role of the RNA-binding protein polypyrimidine tract binding protein 1 (PTBP1) in osteoporosis progression through regulation of protein kinase C zeta (PRKCZ), and elucidates whether PTBP1 modulates the osteogenic-adipogenic fate commitment of bone marrow mesenchymal stem cells (BMSCs) via autophagy. - Source: PubMed
Publication date: 2026/08/12
Wang ChenSun JianDong Meng - The L-type calcium channel Ca1.2 serves as a core trigger for excitation-contraction and excitation-transcription coupling in cardiovascular cells. Its abnormalities are closely linked to multiple cardiovascular diseases, including hypertension, arrhythmias, and cardiac hypertrophy. Alternative splicing (AS) generates Ca1.2 channel isoforms with distinct electrophysiological properties and drug sensitivity, finely tuning channel functions. This review systematically summarizes AS regulation and pathological significance of Ca1.2 in the cardiovascular system. Three key splicing events, mutually exclusive exons 8/8a, cassette exon 9* and exon 33, impact channel gating, calcium influx, and drug responsiveness. These AS events are dynamically regulated by splicing factors such as Rbfox1/2, PTBP1, and RBM20. We further analyze aberrant Ca1.2 splicing in hypertension, heart failure, myocardial infarction, and diabetic cardiomyopathy. Finally, we discuss preclinical and clinical advances of antisense oligonucleotides for treating cardiovascular Ca1.2 channelopathies. This review aims to clarify the regulatory network of Ca1.2 AS, providing theoretical evidence for precision therapies based on splicing modulation. - Source: PubMed
Publication date: 2026/08/12
Wang ChenhaoQin KehanWang Juejin - Cancer cells preferentially rely on aerobic glycolysis, known as the Warburg effect, to support growth and survival. We previously demonstrated that polypyrimidine tract-binding protein 1 (PTBP1) maintains PKM2 dominance by regulating pyruvate kinase isoform splicing, sustaining the Warburg phenotype. PTBP1 suppression shifts metabolism toward PKM1 dominance, enhancing oxidative phosphorylation, reactive oxygen species (ROS) production, apoptosis, and antitumor immunity. Thirteen chemically modified siR-PTBP1 derivatives targeting either the coding region or the 3'-untranslated region (3'-UTR) of PTBP1 mRNA were synthesized and evaluated in colorectal cancer cell lines. Cytotoxicity, protein expression, oxidative stress, and metabolic alterations were assessed using cell-based assays, immunoblotting, and metabolomic analysis. siRNA stability was evaluated following nuclease exposure and quantified by TaqMan RT-qPCR. siRNAs targeting the 3'-UTR more effectively suppressed PTBP1 expression and increased the PKM1/PKM2 ratio than coding-region-targeting siRNAs. Among them, derivative 2-6 showed the strongest cytotoxicity with oxidative stress and apoptosis. Metabolomic profiling demonstrated altered glycolytic flux and preserved pentose phosphate pathway intermediates with activated redox responses, while adenylate and guanylate energy charges remained viable, indicating metabolic stress without energy collapse. Tricarboxylic acid cycle metabolites were elevated, consistent with enhanced oxidative phosphorylation. Derivative 2-6 showed resistance to nuclease-mediated degradation. Direct PKM2 knockdown did not induce comparable cytotoxicity. Chemically modified siR-PTBP1, particularly derivative 2-6, induces a metabolically vulnerable state characterized by oxidative imbalance, leading to apoptosis. These findings identify PTBP1 as a key regulator of the Warburg effect and support siRNA-based metabolic targeting as a therapeutic strategy. - Source: PubMed
Publication date: 2026/08/10
Matsumoto KeitaHayashi HirokatsuTokumaru YoshihisaFujibayashi SeitoMitsui NorikiEndo MasahideHoraguchi TakeshiHatanaka YujiYokoi RyomaMizutani ChikaKuno MasashiFukada MasahiroAsai RyuichiYasufuku ItaruSato YutaTajima Jesse YuTanaka YoshihiroNakashima RemiAkao YukihiroMatsuhashi Nobuhisa - Glioblastoma (GBM), the most common and aggressive primary brain tumor, exhibits profound metabolic reprograming that sustains its progression and therapy resistance. Our previously published work demonstrated that C3G expression is downregulated in GBM, which enhances migration and invasion. Here, we show that C3G silencing or knockout in GBM cells reprograms glucose metabolism favoring glycolysis and lactate production through upregulation of PKM2 and LDHA. Furthermore, Seahorse metabolic profiling further revealed increased respiratory capacity and glycolysis upon C3G downregulation or depletion. Mechanistically, C3G silencing increases the levels of the splicing factor PTBP1, which forces splicing towards PKM2 expression as demonstrated by transient PTBP1 silencing, although other splicing factors such as SRSF3 could also contribute to PKM2 expression. Additionally, C3G downregulation or depletion enhances sphere formation, stemness and tumor initiating capacity in GBM cells, which is rescued by C3G re-expression in C3G knockout GBM cells. This enhanced stemness induced by C3G silencing in GBM cells is prevented by transient PTBP1 or PKM2 silencing or pharmacological inhibition of PKM2 with compound 3K, which also decreases cell viability within the spheres (3D-cell cultures) and the expression of stemness markers. However, in 2D-cell cultures compound 3K increases cell viability in C3G-silenced GBM cells, while decreasing that of C3G knockout cells. This supports a specific role for C3G/PKM2 axis in GBM cancer stem cells through mechanisms likely dependent on both PKM2-mediated metabolic reprogramming and nuclear effects on gene transcription. Altogether, our findings identify C3G as a novel regulator of GBM metabolism and stemness acting through PKM2, unveiling new potential diagnostic and therapeutic implications for C3G in a subset of GBM patients. - Source: PubMed
Publication date: 2026/07/01
Cueto-Remacha MateoManzano SaraIniesta-González MinervaMancebo JaimeMartin-Serna PaulaPalao NereaBaquero CristinaLópez-Pastor Andrea RPeralbo-Avilés CristinaGutierrez-Uzquiza AlvaroCuesta Ángel MBragado PalomaGuerrero CarmenPorras Almudena - Autism spectrum disorder (ASD) is associated with immune and inflammatory dysregulation. However, the molecular networks linking peripheral immune signatures to neuroinflammatory processes remain poorly understood. This study aimed to explore inflammation-related molecular pathways in ASD through integrated transcriptomic network analysis and to validate key cytokine genes (IL6, IL10, IL17, NF-κB1) using quantitative real-time polymerase chain reaction (qRT-PCR). - Source: PubMed
Publication date: 2025/12/27
Najim Abed Al-Saadi YoosraBasim Mohammed ZainabAbdulkareem Abdoun MithalMahmoudi Ali