Ask about this productRelated genes to: RIPK1 antibody
- Gene:
- RIPK1 NIH gene
- Name:
- receptor interacting serine/threonine kinase 1
- Previous symbol:
- -
- Synonyms:
- RIP
- Chromosome:
- 6p25.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-05-07
- Date modifiied:
- 2015-11-17
Related products to: RIPK1 antibody
Related articles to: RIPK1 antibody
- Necroptosis is a regulated inflammatory form of programmed cell death mediated by , , and , but its clinical relevance in surgically resected non-small cell lung cancer (NSCLC) remains uncertain. This study evaluated the transcript-level expression of these genes and their associations with survival in 41 patients who underwent complete NSCLC resection without preoperative therapy. RNA was isolated from frozen tumor tissues, and mRNA expression was quantified using RT-qPCR. Expression was analyzed primarily as continuous log(expression + 1)-transformed variables in Cox proportional hazards models; median-based groups were used only for exploratory Kaplan-Meier visualization. The cohort comprised 34 males and 7 females, with a mean age of 61.0 years; 41.5% had adenocarcinoma and 58.5% had squamous cell carcinoma. The maximum follow-up was 145 months, and the 5-year overall survival rate was 46.3%. None of the three genes was significantly associated with overall or disease-free survival in either univariable or restricted adjusted Cox models. Median-based analyses similarly showed no significant survival differences. These findings do not support , , or transcript levels as standalone prognostic biomarkers in surgically resected NSCLC. Larger studies integrating transcriptomic, protein-level, and functional assessments are warranted. - Source: PubMed
Publication date: 2026/09/19
Ulugun Fatma IlknurYavuzşen TuğbaAktaş SafiyeAltun Zekiye SultanÖzdemir NezihÖmeroğlu Şimşek GökçenGürel DuyguBaran BurçinArayici Mehmet Emin - Garambullo (Myrtillocactus geometrizans) is a Mexican wild fruit rich in phytochemicals. In this study, freeze-dried garambullo was subjected to in vitro gastrointestinal digestion and fermentation. The resulting fermented extract of garambullo (FEG) was evaluated for its effects on cell viability in HT-29 and SW480 CRC cell lines using MTT assays. After 24 h of treatment, FEG exhibited IC values of 2985 μg/mL and 3200 μg/mL in HT-29 and SW480 cells, respectively, indicating a significant reduction in cell viability compared to the control group. This reduction was further confirmed by flow cytometry, which revealed increased late apoptosis and necrosis in HT-29 cells, and a pronounced increase of necrosis in SW480 cells treated with FEG. Molecular docking simulations further supported these findings, demonstrating that butyric acid, a metabolite identified in FEG, demonstrates energetically favorable interactions with Caspase-3 (ΔG: -5.41 kcal/mol) and RIPK1 (ΔG: -5.18 kcal/mol), suggesting potential multi-pathway involvement in apoptotic and necrosis-associated cell death. Furthermore, the colony-forming ability of these CRC cell lines was assessed using 3D culture assays. After 14 days, FEG reduced colony formation in SW480 cells, with complete suppression observed at 149 μg/mL. Notably, HT-29 cells exhibited greater sensitivity, as no colonies were detected at any of the tested concentrations (≥37 μg/mL). These findings indicate that FEG exerts significant anti-proliferative, proapoptotic, and anti-clonogenic effects in CRC cell lines, supporting its potential as a candidate for further investigation in therapeutic or preventive strategies. - Source: PubMed
Soledad López-Alvarez GuadalupeYareli Gutierrez-Silerio GloriaPablo García-SolísRocio Morales-BárcenasYesennia Sánchez-PérezGabriela Hernández-Puga AnaAzeneth Vergara-Castañeda Haydé - Tumor Necrosis Factor (TNF) is a key pro-inflammatory cytokine whose sensing by TNFR1 triggers gene activation or cell death induction. While TNF cytotoxicity can be beneficial during infections by supporting effective immune responses, its chronic or excessive induction is harmful and promotes inflammatory pathologies. Protective brakes, known as cell death checkpoints, normally repress TNF cytotoxicity and therefore constitute crucial safeguards against these diseases. Death by TNF mainly proceeds upon inactivation of a checkpoint by microbial effector proteins or pathological mutations. We previously identified lysosomal turnover of TNFR1 Complex II by TAX1BP1-mediated selective macro-autophagy as a brake on TNF cytotoxicity. Here, we propose an alternative mechanism that prevents TNF-induced RIPK1 kinase-independent apoptosis. We found that inhibiting the ESCRT machinery, HSC70 or TAX1BP1 interferes with the TNF-dependent targeting of activated CASPASE-8 into endosomal intralumenal vesicles (ILVs) and is associated with apoptosis induction. Furthermore, we identified TAX1BP1 and TNFR1 Complex II components as TNF-induced cargoes of extracellular vesicles, suggesting that exosomal release of TNFR1 Complex II serves as a parallel detoxification pathway to lysosomal turnover. Finally, we show that Salmonella Typhimurium and Mycobacterium tuberculosis effector proteins activate TNF cytotoxicity by inhibiting components of the ESCRT machinery involved in this detoxification process. - Source: PubMed
Publication date: 2026/08/25
Huyghe JonPriem DarioHaems AnneloreLippens LienDe Meyer MargauxDelanghe TomDondelinger YvesBruggeman IngeVandenabeele PeterEyckerman SvenHendrix AnBertrand Mathieu Jm - Alzheimer's disease is a multifactorial neurodegenerative disorder in which amyloid-β accumulation, tau pathology, neuroinflammation, synaptic dysfunction, vascular injury, and neuronal loss interact across multiple cellular compartments. Although amyloid and tau remain central to disease definition and biomarker staging, growing evidence indicates that inflammatory and regulated cell-death pathways actively shape disease progression. Receptor-interacting protein kinase 1 (RIPK1) has emerged as a context-dependent signaling checkpoint that links inflammatory signaling to cell-fate decisions. In its scaffold and ubiquitinated forms, RIPK1 supports TNFR1-associated NF-κB and MAPK signaling, whereas RIPK1 kinase activation can promote apoptosis and RIPK1-RIPK3-MLKL-dependent necroptosis when regulatory checkpoints fail. In Alzheimer's disease, RIPK1 signaling has been implicated in disease-associated microglial responses, impaired amyloid-β handling, astrocyte reactivity, tau-associated neuronal stress, neurovascular dysfunction, and necroptotic cell death. Here, we review the molecular regulation of RIPK1; evaluate evidence from human tissue, experimental models, and cellular systems; and discuss how RIPK1 may function as a convergence and amplification node linking amyloid-β, tau, neuroinflammation, and regulated cell death. We also examine the therapeutic rationale for targeting RIPK1, including CNS-penetrant inhibitors, biomarker challenges, timing of intervention, patient selection, and safety considerations. We propose that RIPK1 is an understudied pathway in Alzheimer's disease pathogenesis and that defining its cell-type-specific and stage-dependent functions will be essential to determine whether RIPK1 inhibition can be developed as a disease-modifying therapeutic strategy. - Source: PubMed
Publication date: 2026/09/18
Caccamo AntonellaLanza MarikaCasili GiovannaOddo Salvatore - Necroptosis is a regulated form of lytic cell death that plays important roles in inflammation, host defense, and disease. Central to this pathway is mixed lineage kinase domain-like protein (MLKL), the terminal effector responsible for membrane disruption. Upon phosphorylation by receptor-interacting protein kinase 3 (RIPK3), MLKL undergoes conformational changes, oligomerizes, and translocates to cellular membranes. Despite extensive study, however, the detailed molecular mechanism by which MLKL mediates necroptosis remains incompletely understood. Multiple models have been proposed, including pore formation, cation channel activity, and higher-order or amyloid-like assemblies, yet each is supported by limited and often indirect evidence. Notably, high-resolution structures of membrane-associated, active MLKL assemblies are still lacking, hindering a unified mechanistic understanding. In addition, emerging studies suggest that membrane permeabilization and terminal membrane rupture may be mechanistically distinct processes, potentially involving additional effectors such as SIGLEC12. In this review, we summarize current structural and mechanistic insights into MLKL, including its domain architecture, activation mechanisms, and species-specific divergence. We then evaluate competing models of MLKL-mediated membrane disruption and highlight key challenges and future directions. We emphasize the need to directly visualize the active, oligomeric MLKL assemblies in the membrane-bound state and to integrate structural, biochemical, and cellular approaches for a comprehensive understanding of MLKL-mediated membrane permeabilization. Resolving these questions will be essential for understanding necroptosis and for developing therapeutic strategies targeting MLKL-mediated cell death. - Source: PubMed
Publication date: 2026/09/23
Dreyer BrookeRuan Jianbin