Ask about this productRelated genes to: Apaf1 antibody
- Gene:
- APAF1 NIH gene
- Name:
- apoptotic peptidase activating factor 1
- Previous symbol:
- -
- Synonyms:
- CED4, APAF-1
- Chromosome:
- 12q23.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-01-20
- Date modifiied:
- 2016-10-04
Related products to: Apaf1 antibody
Related articles to: Apaf1 antibody
- Atrial fibrillation (AF), the most prevalent form of cardiac arrhythmia, frequently develops as a complication of acute myocardial infarction (MI). Nonetheless, the temporal dynamics of gene expression and key signaling pathways implicated in the development of AF following MI remain elusive. - Source: PubMed
Publication date: 2026/05/05
Zhang Yun-LongChen Tang-NaHe Jia-KangZhu YueWang Xiang-HaiHan Xiao - Neuronal apoptosis is the core pathological mechanism of cerebral ischemic-reperfusion injury (CIRI); although Astragaloside IV (AS-IV) has demonstrated neuroprotective activity against CIRI, its specific molecular mechanisms underlying the regulation of this apoptosis-related pathway remain to be systematically elucidated. We establish an in vivo model of middle cerebral artery occlusion/reperfusion (MCAO/R) in rats and an in vitro model of oxygen-glucose deprivation/reperfusion (OGD/R) in PC12 cells. Six core apoptotic proteins, including CytC, Apaf-1, BAX, Bcl-2, Caspase3, and Caspase9, were detected using neurological function scoring, TTC/HE/Nissl staining, TUNEL staining, Western blot, and immunofluorescence techniques. Molecular docking and molecular dynamics simulation were utilized to analyze the binding affinity between AS-IV and the aforementioned apoptotic proteins. Molecular docking and dynamics simulation demonstrated AS-IV stably binds six core apoptotic proteins, and comparative analysis with target-specific reference ligands identified Apaf-1 as its primary target with the most favorable binding properties. In rat MCAO/R models, AS-IV alleviated neurological deficits, reduced cerebral infarct volume and improved brain pathological damage; in PC12 cell OGD/R models, it decreased neuronal apoptosis. Western blot and immunofluorescence confirmed AS-IV downregulated pro-apoptotic proteins (cytoplasmic CytC, Apaf-1, BAX, cleaved-Caspase9/3) and upregulated anti-apoptotic Bcl-2. This study clarifies the anti-apoptotic molecular mechanism of AS-IV, it alleviates CIRI by targeting the CytC/Apaf-1 mitochondrial apoptotic pathway. - Source: PubMed
Publication date: 2026/03/29
He TongtongZhang ZheZhou XiaohongGao PingLiu ZhenyiZhao YanmengLiang HuaGao WeijuanJin Xiaofei - Apoptosis, a tightly regulated form of programmed cell death, eliminates damaged or malignant cells and is triggered by internal or external stress signals. A critical decision point is mitochondrial outer membrane permeabilization (MOMP), governed by BCL-2 family proteins. Pro-apoptotic members such as BAX and BAK form pores in the mitochondrial outer membrane, releasing intermembrane space proteins like cytochrome c into the cytoplasm. Once cytosolic, cytochrome c binds APAF-1 to form the apoptosome, which activates caspase-9 and subsequently caspase-3, driving apoptosis through cleavage of key cellular substrates. Cytochrome c release serves as a hallmark and point of no return in the apoptotic cascade. However, cytochrome c release can be variable, occurring at submaximal levels or from only a subset of mitochondria, which complicates detection in heterogeneous cell populations. To address this, we developed a semi-automated imaging-based method to quantify cytochrome c release at the single-cell level using immunofluorescence microscopy. Our approach uses CellProfiler, an open-source image analysis platform, to implement a pipeline that segments adherent cells into nuclear, mitochondrial, and cytoplasmic compartments based on compartment-specific reference stains. The pipeline quantifies cytochrome c distribution across these compartments, calculating the ratio of mitochondrially retained to cytoplasmic cytochrome c for each cell. Automation of segmentation and measurement ensures rapid, robust, and reproducible analysis, with only image acquisition and data interpretation performed manually. This method provides a quantitative readout of MOMP and can be readily adapted to any immunofluorescence-detectable protein given an appropriate compartmental marker, expanding its utility for broader cellular studies. - Source: PubMed
Publication date: 2026/03/31
Klötzer FabianStöhr DanielaRehm Markus - Lysine lactylation (Kla) is a metabolite-sensing post-translational modification that bridges cellular metabolism to protein function. Here, we discover that heat stress triggers anaerobic glycolysis and lactate accumulation in brain microvascular endothelial cells. We find that plasma lactate inversely correlates with Glasgow Coma Scale scores in heat stroke patients and predicts poor outcomes. Mechanistically, AARS1 catalyzes the transfer of lactate to HSP90β at lysine 275 (K275). Critically, the lactylation of HSP90β disrupts its interaction with apoptotic protease-activating factor 1 (APAF-1). This modification compromises the protective function of HSP90β, liberating APAF-1 to activate the mitochondrial apoptosis pathway, resulting in blood-brain barrier (BBB) injury. Functional validation reveals that decreasing lactate production or inhibiting AARS1 confers protection. These findings establish HSP90β K275 lactylation as a metabolic switch that modulates protective mechanisms during heat stress-induced cerebrovascular injury. Collectively, our study provides insights into heat stress pathogenesis and identifies potential therapeutic targets for heat-related brain damage. - Source: PubMed
Publication date: 2026/04/27
Wen JiruiZou YuhaoLi CanWang LingLin ZhengdongCheng JuanZhang TianshanHao ZhizhenLiu ShixiWan XuehongYao RongLiu JifengWu Jiang - H5N6 highly pathogenic avian influenza virus (HPAIV) poses a serious threat to both poultry and public health due to its ability to cross species barriers. Although interferon-stimulated genes (ISGs) are key components of the host's antiviral defense, a systematic identification and functional characterization of duck ISGs has not yet been conducted. In this study, we identified 815 potential duck ISGs induced by type II interferon (IFN-γ) in duck embryo fibroblasts (DEFs). The majority of these type II ISGs were enriched in immune-related pathways, including "cytokine-cytokine receptor interaction" and "influenza A". Functional validation using siRNA-mediated knockdown demonstrated that six ISGs, including duIFI35, promote H5N6 AIV replication when silenced. Through TUNEL assay, flow cytometry, and apoptotic pathway analysis, Our analysis revealed that H5N6 AIV infection markedly upregulates apoptotic genes such as Fas, FADD, caspase-8, BAK, cytochrome c, APAF1, caspase-9, and caspase-3 (P < 0.05), thereby promoting apoptosis in DEFs. In investigating the antiviral mechanism of duIFI35, it was found that overexpression of duIFI35 further enhanced H5N6-induced apoptosis, as evidenced by increased transcription of these apoptotic genes, whereas duIFI35 knockdown had the opposite effect. Importantly, the antiviral effect of duIFI35 was significantly diminished upon treatment with the caspase inhibitor Z-VAD-FMK (20 μM) (P < 0.05), indicating that its antiviral activity is mediated through apoptosis induction. Collectively, this study provides the first systematic identification of type II ISGs in ducks and reveals duIFI35-mediated apoptosis as a critical antiviral mechanism, offering foundational insights into ISG-driven innate immunity against AIV in waterfowl. - Source: PubMed
Publication date: 2026/04/16
Zhang TaoYang NaMa LuluXu FengxiangLin XiaobingHuang JiangwuGao FeiLiao MingFeng MinDai Manman