BNIP3L antibody
- Known as:
- BNIP3L (anti-)
- Catalog number:
- orb101642
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- BNIP3L antibody
Related genes to: BNIP3L antibody
- Gene:
- BNIP3L NIH gene
- Name:
- BCL2 interacting protein 3 like
- Previous symbol:
- -
- Synonyms:
- Nix, BNIP3a
- Chromosome:
- 8p21.2
- Locus Type:
- gene with protein product
- Date approved:
- 1997-07-01
- Date modifiied:
- 2018-04-18
Related products to: BNIP3L antibody
Related articles to: BNIP3L antibody
- Sepsis-induced myocardial injury is a critical condition with limited therapeutic options. This study investigates the therapeutic potential of mesenchymal stem cell (MSC)-derived small extracellular vesicles (MEx) in lipopolysaccharide (LPS)-induced myocardial injury in rat model and explores the underlying molecular mechanisms. We established a sepsis model using LPS and treated it with Mex, which were isolated and loaded with microRNA-23a-3p mimics (MEx-miR-23a-3p). Our findings demonstrate that MEx-miR-23a-3p significantly reduces LPS-induced secretion of B-type natriuretic peptide (BNP), cardiac troponin T (cTnT), tumor necrosis factor-α (TNF-α), interleukin-1β (IL-1β), and interleukin-6 (IL-6) in H9C2 cells and rat serum. Furthermore, MEx-miR-23a-3p attenuates LPS-mediated proliferation impairment, apoptosis, and fibrosis in cardiomyocytes, and enhances migration and tube formation capacity in LPS-injured rat vascular endothelial cells. Notably, the protective role of MEx-miR-23a-3p against LPS-induced cardiomyocyte dysfunction was abolished upon pretreatment with GW4869, an inhibitor of exosome biogenesis and release. Mechanistically, miR-23a-3p directly binds to the 3' untranslated region of BNIP3L mRNA, downregulating its expression. Silencing BNIP3L mimics these protective effects by reducing LPS-induced cardiomyocyte apoptosis. These results suggest that MEx may attenuate myocardial injury, inflammation, and apoptosis in septic rats, possibly through MEx-mediated delivery of miR-23a-3p and modulation of the BNIP3L signaling axis. These results provide preliminary evidence supporting the therapeutic potential of MEx as a candidate intervention for sepsis-induced cardiomyopathy. - Source: PubMed
Publication date: 2026/08/26
Meng YanPan YayunDuan PanpanJi HuiPeng ChuanZhao ZhijiaChen LiangDu JiankuiYang Tao - Emerging evidence indicates that microgravity-induced osteoblast dysfunction is a critical contributor to spaceflight-associated bone loss. This study investigated the temporal dynamics of autophagy-apoptosis crosstalk in MC3T3-E1 osteoblasts under a rotary cell culture system (RCCS)-simulated microgravity. Crucially, time-course analysis (1, 3, 5, 10 days) revealed a biphasic autophagic response: initial enhancement of autophagic flux (LC3-II/Beclin-1 upregulation, p62 degradation) at day 3, exerting cytoprotective effects with reduced apoptosis, subsequently shifting to peak autophagy inhibition at day 5 concomitant with marked apoptosis activation (cleaved caspase-3 elevation) and mitochondrial dysfunction. By day 10, extensive cellular fragmentation dominated. Integrated proteomics identified TSPO, ATG12, and BNip3L as important mediators of this phenotypic switch. Murine hindlimb unloading experiments validated the upregulation of these proteins in bone tissue via Western blot and immunohistochemistry . We hypothesize that Early microgravity exposure triggers compensatory autophagy via ATG12-mediated vesicle expansion, whereas sustained stress is accompanied by TSOPO-associated ROS accumulation and BNip3L-linked alteration in autophagy-related pathways, contributing to apoptosis. Our finding suggests a biphasic temporal pattern in autophagy-apoptosis remodeling under simulated microgravity, highlighting potential time-sensitive windows for future therapeutic targets for spaceflight-associated osteopenia. - Source: PubMed
Publication date: 2026/03/20
Yang AoPeng BoTeng FeiChen YiZhang ShifengYang FeiXia YayiGeng Bin - Parkinson's disease (PD) is characterized by motor deficits and debilitating non-motor symptoms (NMS), including depression, anxiety, and cognitive impairment. While current therapies alleviate motor dysfunction, NMS management remains a critical unmet need. Pramipexole (PPX), a non-ergoline dopamine agonist with high selectivity for D2/D3 receptors (particularly D3), demonstrates potential for multi-target modulation beyond motor improvement. To systematically evaluate the efficacy of PPX against NMS and elucidate its novel mechanism involving autophagy regulation, a dual neurotoxin-induced PD mouse model (MPTP and DSP-4; MPTP:1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine; DSP-4: N-(2-chloroethyl)-N-ethyl-2-bromobenzylamine) recapitulating both motor and NMS was employed. PPX significantly improved NMS, reducing anxiety/depressive -like behavior and cognitive decline, alongside restoring motor function. Moreover, PPX administration promoted survival of dopaminergic and noradrenergic neurons and preserved synaptic integrity in a double lesion model of PD. In our molecular detection, PPX treatment was accompanied by enhanced key components of autophagy (Beclin-1/P62) and rectified deficient mitophagy (BNIP3L/PINK1/Parkin). This study identifies PPX as a dual-action therapeutic that concurrently alleviates motor/NMS in PD model mice, and this therapeutic effect may be associated with altered expression of autophagy-related proteins. - Source: PubMed
Publication date: 2026/08/05
Pang ShiminLiu JingyueSheng LinghuiXia TianjiWang ZheZhou MingYang NanLiu YanyongChan PiuRen Zhili - Mitochondrial quality control is essential for cellular homeostasis, particularly in neurons, where mitochondrial dysfunction is implicated in the pathogenesis of neurodegenerative diseases. Mitophagy, the selective degradation of damaged or superfluous mitochondria, plays a central role in maintaining mitochondrial integrity and metabolic balance. This review provides a comprehensive overview of the best-characterized PINK1-PRKN/parkin-dependent mitophagy pathway and the expanding repertoire of PRKN-independent mechanisms, including additional ubiquitin-dependent, receptor-mediated, and lipid-mediated pathways. We explore how these pathways intersect and compensate for one another, highlighting the complexity and adaptability of mitochondrial quality control networks. Furthermore, we discuss how dysregulated mitophagy contributes to the onset and progression of neurodegenerative diseases. By examining the interplay between mitophagy pathways and their regulation under physiological and pathological conditions, this review underscores the therapeutic potential of targeting mitophagy in neurodegeneration. Future studies should aim to decode the spatiotemporal dynamics of these pathways to uncover novel opportunities for clinical intervention. AD: Alzheimer disease; ALS: amyotrophic lateral sclerosis; AMBRA1: autophagy and beclin 1 regulator 1; AMFR/GP78: autocrine motility factor receptor; AMPK: AMP-activated protein kinase; ARIH1: ariadne RBR E3 ubiquitin protein ligase 1; ATG: autophagy related; Aβ: amyloid beta; BCL2L13: BCL2 like 13; BNIP3: BCL2 interacting protein 3; BNIP3L/NIX: BCL2 interacting protein 3 like; CALCOCO2/NDP52: calcium binding and coiled-coil domain 2; CAMc: core autophagy machinery components; CSNK2/CK2: casein kinase 2; DUB: deubiquitinase; DNM1L/DRP1: dynamin 1 like; FKBP8: FKBP prolyl isomerase 8; FUNDC1: FUN14 domain containing 1; GABARAP: GABA type A receptor-associated protein; GLP-1: glucagon-like peptide 1; HD: Huntington disease; HUWE1: HECT, UBA and WWE domain containing E3 ubiquitin protein ligase 1; IMM: inner mitochondrial membrane; iPSC: induced pluripotent stem cell; LIR: LC3-interacting region; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MARCHF5: membrane associated ring-CH-type finger 5; MCL1: MCL1 apoptosis regulator, BCL2 family member; MDV: mitochondria-derived vesicle; MFN1: mitofusin 1; MFN2: mitofusin 2; MQC: mitochondrial quality control; mtDNA: mitochondrial DNA; MUL1: mitochondrial E3 ubiquitin protein ligase 1; NBR1: NBR1 autophagy cargo receptor; OMM: outer mitochondrial membrane; OMMAD: outer mitochondrial membrane-associated degradation; OPA1: OPA1 mitochondrial dynamin like GTPase; OPTN: optineurin; OXPHOS: oxidative phosphorylation; PARL: presenilin associated rhomboid like; PD: Parkinson disease; PE: phosphatidylethanolamine; PG: phagophore; PGAM5: PGAM family member 5, mitochondrial serine/threonine protein phosphatase; PINK1: PTEN induced kinase 1; PPARGC1A/PGC-1α: PPARG coactivator 1 alpha; PRKN/parkin: parkin RBR E3 ubiquitin protein ligase; PtdIns3K: phosphatidylinositol 3-kinase; RB1CC1/FIP200: RB1 inducible coiled-coil 1; RHOT1/Miro1: ras homolog family member T1; ROS: reactive oxygen species; SIAH1: siah E3 ubiquitin protein ligase 1; SMURF1: SMAD specific E3 ubiquitin protein ligase 1; SOD1: superoxide dismutase 1; SQSTM1/p62: sequestosome 1; TAX1BP1: Tax1 binding protein 1; TBK1: TANK binding kinase 1; TCA: tricarboxylic acid cycle; TFAM: transcription factor A, mitochondrial; TIMM: translocase of inner mitochondrial membrane; TOMM: translocase of outer mitochondrial membrane; Ub: ubiquitin; ULK1: unc-51 like autophagy activating kinase 1; UPRmt: mitochondrial unfolded protein response; UPS: ubiquitin-proteasome system; USP30: ubiquitin specific peptidase 30; VCP: valosin containing protein; VDAC: voltage dependent anion channel; WIPI: WD repeat domain, phosphoinositide interacting. - Source: PubMed
Publication date: 2026/08/13
Rasmussen Laura KristineGomes Moreira DianaOkarmus JustynaSimonsen AnneMeyer Morten - Skeletal muscle differentiation in the C2C12 myoblast model requires extensive mitochondrial remodeling to meet rising bioenergetic demands through coordinated changes in biogenesis, dynamics, and respiratory adaptation. Urolithin A (UA), a gut microbiota-derived metabolite of ellagitannins, improves mitochondrial health, but its role in late-stage myogenic differentiation remains unclear. - Source: PubMed
Publication date: 2026/06/30
Vargas-Foitzick RonaldIrribarra-Tapia DiegoValero-Breton MayalenBalboa Elisa