Ask about this productRelated genes to: ANXA1 protein
- Gene:
- ANXA1 NIH gene
- Name:
- annexin A1
- Previous symbol:
- ANX1, LPC1
- Synonyms:
- -
- Chromosome:
- 9q21.13
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2014-11-19
Related products to: ANXA1 protein
Related articles to: ANXA1 protein
- Inflammation plays a central role in the development of metabolic dysfunction-associated steatohepatitis (MASH). Formyl peptide receptor 1 (FPR1) in myeloid cells emerges as a crucial factor associated with the inflammatory response; however, whether and how FPR1 signaling affects MASH development remain largely unknown. - Source: PubMed
Publication date: 2026/04/24
Yang SitingQian ShengyingYang LiuHe YanghuanGe ShujunFu XinhuanDong SiyueYa RuChen YingfenMa NingningXiao PengZhang ZilingZhou YueChen YuanwenWang YanHe Yong - Neuroinflammation is a key therapeutic target for spinal cord injury (SCI). Apoptotic bodies (ABs) derived from mesenchymal stem cells may modulate early inflammation, promoting SCI repair. Stem cells from human exfoliated deciduous teeth (SHEDs), with neural crest origins, are promising for neurological therapies, but their ABs' role in SCI remains unclear. In this study, as exploratory research, we aimed to investigate the preliminary effects and mechanisms of SHEDs-derived ABs on the treatment of SCI. Herein, SHEDs-derived ABs enhanced functional recovery in SCI mice, improving BMS scores, joint movement, and bioelectrical conduction. Histologically, ABs boosted axonal growth and neuronal regeneration. Moreover, SHEDs-derived ABs significantly suppressed M1 polarization while enhancing M2 polarization in both in vitro and in vivo models. GO/KEGG analyses revealed AB enrichment in immune-related pathways. Mechanistically, the ANXA1/FPR2 axis was critical for ABs-induced microglia/macrophage polarization, with M1 regulation mediated by the NF-κB pathway and M2 modulation driven by the AKT/mTOR pathway. Thus, SHEDs-derived ABs may serve as a clinically translatable strategy for treating SCI by mediating immunomodulation via the ANXA1/FPR2 axis. - Source: PubMed
Publication date: 2026/04/23
Luo LihuaDong NaXu JunpengZhang ChenBao SaXu HaichaoWang XipingDai PengLi CaiyanZhang QiaoYing YiboJiang DaweiLi ShengcunWu PingMei LiqingLi XiaokunDeng JunjiePan YihuaiWang Zhouguang - Oral submucous fibrosis (OSF) is a betel quid chewing-associated precancerous disorder. Studies have shown that the traditional Chinese medicine Jiawei Danxuan Koukang (JDK) exhibits inhibitory effects on OSF, but its specific mechanisms and molecular targets remain unstated. This study aims to elucidate the pharmacological mechanisms of JDK and its component kaempferol in treating OSF. OSF rat model and in vitro cell models were induced by arecoline. Techniques, including hematoxylin-eosin (HE) staining, Masson staining, western blot, quantitative real-time polymerase chain reaction (qRT-PCR), enzyme-linked immunosorbent assay (ELISA), immunofluorescence (IF) staining, co-immunoprecipitation (Co-IP), and molecular docking were used to evaluate the effects of JDK and kaempferol on OSF pathological damage, Annexin-A1 (ANXA1) expression, neutrophil infiltration, collagen deposition, and fibroblast activation. JDK and kaempferol alleviated pathological damage in the oral mucosa tissues of OSF rats, inhibited collagen deposition and fibroblast activation marker expressions, including fibroblast activation protein (FAP), vimentin (VIM), alpha-smooth muscle actin (α-SMA), and matrix metalloproteinase-1 (MMP1), and improved mouth opening function. Further studies revealed that JDK and kaempferol upregulated ANXA1 expression, thereby suppressing neutrophil recruitment, pro-inflammatory cytokine release, and collagen deposition. In vitro experiments confirmed that kaempferol directly bound to ANXA1 in epithelial cells, enhancing its stability, and interacted with FPR2 signaling in fibroblasts to inhibit their activation, thereby restoring epithelial-fibroblast homeostasis. However, knockdown of ANXA1 reversed these protective effects. JDK and kaempferol attenuated OSF by upregulating the ANXA1/FPR2 axis, inhibiting neutrophil infiltration and fibroblast activation, suggesting ANXA1 as a potential therapeutic target for OSF. To our knowledge, this is the first study to demonstrate that JDK/kaempferol exert anti-fibrotic effects in OSF specifically through the ANXA1/FPR2 axis. - Source: PubMed
Publication date: 2026/04/15
Xiao YaoTan YisiLiu YanliChen RuiyiZhou TaoHu ZhaoyongTan Jin - In chronic kidney disease (CKD), there is evidence of loss of function and fibrosis in the progression of tubular epithelial cells; however, the cellular heterogeneity and underlying molecular mechanisms are not well defined. Knowledge of the diversity among tubular cells is essential for precision medicine therapy. - Source: PubMed
Publication date: 2026/04/17
Mao XinhuiWei MinggangLi YilinXia Ping - Neutrophil extracellular traps (NETs) constitute a critical antimicrobial mechanism, yet excessive or dysregulated NET release contributes to endothelial injury and tissue damage. Therefore, identifying physiological and pharmacological regulators of NET formation remains an important goal. Although the role of mitochondrial dynamics in NETs remains incompletely elucidated, accumulating evidence suggests that mitochondria may be underexplored regulators with therapeutic potential. In fact, in certain NET forms, their DNA is of mitochondrial origin. Here, we investigated how exogenous dimethyl fumarate (DMF), an ester of the tricarboxylic acid cycle (TCA) metabolite fumarate, modulates NET formation. Foremost, we observed that DMF markedly suppresses PAD4-dependent NET release by LPS-stimulated neutrophils of wild-type and PAD4-deficient mice. Mechanistic analyses demonstrated that DMF activates the nuclear factor erythroid 2-related factor 2 (Nrf2) pathway and increases the secretion of anti-inflammatory Annexin A1 (ANXA1). Functionally, inhibition of either Nrf2 or the ANXA1 receptor Fpr2 restores NET formation. To integrate these observations with mitochondrial function, we examined markers of mitochondrial dynamics. We found that DMF decreases phosphorylation of dynamin-related protein 1 (DRP1) at Serine 616, a modification typically associated with reduced mitochondrial fission. Consistently, pharmacological inhibition of DRP1 (Mdivi-1) also diminishes NET formation, whereas induction of mitochondrial fragmentation (CCCP) triggers PANoptotic neutrophil death and extracellular DNA release, both of which were prevented by DMF. Collectively, these data identify DMF as a mitochondria-linked immunometabolic regulator that suppresses NET formation through coordinated engagement of Nrf2 and ANXA1 signaling and modulation of mitochondrial dynamics. These findings highlight mitochondrial remodeling as a promising avenue for future exploration and position DMF as a potential pharmacological tool for controlling excessive neutrophil activation. - Source: PubMed
Publication date: 2026/03/31
Burczyk GabrielaKolaczkowska Elzbieta