Ask about this productRelated genes to: TYRO3 antibody
- Gene:
- TYRO3 NIH gene
- Name:
- TYRO3 protein tyrosine kinase
- Previous symbol:
- RSE
- Synonyms:
- Dtk, Brt, Tif, Sky, Etk-2, Rek
- Chromosome:
- 15q15.1
- Locus Type:
- gene with protein product
- Date approved:
- 1992-10-02
- Date modifiied:
- 2016-10-05
Related products to: TYRO3 antibody
Related articles to: TYRO3 antibody
- Sepsis-associated encephalopathy (SAE) is a common and debilitating complication of sepsis, yet its cellular mechanisms and targeted therapies remain unclear. Microglia preserve neuroinflammatory homeostasis and neural circuit integrity through efferocytosis, but how this process is altered in SAE and regulated by immunometabolism is poorly defined. Here, we investigated the molecular basis of microglial efferocytosis impairment using LPS-stimulated BV2 cells and a cecal ligation and puncture (CLP) murine SAE model. We integrated RNA sequencing, HIF-1α and SLC7A11 gain- and loss-of-function approaches and in vitro functional assays. In vivo, HIF-1α was pharmacologically inhibited (KC7F2) or stabilized (DMOG) to evaluate its role in SAE. We assessed microglial efferocytosis and polarization, neuronal and synaptic integrity, cognition, survival, and brain metabolomics. LPS induced a pro-inflammatory microglial phenotype and reduced efferocytosis mediators (Tyro3, Mertk, Axl), impairing clearance of apoptotic neurons. HIF-1α upregulation interacted with SLC7A11 to suppress the TAM-Rac1-NCKAP1 axis, leading to efferocytic failure; knockdown of HIF-1α or SLC7A11 restored efferocytosis. In CLP mice, HIF-1α/SLC7A11 elevation coincided with TAM-Rac1-NCKAP1 suppression. These results reveal that impaired microglial efferocytosis is a key but overlooked feature in SAE. KC7F2 restored efferocytosis, shifted cytokines toward anti-inflammatory profiles, improved cognition and survival, and normalized metabolomic signatures, while DMOG produced opposite effects. This work uncovers a previously unknown HIF-1α-SLC7A11 pathway driving microglial dysfunction in SAE, offering fresh insight into disease mechanisms and pointing to HIF-1α as a promising therapeutic target. - Source: PubMed
Publication date: 2026/04/15
Wang ShengnanChen YoufangSun ZhendongZeng YafenWang GuidanLin QingfanChen ChunnuanHe Hefan - The TAM family of receptor tyrosine kinases (TYRO3, AXL, MERTK) promotes tumor survival, metastasis, and immune evasion. Its dysregulation across solid and hematologic cancers is associated with therapy resistance and poor outcomes. FLT3 is a key oncogenic driver in acute myeloid leukemia (AML). We report the preclinical characterization of CPL423, a low-molecular-weight inhibitor of all TAMs and FLT3. - Source: PubMed
Publication date: 2026/03/25
Mikołajczyk AgataPopiel DelfinaJastrzębska KingaWiernicki BartoszMituła FilipJanusz ArturDominowski JakubGórka MichałKornatowski TomaszHucz-Kalitowska JoannaTeska-Kamińska MałgorzataSmuga DamianDelis MonikaKamecki KrystianMaliszewski PawełYamani AbdellahDubiel KrzysztofPieczykolan JerzyWieczorek Maciej - Epithelial-mesenchymal transition (EMT) plays a critical role in tumor progression; however, the underlying molecular mechanisms of EMT in papillary thyroid carcinoma (PTC) remain incompletely understood. This study aimed to investigate EMT-related mechanisms in PTC using an integrative approach combining single-cell RNA sequencing and machine learning. - Source: PubMed
Xu TianfengSun RuonanZhang YujieZheng Xun - Efferocytosis plays a critical role in clearing apoptotic tumor cells and suppressing inflammation in hepatocellular carcinoma (HCC). This study aimed to identify efferocytosis-related genes (ERGs) with prognostic value and develop a predictive model for HCC outcomes. - Source: PubMed
Publication date: 2026/03/04
Yang Jiao-JiaoOuyang QingZeng Xin-XinCen Wen-JianDeng LingSong Gao-PingWang FangSun Li-Yue - Marburg virus is a highly virulent filovirus responsible for severe hemorrhagic fever outbreaks with high mortality rates. This study aimed to (1) investigate the structural and functional consequences of mutations in major MARV proteins-particularly Glycoprotein (GP)-and (2) evaluate the antiviral potential of selected plant-derived compounds using computational approaches. Comparative sequence analysis identified recurrent amino acid substitutions in GP, with mutations such as P278L and D364Y predicted to induce structural damage and impact host receptor binding. Molecular dynamics simulations revealed that these mutations disrupted GP stability, altered solvent accessibility, and reduced hydrogen bonding with TYRO3 and MER receptors, potentially facilitating immune evasion and viral adaptability. Disorder prediction analysis further indicated high flexibility around these sites, reinforcing their role as mutational hotspots. To explore potential antiviral strategies, a panel of five plant-derived compounds-Aesculetin, Carvacrol, Cinnamaldehyde, Eugenol, and Geranial-was computationally screened against GP and host cell receptors (AXL, TYRO3, MER). Only Aesculetin demonstrated consistent docking scores below the -5.5 kcal/mol threshold, suggesting limited but measurable binding affinity. Other compounds exhibited weaker interactions and did not meet the minimal binding energy criterion. In contrast, known EBOV/MARV inhibitors (IN-1, IN-2, IN-3) showed significantly stronger and more stable binding profiles across all targets. Protein-ligand interaction analysis revealed that natural compounds formed fewer stabilizing contacts compared to synthetic inhibitors, though Aesculetin engaged in key hydrogen bonds and weak electrostatic/π-cation interactions with GP. Overall, the findings highlight the structural plasticity of MARV GP, the functional relevance of specific mutations, and the potential-albeit limited-of plant-derived compounds as antiviral candidates. - Source: PubMed
Publication date: 2026/03/28
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