PTK2 (phospho-Tyr397) Antibody
- Known as:
- PTK2 (phosphorilated-Tyr397) Antibody
- Catalog number:
- abx000350
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Abbexa
- Gene target:
- PTK2 (phospho-Tyr397) Antibody
Related genes to: PTK2 (phospho-Tyr397) Antibody
- Gene:
- PTK2 NIH gene
- Name:
- protein tyrosine kinase 2
- Previous symbol:
- -
- Synonyms:
- FAK, FADK, FAK1, PPP1R71
- Chromosome:
- 8q24.3
- Locus Type:
- gene with protein product
- Date approved:
- 1992-10-02
- Date modifiied:
- 2014-11-18
Related products to: PTK2 (phospho-Tyr397) Antibody
Related articles to: PTK2 (phospho-Tyr397) Antibody
- Retinal angiogenesis requires precise transcriptional regulation. Krüppel-like factor 9 (Klf9) has been implicated in various biological processes; however, its specific role in retinal vascular development and ocular neovascular disease remains unclear. In this study, we identified Klf9 as a critical transcriptional regulator of retinal vascular homeostasis. Spatiotemporal transcriptomic and single-cell RNA sequencing analyses revealed that Klf9 was highly enriched in retinal endothelial cells and upregulated during vascular maturation. Using genetic mouse models, we demonstrated that endothelial-specific Klf9 deletion accelerated neonatal retinal vascular expansion and tip cell formation, whereas its overexpression delayed angiogenesis and disrupted barrier function. In oxygen-induced retinopathy, Klf9 loss exacerbated pathological neovascularization and leakage, while its overexpression conferred protection. Integrated RNA-seq and ATAC-seq profiling of human retinal microvascular endothelial cells revealed that Klf9 represses a network of genes involved in the PI3K-Akt pathway and focal adhesions. Key effectors, including , , and were suppressed by reduced chromatin accessibility at their promoters. Both and rescue experiments confirmed that Akt activation reverses vascular hypoplasia caused by Klf9 overexpression, whereas Akt inhibition normalizes the hyper-angiogenic phenotype of the Klf9-deficient endothelium. Collectively, these findings establish Klf9 as a transcriptional brake on retinal angiogenesis, acting through chromatin-mediated suppression of the PI3K-Akt pathway, and provide new mechanistic insights and potential therapeutic targets for pathological retinal angiogenesis. - Source: PubMed
Publication date: 2026/05/11
Wu HonglianYang TianjingXun YuningZhou MingZhang YutianYao XuemingChang YongshengLei YiYan Hua - Proline-rich tyrosine kinase 2 (PYK2) and focal adhesion kinase (FAK) are non-receptor tyrosine kinases implicated in Alzheimer's disease (AD), but their functional role in microglia remains understudied. Selective pharmacological tools are required for preclinical studies leading to translational therapeutic development. - Source: PubMed
Weerawarna Pathum MJesudason Cynthia DLobb Karen LMason Emily RGu XiaopingChu ShaoyouRichardson Timothy I - Pulmonary fibrosis is a severe, chronic, and often lethal interstitial lung disease characterized by a destructive cycle of alveolar injury and inflammation, culminating in irreversible lung scarring. Its complex and multifactorial pathogenesis contributes to a poor prognosis and susceptibility to recurrent lung damage. This study employed an integrated network pharmacology and molecular docking approach to investigate the therapeutic repurposing of cilostazol for pulmonary fibrosis. Cilostazol was selected as a highly promising candidate owing to its broad pharmacological profile, encompassing anti-inflammatory, antioxidant, antiapoptotic, and antifibrotic properties. Network pharmacology analysis identified 10 potential targets of cilostazol, of which eight emerged as key network regulators: phosphodiesterase 3 (PDE3), PIK3CA, PTK2, RPS6KB1, VEGFR, F2-thrombin, ULK3 kinase, and PI3K delta. Molecular docking demonstrated that cilostazol binds to these profibrotic and fibrotic target proteins with binding affinities comparable to those of established experimental inhibitors. Experimental validation was performed using a bleomycin (BLM)-induced rat model of pulmonary fibrosis, incorporating histopathological and biochemical analyses of lung tissue and bronchoalveolar lavage fluid. Cilostazol exhibited significant antioxidant activity by reducing lipid peroxidation and restoring antioxidant enzyme levels. It exerted anti-inflammatory effects by downregulating proinflammatory cytokines (TNF-α, NO, and IL-6) and inflammatory markers (CRP, LDH, and MPO). Furthermore, cilostazol attenuated key indicators of fibrosis progression, including KL-6 and endothelin-1, alongside fibrotic markers such as TGF-β, α-SMA, and collagen I and III. At the molecular level, it significantly reduced the mRNA expression of fibrosis-associated genes, including TGF-β, fibronectin, α-SMA, collagen I, and MMP-7. Collectively, these findings demonstrate that cilostazol confers significant protection against bleomycin-induced pulmonary fibrosis through the targeted inhibition of the TGF-β/Smad, PI3K/AKT, and Wnt/β-catenin signaling cascades, highlighting its potential as a viable repurposed therapeutic strategy for inflammation-driven pulmonary fibrosis. - Source: PubMed
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