The neuroprotective and tissue-repairing functions of FGF-10 in ischemic stroke

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This article systematically elucidates the molecular basis of the neuroprotective effects of FGF-10 in the treatment of ischemic stroke, highlighting its multiple mechanisms, including suppressing neuroinflammation, preserving blood-brain barrier integrity, and promoting angiogenesis.

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Neuroprotective and Tissue Repair Functions of FGF-10 in Ischemic Stroke

Overview
This article systematically elaborates on the potential value of FGF-10 in the treatment of ischemic stroke, highlighting its neuroprotective mechanisms through multiple pathways, including suppression of neuroinflammation, preservation of blood-brain barrier integrity, and promotion of angiogenesis.

1. Therapeutic Challenges in Ischemic Stroke and the Opportunity Presented by the FGF Family.

Ischemic stroke is one of the leading causes of death and long-term disability worldwide, with its pathological process beginning with local cerebral ischemia and hypoxia due to vascular occlusion. Currently, the only approved thrombolytic drug has a narrow treatment window of 3 to 4.5 hours, and in reality, the majority of patients miss this opportunity due to delayed hospital arrival. Neurons in the ischemic core undergo irreversible death within minutes, while the surrounding penumbra region faces secondary damage from inflammatory cascades, blood-brain barrier disruption, and apoptosis. Therefore, developing a drug that is not time-limited and can simultaneously block multiple pathways of brain injury has become an urgent need in stroke research.

Members of the fibroblast growth factor (FGF) family have emerged as promising candidates due to their multifaceted roles in neuroprotection, anti-inflammation, and vascular repair. Among them, FGF-10, with its unique biological functions, has demonstrated protective effects in animal models of ischemic brain injury, attracting significant research attention.

2. Molecular Characteristics and Tissue Distribution of FGF-10.

FGF-10 consists of approximately 208 amino acid residues, with a molecular structure featuring a β-trefoil core domain formed by 12 antiparallel β-strands. Compared to other FGF members, FGF-10 exhibits unique receptor-binding specificity—it primarily binds with high affinity to the FGFR2 IIIb isoform, which is predominantly expressed on epithelial cell surfaces, determining the targeting specificity of FGF-10.

Under normal physiological conditions, FGF-10 is expressed in various tissues, including the lungs, gastrointestinal tract, skin, bones, and the central nervous system. In the brain, FGF-10 is mainly expressed in neurons and certain glial cells, where it participates in neurodevelopment and synaptic plasticity regulation. FGF-10 knockout mice exhibit severe defects in limb and lung development, leading to postnatal death due to respiratory failure, underscoring the indispensable role of FGF-10 in embryonic organ formation.

3. Multifaceted Protective Mechanisms of FGF-10 in Cerebral Ischemia.

In the pathological process of ischemic stroke, FGF-10 exerts neuroprotective effects through multiple pathways. In terms of anti-inflammation, FGF-10 can block inflammatory signals released by neurons, reducing the levels of pro-inflammatory cytokines such as IL-6 and TNF-α in the brains of ischemic mice, thereby preventing sustained inflammatory damage to brain tissue. Regarding blood-brain barrier protection, FGF-10 upregulates the expression of tight junction proteins ZO-1 and occludin, helping to maintain the tight connections between vascular endothelial cells and inhibiting the RhoA pathway to reduce vascular permeability, thereby alleviating cerebral edema. Additionally, FGF-10 stimulates endothelial cell proliferation by activating the PI3K/Akt signaling pathway, promoting angiogenesis in the peri-infarct region and restoring blood supply to ischemic brain tissue.

4. Conclusion.

With its multifaceted functions in anti-inflammation, blood-brain barrier protection, and angiogenesis, FGF-10 has demonstrated significant potential for neuroprotection and tissue repair in preclinical studies of ischemic stroke. Although the translation from animal experiments to clinical applications still faces challenges such as delivery efficiency, dosage optimization, and safety assessment, FGF-10, as a multi-target repair factor, offers a new perspective for overcoming the limitations of current thrombolytic therapies. High-quality rat-derived recombinant FGF-10 protein serves as a critical tool for in-depth exploration of its molecular mechanisms in cerebral ischemia and optimization of delivery strategies.

In basic research and drug screening related to FGF-10, high-quality rat-derived recombinant FGF-10 protein is essential for neuronal culture, signaling pathway analysis, and animal model studies. To meet this research demand, UniLove offers FGF-10 Protein, Rat, which is suitable for studies on ischemic-hypoxic injury in rat primary neurons and glial cells, exploration of FGFR2 signaling pathways, and optimization of FGF-10 administration methods and dosages in animal models of cerebral ischemia.

This article is reviewed and published by the technical expert team of UA

Disclaimer: This article partially utilizes artificial intelligence assistance in its creation. If any content involves copyright or intellectual property issues, please let us know and we promise to verify and remove it as soon as possible.

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