FGF 1 Human
Description
Structure and Synthesis
-
Gene: FGF1 (chromosome 5q31.3) encodes the FGF-1 precursor, processed into a mature 141-amino-acid protein .
-
Secretion: Lacks a classical signal peptide; secreted via a non-canonical pathway involving S100A13, synaptotagmin-1 (SYT1), and Cu²⁺-dependent dimerization .
-
Stability: Heparin binding enhances stability and facilitates FGFR activation .
Signaling Pathways
FGF-1 binds all four FGFR isoforms (FGFR1–4) and activates:
-
PI3K/AKT: Enhances cell migration and metabolic regulation .
-
Nuclear Activity: Enters the nucleus via an NLS to regulate gene expression (e.g., VEGF, antioxidant enzymes) .
Key Roles in Physiology
-
Angiogenesis: Stimulates endothelial cell proliferation and blood vessel formation .
-
Neuroprotection: Restores dopamine neurons in Parkinson’s disease models .
-
Metabolism: Reverses hyperglycemia in diabetic mice via insulin sensitization .
-
Antioxidant Defense: Upregulates glutathione peroxidase (GPx) in retinal cells under high glucose .
Preclinical and Clinical Trials
-
Parkinson’s Disease: Intranasal FGF-1 improved motor function by 18%–82% in a Phase I trial (NCT data pending), with no adverse events reported .
-
Retinal Disorders: Mitigated oxidative stress and apoptosis in diabetic retinopathy models .
-
Ischemia: Reduced infarct size in cardiac and cerebral ischemia models .
Key Interactions
-
Intracellular Partners: CK2, FIBP, LRRC59, and mortalin modulate nuclear signaling .
-
Extracellular Matrix: Heparan sulfate proteoglycans sequester FGF-1 for sustained release .
Challenges and Future Directions
-
Short Half-Life: Rapid degradation in vivo necessitates heparin co-administration or engineered analogs .
-
Dual Roles in Cancer: Pro-angiogenic effects may exacerbate tumor growth, requiring targeted delivery .
-
Immune Modulation: Enhances IL-2 production in T cells via NF-κB, suggesting applications in immunotherapy .
Product Specs
Product Science Overview
FGF-acidic is a single-chain polypeptide consisting of 140 amino acids and has a molecular weight of approximately 15.8 kDa . It is produced in a non-glycosylated form in Escherichia coli (E. coli) and is purified using proprietary chromatographic techniques . The protein is known for its ability to bind heparin, which is essential for its interaction with fibroblast growth factor receptors (FGFRs) .
FGF-acidic is a potent activator of DNA synthesis, cell proliferation, and chemotaxis . It plays a crucial role in various physiological processes, including:
- Development: FGF-acidic is involved in the development of multiple tissues and organs. It is highly expressed in the central and peripheral nervous systems .
- Regeneration: The protein promotes tissue repair and regeneration by stimulating the proliferation of various cell types, including fibroblasts, endothelial cells, and neurons .
- Angiogenesis: FGF-acidic is a key player in angiogenesis, the formation of new blood vessels, which is vital for wound healing and tissue growth .
FGF-acidic exerts its effects by binding to specific FGFRs on the cell surface. This binding triggers a cascade of intracellular signaling pathways, including the activation of protein kinase C and the inhibition of p53 and proapoptotic signaling . These pathways promote cell survival, proliferation, and differentiation .
Human recombinant FGF-acidic is widely used in research and therapeutic applications. Some of its notable uses include:
- Cell Culture: FGF-acidic is used as a growth factor in cell culture media to promote the proliferation of various cell types .
- Tissue Engineering: The protein is incorporated into biomaterials to enhance tissue regeneration and repair .
- Neuroscience Research: FGF-acidic is used to study neural development and neuroprotection .
