Growth factors are the molecular architects of tissue development, repair, and homeostasis. They orchestrate cell proliferation, differentiation, migration, and survival through precisely regulated signalling cascades that have profound implications for both health and disease. Among the dozens of growth factors that have been characterised, EGF , FGF2 , and VEGF121 stand out as three of the most extensively studied and translationally relevant members of this family. Each governs a distinct biological domain—EGF drives epithelial regeneration and tissue repair, FGF2 directs mesenchymal and neural development, and VEGF121 is the master regulator of vascular formation and remodelling—yet all three share a common feature: they are indispensable research tools for understanding fundamental biological processes and developing novel therapeutic strategies.
EGF: The Prototypic Regulator of Epithelial Growth and Repair
Epidermal growth factor (EGF) is the founding member of the EGF family of growth factors and one of the most thoroughly characterised signalling molecules in biology. First discovered for its ability to stimulate epidermal growth and keratinocyte proliferation, EGF has since been shown to play critical roles in wound healing, tissue regeneration, and the maintenance of epithelial barrier function. Its clinical significance has been underscored by recent meta-analyses demonstrating that EGF/EGFR vaccines may improve survival in EGFR-driven solid tumours, particularly non-small cell lung cancer and glioblastoma.
The translational potential of EGF has been further expanded by innovations in delivery systems. A 2026 study published in Advanced Healthcare Materials described the construction of EGF mRNA-enriched extracellular vesicles based on the AAVS1 safe harbour site—a CRISPR/Cas9-based approach that generates a cell line stably secreting EVs enriched in EGF mRNA. This strategy overcomes a key limitation of EGF therapy—its rapid degradation at wound sites—by leveraging EVs as natural nanocarriers that protect nucleic acids from degradation and enhance bioavailability. In parallel, researchers have developed a modular bioadhesive incorporating mussel adhesive protein and EGF via the Spycatcher-Spytag system, achieving robust growth factor immobilisation and significantly accelerated full-thickness wound healing in rat models. These advances highlight the continued relevance of EGF as both a therapeutic agent and a research tool for studying tissue repair mechanisms.
FGF2: The Multifaceted Regulator of Development, Regeneration, and Fibrosis
Fibroblast growth factor 2 (FGF2), also known as basic fibroblast growth factor (bFGF), is a canonical member of the FGF family with essential roles in embryonic development, tissue regeneration, and stem cell biology, where it supports pluripotency and high proliferative capacity. Unlike EGF, which primarily targets epithelial cells, FGF2 acts on a broader range of cell types—including fibroblasts, endothelial cells, and mesenchymal stem cells—and has been implicated in skeletal muscle development, bone regeneration, and periodontal healing.
Recent research has revealed the remarkable versatility of FGF2 signalling. A 2026 review published in Cytokine & Growth Factor Reviews provided a comprehensive synthesis of current mechanistic insights into FGF2 signalling, elucidating its regulatory interplay with TGF-β that favours regenerative repair over fibrosis. This balance is critical: while FGF2 promotes inflammation resolution, proliferation, vascularisation, and re-epithelialisation during wound healing, dysregulated FGF2 signalling can contribute to fibrotic pathology. Indeed, an FGF2-derived short peptide has been shown to significantly attenuate bleomycin-induced pulmonary fibrosis by inhibiting collagen deposition and epithelial-mesenchymal transition via the FGFR/MAPK signalling pathway.
In the field of regenerative medicine, FGF2 has been engineered into advanced biomaterial platforms. A 2026 study demonstrated that FGF2-immobilised biointerfaces drive exogenous TGF-β1-independent chondrogenesis of human mesenchymal stem cells and ectopic cartilage tissue formation. The immobilised FGF2 interface promotes spontaneous, scaffold-free spheroid assembly via FGFR1–heparan sulfate proteoglycan-mediated adhesion, providing localised and sustained signalling that up-regulates SOX9, COL2A1, and aggrecan while suppressing COL1A1 and COL10A1. Subcutaneous implantation of pre-differentiated spheroids into immunodeficient mice generated ectopic cartilage tissue rich in type II collagen and aggrecan, even in the absence of TGF-β1. These findings establish FGF2 as a bioinstructive matrix component that provides a defined and reproducible route for generating chondrogenic constructs for regenerative medicine.
VEGF121: The Freely Diffusible Isoform Shaping Angiogenesis and Immunotherapy
Vascular endothelial growth factor (VEGF)-A is a central regulator of angiogenesis, and its isoforms—generated by alternative splicing—exhibit distinct functional properties. VEGF121 is the only VEGF-A isoform that lacks heparin-binding activity and is freely diffusible. It binds to VEGF receptors (VEGFRs) overexpressed on vessels of ischaemic tissue and plays a critical role in tumour angiogenesis and vascular remodelling.
The clinical significance of VEGF121 has been highlighted by recent studies demonstrating its utility as a predictive biomarker. A 2025 study published in Cancers found that serum VEGF121 levels could serve as a useful biomarker for predicting the efficacy of anti-PD-1/PD-L1 antibody monotherapy in patients with non-small cell lung cancer. Patients with higher VEGF121 serum levels showed significantly shorter progression-free survival and a lower objective response rate than those with lower levels. This finding underscores the interplay between angiogenic signalling and immune checkpoint pathways—a relationship that is increasingly recognised as central to the tumour microenvironment.
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