Discovery and Functional Characterization of a Recombinant Fragment of Human Collagen Type XVII.
Summary
This mechanistic study identifies a functional recombinant fragment of human collagen XVII that binds integrin α3β1, upregulates adhesion and polarity proteins, activates PRKCZ/AKT/TGF-β1 signaling, enhances keratinocyte proliferation, and reduces UV-induced damage. The data position rhCOL17 as a promising antiaging biomaterial targeting epidermal-dermal cohesion and photoprotection.
Key Findings
- rhCOL17 bound stably to the canonical ligand-binding interface of integrin α3β1 (SPR and computational modeling).
- rhCOL17 upregulated laminin-332, integrin β1, PAR-3, and PAR-6B, and activated PRKCZ, AKT, and TGF-β1 signaling.
- rhCOL17 promoted keratinocyte proliferation and mitigated UV-induced cellular damage.
Clinical Implications
Supports development of topical or minimally invasive formulations leveraging rhCOL17 to improve skin firmness and photoprotection; informs target engagement (integrin α3β1/laminin‑332) for future clinical translation.
Why It Matters
Introduces a novel, mechanistically supported biomaterial with antiaging potential that targets epidermal anchoring and UV resilience—key unmet needs in aesthetic dermatology.
Limitations
- In vitro and cellular models only; no in vivo human or animal efficacy/safety data.
- Immunogenicity, delivery, and stability of rhCOL17 in topical systems were not assessed.
Future Directions
Evaluate dermal penetration, formulation stability, immunogenicity, and efficacy in animal photoaging models and early-phase human studies; compare with existing peptides and growth factors.
Study Information
- Study Type
- Basic/mechanistic study
- Research Domain
- Pathophysiology
- Evidence Level
- V - Laboratory mechanistic evidence without in vivo or clinical data.
- Study Design
- OTHER