Jing Wang

Rapid wound healing of oral soft tissue may reduce the opportunity for infection and discomfort of patients. Given that recombinant humanized collagen type III (rhCol III) is considered a nonallergenic biomaterial and can help repair skin wound healing and activate tissue remodeling, the potential effect of rhCol III on palate mucosal wound healing was preliminarily evaluated in vitro and in vivo in this study. A mouse model of an oral palate wound was established, and rhCol III solutions were injected periwound, resulting in a significant acceleration in wound healing compared to the control groups. Histological evaluation showed that rhCol III promoted angiogenesis, collagen deposition, and cell proliferation. Furthermore, the results demonstrated that rhCol III could promote human gingival fibroblast (HGF) and human oral keratinocyte (HOK) proliferation, adhesion, and migration. To further explore the mechanism, RNA-sequencing analysis results showed that rhCol III could regulate the focal adhesion signaling pathway of HGFs. The expression of vinculin and phosphorylation of FAK (Tyr397 and Tyr576) in HGFs was upregulated with rhCol III treatment. In addition, inhibition of FAK phosphorylation could inhibit HGF migration. These results suggested that rhCol III promoted HGF migration by upregulating the focal adhesion signaling pathway. These findings suggest that the topical application of rhCol III is a promising treatment for oral soft tissue wounds with the potential for future clinical use.

Collagen type XVII is a unique transmembrane protein that plays a crucial role in anchoring epithelial cells to the underlying basement membrane. However, the low natural abundance of collagen type XVII in the human body poses significant challenges for large-scale extraction and production. With a development in biosynthesis technology, type A recombinant humanized collagen type XVII (rhCol XVII) has emerged as a promising and innovative alternative. In this study, rhCol XVII was successfully synthesized and expressed using genetic engineering techniques. The amino acid composition of rhCol XVII was analyzed, and its molecular weight was determined to be consistent with the theoretical design. Key physicochemical properties, including isoelectric point, particle size, and thermal stability, were evaluated. The experimentally measured pI was approximately 9.00, a particle size ranges from 820 to 857 nm, and thermal stability up to 23.60°C. The structure of rhCol XVII was characterized using infrared spectroscopy and circular dichroism. Furthermore, the cytocompatibility of rhCol XVII was assessed in vitro, and its systemic safety was evaluated in vivo. This research provided a solid foundation for the potential application of rhCol XVII in tissue engineering and regenerative medicine.