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Enhanced wound healing function of fibronectin variants via fusing with platelet factor 4
Guangyuan Wang1, Yunjia Zhang2, Hui Li2
1Shenzhen Public Platform for Screening and Application of Marine Microbial Resources, Institute for Ocean Engineering, Shenzhen International Graduate School, Tsinghua University, Shenzhen 518055, Guangdong Province, PR China; Shenzhen Key Laboratory of Advanced Technology for Marine Ecology, Institute for Ocean Engineering, Shenzhen International Graduate School, Tsinghua University, Shenzhen 518055, Guangdong Province, PR China.
None:
Skin injuries affect the daily life of millions of individuals, which may result in serious infection or even death. Wound healing is a complex process involved in cell differentiation, migration, proliferation, and has a significant influence on health status. Fibronectin (FN) is an essential non-collagenous glycoprotein of the extracellular matrix (ECM), which plays critical roles in complex physiological process by binding to integrins, syndecans, collagen, and growth factors, especially in the wound healing process. Herein, we report a FN mutant, named FN1, which assembles with specific domains of full-length FN. Two FN variants, PF4-FN1 and FN1-PF4, fuse with platelet factor 4 (PF4) peptide-a secondary messenger related to anti-aging-at the N-terminal or C-terminal of FN1. We also characterized the biological activities at the cellular level including cell migration, proliferation, adhesion, and efficiency of wound healing through animal experiments. Our results revealed that PF4-FN1 exhibited a significant influence on cell proliferation and adhesion compared with FN1 and FN1-PF4. Using a mouse skin injury model and detection of inflammatory factors, the PF4-FN1 could suppress inflammation during the healing process, and result in faster healing.
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