Shenzhen Weiguang Biological Products Co., Ltd.

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.

As an important coagulation factor, activated coagulation factor VII (FVIIa) is mainly used to treat the bleeding of hemophilia patients who have developed inhibitory antibodies against FVIII and FIX conventional treatment. Recombinant human factor VII (rhFVII) produced in mammalian cell lines have been developed as the most important resource of FVIIa. However, cell lines express rhFVII protein derived from an exogenous expression vector at a lower level than most other proteins. In the current study, we have shown efficient rhFVII production in CHO cell lines using piggyBac (PB) transposon system. rhFVII is successfully expressed in fed-batch culture of CHO cells, and the expression of rhFVII up to 100 mg/L. Moreover, the purified secreted rhFVII was determined by SDS-PAGE and Western Blot. The coagulation activity was determined by the chromogenic Activity ELISA kit. In conclusion, this study has demonstrated that the piggyBac transposon system can be used for an efficient production of recombinant FVII.

In the original publication of the article, the Acknowledgement section was published incompletely. The complete Acknowledgement is given in this Correction.