Abstract
Integrin-mediated cell-matrix interactions play an important role in osteogenesis. Here, we constructed a novel osteoinductive fibronectin matrix protein (oFN) for bone tissue engineering, designed to combine the integrin-binding modules from fibronectin (iFN) and a strong osteoinductive growth factor, bone morphogenetic protein-2. Compared with iFN, the purified oFN matrix protein caused a significant increase in cell adhesion and osteogenic differentiation of pre-osteoblast MC3T3-E1 cells (p < 0.05).
Highlights
Fibronectin (FN) is a component of the extracellular matrix and its interaction with integrin is essential in the early stages of osteoblast differentiation [1]
We recently reported that the integrin-binding modules from fibronectin (iFN)-osteocalcin fusion proteins are observed in an end-on orientation after absorption from the measurements of dissipation energy and atomic force microscopy (AFM), indicating that the active sites of the iFN-osteocalcin fusion proteins are exposed [13]
The apparent size of the expressed osteoinductive fibronectin matrix protein (oFN) was in good agreement with the estimated molecular mass, i.e., 50 kDa for a fusion protein consisting of oFN and Bone morphogenetic protein-2 (BMP-2)
Summary
Fibronectin (FN) is a component of the extracellular matrix and its interaction with integrin is essential in the early stages of osteoblast differentiation [1]. FN binds to the integrin family of cell surface receptors and regulates many biological processes [2]. FN is composed of homologous repeating structural modules consisting of 40–90 amino acids, classified as type I, II, and III repeats (FNI, FNII, and FNIII) [3]. An Arg-Gly-Asp (RGD) sequence located in the tenth type-III domain (FNIII10) and a.
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
