Production of EGF-collagen chimeric protein which shows the mitogenic activity.
Collagen has been utilized as a natural biomaterial because of its high biocompatibility, adhesiveness to cells and tissues, and biodegradability. The present study developed a recombinant technology to confer a mitogenic activity on type III collagen by fusing it to epidermal growth factor (EGF) at the collagen's N-terminus. The chimeric protein of EGF-collagen was synthesized in insect cells by the baculovirus-insect cell expression system. The fusion protein was shown to hold the triple helical conformation of collagen and the mitogenic activity of EGF. It was also demonstrated that the chimeric protein can be immobilized on tissue culture dishes as a fibrous form and in collagen fibrils without abolishing the original mitogenic activity of EGF. This fusion protein can be utilized as a biocompatible, biodegradable, and adhesive fibrous mitogen for a variety of purposes in the area of tissue engineering.
Hayashi
M
M
Developmental Biology Laboratory, Department of Biological Science, Graduate School of Science, Hiroshima University, Japan.
Tomita
M
M
Yoshizato
K
K
D000818:Animals; D016367:Baculoviridae / Q000378:metabolism; D002460:Cell Line; D003094:Collagen / Q000737:chemistry*; D003470:Culture Media; D004815:Epidermal Growth Factor / Q000737:chemistry*; D005782:Gels; D005822:Genetic Vectors; D008934:Mitogens / Q000096:biosynthesis*; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis*
D003470:Culture Media; D005782:Gels; D008934:Mitogens; D011993:Recombinant Fusion Proteins; D004815:Epidermal Growth Factor; D003094:Collagen