Construction and characterization of a fusion protein with epidermal growth factor and the cell-binding domain of fibronectin.
An efficient expression system was constructed for C-EGF, a fusion protein made of a fragment of the cell-binding domain of human fibronectin (FN) bound with epidermal growth factor (EGF). C-EGF was produced in Escherichia coli HB101 cells carrying the recombinant plasmid pCE102 as inclusion bodies, which were solubilized and refolded after purification. C-EGF had both cell-adhesive and EGF activities, so it might be more effective than EGF in therapeutic applications. This fusion system would be useful for the construction of a recombinant drug delivery system for cells that have fibronectin receptors (integrins).
Kawase
Y
Y
Biotechnology Research Laboratories, Takara Shuzo Co. Ltd., Shiga, Japan.
Ohdate
Y
Y
Shimojo
T
T
Taguchi
Y
Y
Kimizuka
F
F
Kato
I
I
D002448:Cell Adhesion; D002478:Cells, Cultured; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004815:Epidermal Growth Factor / Q000235:genetics* / Q000378:metabolism / Q000494:pharmacology; D004926:Escherichia coli / Q000235:genetics; D005353:Fibronectins / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D010957:Plasmids; D011993:Recombinant Fusion Proteins / Q000235:genetics* / Q000378:metabolism / Q000494:pharmacology
D005353:Fibronectins; D011993:Recombinant Fusion Proteins; D004815:Epidermal Growth Factor