Construction of epidermal growth factor fusion protein with cell adhesive activity.
A novel protein for controlling cellular functions was constructed by combining functional units of various proteins. The Arg-Gly-Asp (RGD) sequence functioning as a cell adhesive function, an epidermal growth factor (EGF) as a cell growth function, and a hydrophobic sequence (E12) as an efficient assembling function, were combined and incorporated into one molecule. The fusion protein, designated ERE-EGF, was produced in Escherichia coli and purified with affinity chromatography using a His-tag. The ERE-EGF coated on an unmodified hydrophobic surface of a cell-culture plate (through the hydrophobic E12 moiety) retained both cell adhesive activity (through the RGD sequence) and cell growth activity (through the EGF moiety).
Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan.
Imen
I
Elloumi
Rie
R
Kobayashi
Hisakage
H
Funabashi
Masayasu
M
Mie
Eiry
E
Kobatake
D000595:Amino Acid Sequence; D002448:Cell Adhesion / Q000187:drug effects*; D004926:Escherichia coli / Q000235:genetics; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry / Q000494:pharmacology; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000235:genetics / Q000494:pharmacology*; D014407:Tumor Cells, Cultured
C510655:ERE-EGF fusion protein; D009842:Oligopeptides; D011993:Recombinant Fusion Proteins; C047981:arginyl-glycyl-aspartic acid