title: Production and properties of a bifunctional fusion protein that mediates attachment of vero cells to cellulosic matrices.
abstract: The sequence Arg-Gly-Asp (RGD) in extracellular matrix proteins such as fibronectin, collagen, and laminin mediates cell attachment by interacting with proteins of the integrin family of cell surface receptors. A gene fusion encoding the RGD-containing peptide, fused to the C-terminus of a cellulose-binding domain (CBD/RGD), was expressed in Escherichia coli. Cultures produced up to 50 mg of CBD/RGD per liter, most of which was extracellular. It was purified from the culture supernatant by affinity chromatography on cellulose. CBD/RGD promoted the attachment of green monkey Vero cells to polystyrene and cellulose acetate. Attachment was inhibited by small synthetic peptides containing the RGD sequence. CBD/RGD was as effective as collagen in promoting the attachment of Vero cells to Cellsnowtrade mark microcarriers. (c) 1995 John Wiley & Sons, Inc.
authors.affiliation: Biotechnology Laboratory and Department of Chemical Engineering, The University of British Columbia, 237-6174 University Boulevard, Vancouver, British Columbia, V6T 1Z3, Canada.
authors.forename: A
authors.initials: A
authors.lastname: Wierzba
authors.forename: U
authors.initials: U
authors.lastname: Reichl
authors.forename: R F
authors.initials: RF
authors.lastname: Turner
authors.forename: R A
authors.initials: RA
authors.lastname: Warren
authors.forename: D G
authors.initials: DG
authors.lastname: Kilburn