Posttranslational Modifications Limit High Level Expression of Functionally Active Chimeric P-Selectin Glycoprotein Ligand-1 in rCHO Cells

Autor: TroyZ Richards, Mark R. Hardy, Steve Koza, Deb Ellis, Martin S. Sinacore, Scott Harrison, Linda Francullo, Monique Davies, Richard J. Cornell, Amy Woodard
Rok vydání: 2008
Předmět:
Zdroj: Animal Cell Technology: Products from Cells, Cells as Products ISBN: 9780792360759
DOI: 10.1007/0-306-46875-1_53
Popis: P-Selectin Glycoprotein Ligand-1 (PSGL-1) is a dimeric mucin-like transmembrane glycoprotein identified as a functional ligand for P-Selectin (1). Functional activity of PSGL-1 is dependent upon at least two key posttranslational modifications made to the amino terminus. Core 2 O-linked oligosaccharide structures at Thr16 bearing the sialyl-Lewisx (SLex) antigen and sulfation of one or more of the NH2-terminal tyrosine it has been shown that a polypeptide containing the NH2-terminal 47 amino acid sequence of human PSGL-1 is sufficient for high-affinity binding to P-Selectin (2).
Databáze: OpenAIRE