JBC Invitrogen Ultrasensitive Cytokine Assays

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J Biol Chem, Vol. 274, Issue 16, 11237-11244, April 16, 1999

Recombinant Glycoproteins That Inhibit Complement Activation and Also Bind the Selectin Adhesion Molecules

Charles W. Rittershaus, Lawrence J. Thomas, David P. Miller, Michele D. Picard, Kathleen M. Geoghegan-Barek, Susanne M. Scesney, Larry D. Henry, Asok C. Sen, Amy M. Bertino, Gerhard Hannig, Hedy Adari, Richard A. Mealey, Michael L. Gosselin, Mintas Couto, Edward G. Hayman, James L. Levin, Vernon N. ReinholdDagger , and Henry C. Marsh Jr.

From the Avant Immunotherapeutics, Inc., Needham, Massachusetts 02494-2725 and the Dagger  Department of Chemistry, University of New Hampshire, Durham, New Hampshire 02824-3598

Soluble human complement receptor type 1 (sCR1, TP10) has been expressed in Chinese hamster ovary (CHO) DUKX-B11 cells and shown to inhibit the classical and alternative complement pathways in vitro and in vivo. A truncated version of sCR1 lacking the long homologous repeat-A domain (LHR-A) containing the C4b binding site has similarly been expressed and designated sCR1[desLHR-A]. sCR1[desLHR-A] was shown to be a selective inhibitor of the alternative complement pathway in vitro and to function in vivo. In this study, sCR1 and sCR1[desLHR-A] were expressed in CHO LEC11 cells with an active alpha (1,3)-fucosyltransferase, which makes possible the biosynthesis of the sialyl-Lewisx (sLex) tetrasaccharide (NeuNAcalpha 2-3Galbeta 1-4(Fucalpha 1-3)GlcNAc) during post-translational glycosylation. The resulting glycoproteins, designated sCR1sLex and sCR1[desLHR-A]sLex, respectively, retained the complement regulatory activities of their DUKX B11 counterparts, which lack alpha (1-3)-fucose. Carbohydrate analysis of purified sCR1sLex and sCR1[desLHR-A]sLex indicated an average incorporation of 10 and 8 mol of sLex/mol of glycoprotein, respectively. sLex is a carbohydrate ligand for the selectin adhesion molecules. sCR1sLex was shown to specifically bind CHO cells expressing cell surface E-selectin. sCR1[desLHR-A]sLex inhibited the binding of the monocytic cell line U937 to human aortic endothelial cells, which had been activated with tumor necrosis factor-alpha to up-regulate the expression of E-selectin. sCR1sLex inhibited the binding of U937 cells to surface-adsorbed P-selectin-IgG. sCR1sLex and sCR1[desLHR-A]sLex have thus demonstrated both complement regulatory activity and the capacity to bind selectins and to inhibit selectin-mediated cell adhesion in vitro.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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