Glycobiology, 2000, Vol. 10, No. 1 21-29
© 2000 Oxford University Press
Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1
Laboratoire de Biologie Cellulaire JE 2138, Université Paris 13, Faculté de Médecine, 93017 Bobigny, France and 2ESA 7087, Université Paris 6-Centre National de la Recherche Scientifique and Laboratoire d’Immunologie Cellulaire de l’Ecole Pratique des Hautes Etudes, Hôpital Pitié-Salpêtrière, 75651 Paris Cedex 13, France
We show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1
to CD4+ lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1 binding by 40–41% and 31–35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1 binding to the cells by 45–52% and 42–56%, respectively, while dextran has no significant effect. Taken together, these results indicate the role of GAGs in SDF-1 attachment to the cells. However, the effects of heparitinase and chondroitinase as well as those of heparin and chondroitin sulfate are not additive, which suggests that SDF-1 may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1 binding to the cells by 30–33%. Additivity between this effect and that of heparin or chondroitin sulfate is observed. Therefore, beside GAGs, mannose-containing species may also be involved in SDF-1 attachment to the cells. Accordingly, SDF-1 specifically binds to heparin-agarose and mannose-divinylsulfone agarose affinity matrices, and these interactions are inhibited respectively by soluble heparin, chondroitin sulfate, and mannan. We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin. The present data therefore indicate that, in the same manner as HIV-1 Env, SDF-1 can interact with GAGs and glycans at the cell surface.
1 To whom correspondence should be addressed at: School of Medicine, 74 Rue Marcel Cachin, 93017 Bobigny, France
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