Glycan and glycosaminoglycan binding properties of stromal cell-derived factor (SDF)-1alpha

Glycobiology. 2000 Jan;10(1):21-9. doi: 10.1093/glycob/10.1.21.


We show here that cell surface glycosaminoglycans (GAGs) are involved in the binding of stromal cell-derived factor (SDF)-1alpha to CD4(+)lymphoid CEM or monocytic U937 cells, inasmuch as pretreating the cells with heparitinase or chondroitinase inhibits SDF-1alpha binding by 40-41% and 31-35%, respectively. Soluble heparin or chondroitin sulfate partially but significantly inhibits SDF-1alpha 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-1alpha 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-1alpha may attach to the cells through different GAGs, and also through other ligands. Soluble mannan also inhibits SDF-1alpha 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-1alpha attachment to the cells. Accordingly, SDF-1alpha 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-1alpha can interact with GAGs and glycans at the cell surface.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Line
  • Chemokine CXCL12
  • Chemokines, CXC / chemistry
  • Chemokines, CXC / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Glycosaminoglycans / metabolism*
  • Humans
  • Molecular Sequence Data
  • Polysaccharides / metabolism*
  • Protein Binding
  • Sepharose / analogs & derivatives
  • Sepharose / metabolism


  • CXCL12 protein, human
  • Chemokine CXCL12
  • Chemokines, CXC
  • Glycosaminoglycans
  • Polysaccharides
  • heparin-sepharose
  • Sepharose