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Glycobiology Advance Access published online on May 28, 2003
Glycobiology, doi:10.1093/glycob/cwg083
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Submitted on January 20, 2003
Revised on May 20, 2003
Accepted on May 20, 2003

© 2003 Oxford University Press

ORIGINAL ARTICLES

Binding of the CC-chemokine RANTES to syndecan-1 and syndecan-4 expressed on HeLa cells

Hocine Slimani 1, Nathalie Charnaux 1, Elisabeth Mbemba 1, Line Saffar 1, Roger Vassy 2, Claudio Vita 3, Liliane Gattegno 1*

1 Laboratoire de Biologie Cellulaire, Biothérapies Bénéfices et Risques, UPRES 3410, UFR-SMBH, Université Paris XIII, 74, rue Marcel Cachin, 93017, Bobigny, France
2 Laboratoire de Ciblage Fonctionnel des Tumeurs Solides, UPRES 2360, UFR-SMBH, Université Paris XIII, 74, rue Marcel Cachin, 93017, Bobigny, France; Hôpital Jean Verdier, 93017, Bondy, France
3 CEA, Saclay, Département d'Ingénierie et d'Etudes des Protéines, 91191 Gif-sur-Yvette, France

* To whom correspondence should be addressed. E-mail: liliane.gattegno{at}jvr.ap-hop-paris.fr.

Abstract

It is believed that proteoglycans influence biological properties of chemokines. We show that the CC chemokine, RANTES, binds not only to high affinity binding sites on CCR5 positive HeLa cells, but also to low affinity binding sites on HeLa cells, expressing or lacking RANTES G-protein-coupled receptors. Co-immunoprecipitation studies demonstrate that RANTES forms complexes with glycanated syndecan-1 and syndecan-4, in addition to CCR5 on the CCR5 positive HeLa cells. Moreover, confocal microscopy analysis shows the co-localization of RANTES with syndecan-1 and syndecan-4. Glycosaminoglycans removal from the cells by glycosaminidases treatment prevented RANTES binding to syndecan-1 and syndecan-4 and decreased RANTES binding to CCR5 on the CCR5 positive HeLa cells. Removal of glycosaminoglycans by glycosaminidases treatment of the complexes, RANTES/syndecan-1/syndecan-4/+/-CCR5, immobilized on beads, reversed syndecan-1 and syndecan-4 bindings. Therefore, RANTES bindings to syndecan-1 and syndecan-4 depend from glycosaminoglycans and facilitate RANTES interaction with CCR5. Extracting plasma membrane cholesterol abolished the co-immunoprecipitation of syndecan-1 with RANTES, suggesting that rafts are involved in RANTES association to syndecan-1.

Confocal microscopy analysis as well as co-immunoprecipitation experiments show a RANTES-independent heteromeric complex, which comprises on the CCR5 positive HeLa cells, syndecan-1, syndecan-4 and CCR5. This complex is likely a functional unit in which PGs may modulate RANTES binding to CCR5.


CCR5, HIV, RANTES, Syndecans
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