Related Experiment Video
Updated: Jul 11, 2026

RhoC GTPase Activation Assay
Published on: August 23, 2010
Glycans are involved in RANTES binding to CCR5 positive as well as to CCR5 negative cells
E Mbemba1, H Slimani, A Atemezem
1Laboratoire de Biologie Cellulaire JE 2138, Faculté de Médecine, Université Paris XIII, 74 rue Marcel Cachin, 93017 Bobigny, France.
Abstract:
We show that cell surface glycans, sialic acid and mannose-containing species, are involved beside glycosaminoglycans (GAGs), heparan sulfate and chondroitin sulfate in the binding of full length (1--68) RANTES not only to CCR5 positive human primary lymphocytes or macrophages but also to CCR5 negative monocytic U937 cells. Pretreating the cells with neuraminidase, heparitinase, chondroitinase or adding soluble glycans such as mannan or GAGs (heparin or chondroitin sulfate), significantly inhibited RANTES binding. Such effects were not observed with truncated (10--68) RANTES. Heat-denaturation of (1--68) RANTES strongly decreased its binding to the cells, demonstrating involvement of the three-dimensional structure. Accordingly, full length, but not truncated (10--68) RANTES, specifically bound to soluble mannan as well as to mannose-divinylsulfone-agarose affinity matrix and to soluble heparin or chondroitin sulfate as well as to heparin-agarose. Soluble heparin exerts, depending on its concentration, inhibitory or enhancing effects on RANTES binding to mannose-divinylsulfone-agarose, which indicates that RANTES interaction with glycans is modulated by GAGs. These data demonstrate that full length RANTES, but not its (10--68) truncated counterpart, interacts with glycans and GAGs, in soluble forms or presented either by affinity matrices or CCR5 positive as well as CCR5 negative cells.
More Related Videos
06:56A Flow Cytometry-based Assay to Identify Compounds That Disrupt Binding of Fluorescently-labeled CXC Chemokine Ligand 12 to CXC Chemokine Receptor 4
Published on: March 10, 2018
09:12Efficient Retroviral Transduction and Competitive Homing for Investigating GPCR-Mediated T-Cell Localization in Diverse Tissue Microenvironments
Published on: March 28, 2025
Related Concept Videos
Rab Proteins
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
The Ras Gene
Ras is a superfamily...
Cell Polarization by Rho Proteins
Rab Cascades
Small GTPases - Ras and Rho
Three regulatory proteins control their activity:
Selectins