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Originally published In Press as doi:10.1074/jbc.M201068200 on May 13, 2002

J. Biol. Chem., Vol. 277, Issue 29, 26600-26608, July 19, 2002
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Hyaluronan Binding Properties of a CD44 Chimera Containing the Link Module of TSG-6*

Jayne LesleyDagger , Nicole M. EnglishDagger , István Gál§, Katalin Mikecz§, Anthony J. Day||, and Robert HymanDagger

From the Dagger  Molecular and Cell Biology Laboratory, Salk Institute, San Diego, California 92186, the § Departments of Orthopedic Surgery and Biochemistry, Rush University at Rush-Presbyterian-St. Luke's Medical Center, Chicago, Illinois 60612, and the || Medical Research Council Immunochemistry Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom

CD44, a cell-surface receptor for the extracellular matrix glycosaminoglycan hyaluronan, can mediate leukocyte rolling on hyaluronan substrates and has been implicated in leukocyte migration to sites of inflammation. CD44-mediated binding to hyaluronan is of low affinity, and effective cell/matrix interaction depends on multiple interactions with the multivalent ligand. We replaced the Link module of CD44 with the homologous region of TSG-6, a hyaluronan-binding protein secreted in response to inflammation whose Link module has a higher affinity for ligand. Monoclonal antibodies raised against the CD44/TSG-6 chimera recognized recombinant human TSG-6 and native mouse TSG-6 and blocked hyaluronan binding to these proteins. Cells expressing the CD44/TSG-6 molecule bound hyaluronan with higher avidity than cells expressing CD44. This resulted in changes in the hyaluronan binding properties characteristic of cells expressing CD44 such as requirements for threshold levels of receptor expression and for hyaluronan of high molecular mass. In parallel plate flow assays used to model leukocyte rolling, cells expressing CD44/TSG-6 failed to roll on hyaluronan. Instead, they stuck and remained "tethered" to the substrate under fluid flow. This result argues that the low affinity of CD44 for its ligand is important for rolling, an early phase of leukocyte extravasation from the blood.

* This work was supported by NIAID Grants AI-31613 (to R. H.) and AR-45652 (to K. M.) from the National Institutes of Health and by the Medical Research Council, United Kingdom (to A. J. D.). The flow cytometry facilities at the Salk Institute were supported by NCI Cancer Center Grant CA-14195 from the National Institutes of Health and by the H. N. and Frances C. Berger Foundation.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Orthopedic Surgery, Rush University at Rush-Presbyterian-St. Luke's Medical Center, 1653 W. Congress Pkwy., Chicago, IL 60612. Tel.: 312-942-5767; Fax: 312-942-8828; E-mail: kmikecz@rush.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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