Role of the Sulfation Pattern of Chondroitin Sulfate in its Biological Activities and in the Binding of Growth Factors

Abstract

This chapter reviews the structural characteristics of various chondroitin sulfate (CS) chains and their binding activity toward growth factors based on available data. CS variants exhibit typical patterns of binding to growth factors and neurotrophic factors, when tested using the BIAcore or the interaction analysis system (IAsys). Heparan sulfate (HS) and CS chains in a proteoglycan (PG) show synergistic effects by complementing or cooperating with each other in the binding of a growth factor through dynamic interactions. The presence of iduronic acid results in better binding of growth factors. However, for a more efficient binding, a domain consisting of both glucuronic acid and iduronic acid appears to be essential. Various monoclonal antibodies, directed against CS variants, have been generated, which has contributed greatly to the localization of CS chains in various tissues. Antibodies, such as CS‐56 and MO‐225, have been widely used in detecting CS variants.