| 摘要 |
It has been discovered that the heparan sulfate chains of proteoglycans vary markedly from one cell type to another and these differences can be exploited for therapeutic and/or diagnostic purposes. In particular, the heparan sulfate chains of cell surface proteoglycans, such as the integral membrane protein, syndecan, isolated from various cells differ not only in size but also in chemical structure (e.g., specific disaccharide composition and distribution). These structural differences appear to be a basis for differences in binding affinity of specific types of cells for particular ligands, and thereby permit the isolation and/or construction of decays, agonists, antagonists and other substrates which can influence or measure biological activity. |
