| First Author | Narouz-Ott L | Year | 2000 |
| Journal | J Biol Chem | Volume | 275 |
| Issue | 47 | Pages | 37110-7 |
| PubMed ID | 10956668 | Mgi Jnum | J:383764 |
| Mgi Id | MGI:8327705 | Doi | 10.1074/jbc.M007223200 |
| Citation | Narouz-Ott L, et al. (2000) Thrombospondin-4 binds specifically to both collagenous and non-collagenous extracellular matrix proteins via its C-terminal domains. J Biol Chem 275(47):37110-7 |
| abstractText | Full-length and truncated forms of rat thrombospondin-4 (TSP-4) were expressed recombinantly in a mammalian cell line and purified to homogeneity. Biochemical analysis revealed a limited proteolytic processing, which detaches the N-terminal heparin-binding domain from the rest of the molecule and confirmed the importance of the heptad-repeat domain for pentamerization. In electron microscopy the uncleaved TSP-4 was seen as a large central particle to which five smaller globules are attached by elongated linker regions. Binding of TSP-4 to collagens and to non-collagenous proteins could be detected in enzyme-linked immunosorbent assay-style ligand binding assays, by surface plasmon resonance spectroscopy, and in rotary shadowing electron microscopy. Although the binding of TSP-4 to solid-phase collagens was enhanced by Zn(2+), that to non-collagenous proteins was not. The interactions of TSP-4 with both classes of proteins are mediated by C-terminal domains of the TSP-4 subunits but do not require an oligomeric structure. Major binding sites for TSP-4 are located in or close to the N- and C-terminal telopeptides in collagen I, but additional sites are detected in more central regions of the molecule. |
