| Primary Identifier | IPR028499 | Type | Family |
| Short Name | Thrombospondin-1 |
| description | Thrombospondin 1 (TSP-1) is a member of the thrombospondin (TSP) family, which consists of five extracellular calcium-binding multifunctional proteins: TSP-1, TSP-2, TSP-3, TSP-4, and TSP-5. TSP-1 is involved in angiogenesis, cancer, and inflammation. It is a major activator of transforming growth factor (TGFbeta1), which mediates wound healing, cell proliferation, extracellular matrix formation, and the immune response [].TSP-1 is a large, homotrimeric molecule. Each monomer consists of an N-terminal globular domain that binds heparin, type I, type II, and type III repeats, and a C-terminal globular domain. All five members of the TSP family have the repeat domains type II and III, but only TSP-1 and TSP-2 contain the type I repeats []. TSP-1-specific domains bind to proteoglycans, membrane proteins such as integrins, and other matrix proteins expressed by a variety of cells [, ]. Type I repeats, also called thrombospondin structural homology repeats (TSRs), inhibit angiogenesis by activating CD36 and inducing apoptosis in endothelial cells []. |
