TSP1s

TSP1s, also known as Thrombospondin-1, are secreted proteins belonging to the thrombospondin family. These proteins are involved in a wide array of biological processes, including angiogenesis, inflammation, cell adhesion, and wound healing. TSP1 is a matricellular protein, meaning it is a secreted protein that is not a structural component of the extracellular matrix but rather modulates the interactions of cells with the matrix.

TSP1 is a large glycoprotein that forms disulfide-linked trimers. It is expressed by various cell types, including endothelial cells, platelets, and fibroblasts. Its functions are mediated through interactions with a variety of cell surface receptors and matrix components, such as CD36, integrins, and heparin.

One of the most well-studied roles of TSP1 is its potent anti-angiogenic activity. It inhibits the formation of new blood vessels by directly interfering with endothelial cell proliferation, migration, and survival. This anti-angiogenic property has made TSP1 a target of research for cancer therapy, aiming to starve tumors by preventing blood supply.

Beyond angiogenesis, TSP1 plays a role in immune modulation by promoting the differentiation of regulatory T cells and suppressing inflammatory responses. It also participates in hemostasis and thrombosis by interacting with platelets and components of the coagulation cascade. Furthermore, TSP1 is implicated in tissue repair and fibrosis, influencing fibroblast behavior and extracellular matrix deposition. Dysregulation of TSP1 has been associated with various diseases, including cancer, arthritis, and cardiovascular disease.