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Endostatin, a 20 kDa proteolytic fragment of the C-terminal non-collagenous (NC1) domain of type XVIII collagen, is an endogenous angiogenesis inhibitor. It was originally identified as a factor produced by murine hemangioendothelioma cells that specifically inhibits endothelial cell proliferation and angiogenesis. In wound healing, it inhibits tumor growth and disrupts the maturation of blood vessels. Endostatin plays an important role in endothelial cell adhesion and cytoskeletal organization. It may also be involved in the downregulation of angiogenesis in physiological processes such as wound healing and establishment of placental circulation. The anti-angiogenic activity of endostatin has been attributed to its ability to inhibit endothelial cell proliferation and inhibit VEGF- and bFGF-induced endothelial cell migration and adhesion.
ET-1 has two other isomer families, namely ET-2 and ET-3, the difference lies in individual amino acid residues, and ET-1 plays a major role in cardiovascular.