Endostatin (C-terminal fragment of collagen XVIII) (ES)

Endostatin is a naturally occurring, 20-kDa C-terminal fragment of collagen XVIII, released through proteolytic cleavage in the extracellular matrix[1][3][5][8]. It is regarded as one of the most potent inhibitors of angiogenesis, acting predominantly by binding to endothelial cell surface receptors including integrins (αvβ3, α5β1), glypicans (heparan sulfate proteoglycans), and VEGF receptors to block proliferation, migration, invasion, and tube formation of vascular endothelial cells, and to promote apoptosis[2][3][4][8]. Endostatin also interacts with matrix metalloproteinases, inhibiting their activity and further dampening extracellular matrix remodeling and angiogenic responses[8]. In cancer therapy, recombinant human endostatin (Endostar) is approved in China for lung cancer, demonstrating anti-tumor efficacy mainly via anti-angiogenic and immunomodulatory effects[3][5][8]. Endostatin's fragment origin, receptor binding specificity, and broad regulatory functions in angiogenesis and the tumor microenvironment make it a unique molecular target in oncology and vascular biology.

Other names

EndostatinESC-terminal fragment of collagen XVIIIRecombinant human endostatin (Endostar, a modified form)

Binds and blocks VEGF receptors (VEGFR2, VEGFR3), interfering with VEGF-C and VEGF-induced angiogenic signaling; Inhibits FGF (fibroblast growth factor)-induced signaling; Binds integrins (αvβ3, α5β1) on endothelial cells, blocking cell migration and survival; Inhibits matrix metalloproteinases (MMP-2, MMP-9, MMP-13, and MT1-MMP) catalytic activity, thus indirectly suppressing ECM remodeling and angiogenesis; Induces endothelial cell apoptosis and halts cell cycle progression; Modulates immune cell function, promoting anti-tumor M1 macrophage polarization