Thrombospondin-1–CD36 protein–protein interaction (TSP-1–CD36 interaction)

The **Thrombospondin-1–CD36 protein–protein interaction** refers to the binding between the type 1 repeats (TSR) of the extracellular matrix glycoprotein thrombospondin-1 (TSP-1) and a specific extracellular CLESH domain of the transmembrane receptor CD36 on microvascular endothelial cells. This interaction triggers an intracellular signaling cascade involving recruitment of the protein tyrosine phosphatase SHP-1, leading to dephosphorylation and inhibition of vascular endothelial growth factor receptor 2 (VEGFR2) signaling. As a result, endothelial cell migration, proliferation, and vessel formation are suppressed[1][3][6]. The TSP-1–CD36 axis is a well-characterized anti-angiogenic pathway, making it a key therapeutic target in diseases where abnormal angiogenesis plays a role, including many cancers and certain eye or cardiovascular diseases. Pharmacological mimetics that exploit this pathway aim to reproduce the anti-angiogenic and pro-apoptotic signals by targeting CD36 with TSP-1–derived peptides or small molecules.

Other names

Thrombospondin-1–CD36 bindingTSP-1–CD36 complexThrombospondin-1 type 1 repeat–CD36 interactionTSP1–CD36 PPI

Anti-angiogenic (inhibition of endothelial migration and tube formation via CD36 engagement); Induction of apoptosis in endothelial cells; Blockade of VEGF–VEGFR2 signaling (via SHP-1 recruitment) [3][6]