TEK receptor tyrosine kinase (Tie2) (Tie2)

The TEK receptor tyrosine kinase, commonly known as Tie2, is a critical cell-surface receptor primarily expressed on vascular endothelial cells. It serves as the primary receptor for the angiopoietin family of growth factors, specifically Angiopoietin-1 (an agonist) and Angiopoietin-2 (a context-dependent antagonist). Tie2 signaling is essential for maintaining vascular integrity, promoting endothelial cell survival, and regulating both physiological and pathological angiogenesis. In diseases such as cancer and diabetic retinopathy, dysregulation of the Tie2 pathway leads to vessel destabilization and abnormal growth, making it a significant therapeutic target. Drugs targeting this pathway include monoclonal antibodies, peptibodies, and small molecules that either activate Tie2 to stabilize vessels or inhibit its ligands to suppress tumor-associated blood vessel formation. The inclusion of "other heparin-binding extracellular proteins" in the target name likely refers to the broader interactome of Tie2 and its ligands, as many angiogenic factors (like VEGF and FGF) and even some Tie2 ligands (like Ang3) are sequestered or modulated by heparan sulfate proteoglycans on the cell surface.

Other names

TEKCD202BAngiopoietin-1 receptorTunica interna endothelial cell kinaseTyrosine kinase with Ig and EGF homology domains-2

Tie2 activation (agonism) promotes vascular stability and endothelial cell survival, while Tie2 inhibition (antagonism) or sequestration of its ligands (Ang1/Ang2) can inhibit pathological angiogenesis and increase vascular permeability.