Tyrosine-protein kinase receptor TEK (Tie2)

Tyrosine-protein kinase receptor TEK (Tie2) is a member of the receptor tyrosine kinase family predominantly expressed on endothelial cells lining blood vessels. It features a unique extracellular domain with immunoglobulin-like loops, EGF-like repeats, and fibronectin type III domains. Its primary ligands are the angiopoietins—especially Angiopoietin‑1—which regulate key processes such as blood vessel maturation, stability, permeability, and branching during development and adult tissue maintenance. Mutations or dysregulation can lead to inherited vascular malformations or contribute to pathological neovascularization seen in cancer. The protein is also found at lower levels outside the vasculature—including certain tumor cells—and plays roles in hematopoietic stem cell biology within bone marrow. Because it is central to both physiological and pathological blood vessel formation, it remains an important therapeutic target for antiangiogenic strategies across oncology and vascular medicine.

Other names

Angiopoietin-1 receptorCD202BTIE2TEK tyrosine kinase, endothelialp140 TEK

Drugs or biologics targeting this molecule typically act by inhibiting its tyrosine kinase activity or blocking ligand binding (e.g., inhibition of angiopoietin-Tie2 signaling), leading to reduced angiogenesis and tumor vascularization.