Isolation of angiopoietin-1, a ligand for the TIE2 receptor, by secretion-trap expression cloning

Article Abstract:

The TIE2 receptor ligand, Angiopoietin-1, was isolated by utilizing a novel secretion-trap expression cloning technique. The receptor-like tyrosine kinase ligand exhibited a coiled-coil structure that is distinct from other angiogenic factors which bind to receptor tyrosine kinases. Furthermore, the ligand did not promote cell proliferation or tubule formation unlike other angiogenic factors. However, Angiopoietin-1 was expressed in developing blood vessels indicating its role in vascularization.

Neovascularization

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The anticoagulation factor protein S and its relative, Gas6, are ligands for the Tyro 3/Axl family of receptor tyrosine kinases

Article Abstract:

A study of ligands for the Tyro3 and Axl receptor-like tyrosine kinases using receptor-based detection and affinity purification methods reveals that the anticoagulation factor protein S binds and stimulates Tyro3, while Gas6, a protein-S-related protein, binds Axl. These and other ligands are bound by other Tyro3 related receptors. The binding and activation of Tyro3 facilitate protein S functions such as anticoagulation or as a mitogen for smooth muscle cells.

Research, Protein tyrosine kinase, Protein-tyrosine kinase, Cooperative binding (Biochemistry)

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Agrin acts via a MuSK receptor complex

Article Abstract:

The muscle-specific kinase (MuSK) receptor is activated by agrin to initiate the formation of neuromuscular junctions. The inability of agrin to induce the clustering acetylcholine receptors in MuSK deficient mice also indicates that MuSK acts further downstream in the agrin signaling pathway. The binding of agrin to MuSK receptors requires myotube-specific components that are not expressed in fibroblast or undifferentiated myoblasts.

Tyrosine in the body, Tyrosine, Neuromuscular junction

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