Using homology-based PCR, we have isolated cDNA encoding a novel member (491 amino acids) of the angiopoietin (Ang) family from human adult heart cDNA and have designated it angiopoietin-3 (Ang3). The NH2-terminal and COOH-terminal portions of Ang-3 contain the characteristic coiled-coil domain and fibrinogen-like domain that are conserved in other known Angs. Ang3 has a highly hydrophobic region at the N-terminus (~21 amino acids) that is typical of a signal sequence for protein secretion. Ang3 mRNA is most abundant in adrenal gland, placenta, thyroid gland, heart and small intestine in human adult tissues. Additionally, Ang3 is a secretory protein, but is not a mitogen in endothelial cells. Copyright (C) 1999 Federation of European Biochemical Societies.
Kim, I., Kwak, H. J., Ahn, J. E., So, J. N., Liu, M., Koh, K. N., & Koh, G. Y. (1999). Molecular cloning and characterization of a novel angiopoietin family protein, angiopoietin-3. FEBS Letters, 443(3), 353–356. https://doi.org/10.1016/S0014-5793(99)00008-3