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 (Ang
3). The NH
2-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. Ang
3 has a highly hydrophobic region at the N-terminus (
![](/images/glyphs/BQ1.GIF)
21 amino acids) that is typical of a signal sequence for
protein secretion. Ang
3 mRNA is most abundant in adrenal gland, placenta, thyroid gland, heart and small intestine in human adult tissues. Additionally, Ang
3 is a secretory
protein, but is not a mitogen in endothelial cells.