Using homology-based PCR, we have isolated cDNA encoding a novel member (49
1 amino acids) of the angiopoietin (Ang) family from human adult heart cDNA
and have designated it angiopoietin-3 (Ang3). The NH2-terminal and COOH-te
rminal portions of Ang-3 contain the characteristic coiled-coil domain and
fibrinogen-like domain that are conserved in other known Angs. Ang3 has a h
ighly hydrophobic region at the N-terminus (similar to 21 amino acids) that
is typical of a signal sequence for protein secretion. Ang3 mRNA is most a
bundant in adrenal gland, placenta, thyroid gland, heart and small intestin
e in human adult tissues. Additionally, Ang3 is a secretory protein, but is
not a mitogen in endothelial cells. (C) 1999 Federation of European Bioche
mical Societies.