Molecular cloning and characterization of a novel angiopoietin family protein, angiopoietin-3

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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 (similar to 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. (C) 1999 Federation of European Biochemical Societies.
Publisher
ELSEVIER SCIENCE BV
Issue Date
1999-01
Language
English
Article Type
Article
Keywords

ENDOTHELIAL-CELLS; TIE2 RECEPTOR; ANGIOGENESIS; LIGAND

Citation

FEBS LETTERS, v.443, no.3, pp.353 - 356

ISSN
0014-5793
DOI
10.1016/S0014-5793(99)00008-3
URI
http://hdl.handle.net/10203/77759
Appears in Collection
MSE-Journal Papers(저널논문)
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