Premium
Molecular cloning and characterization of a novel angiopoietin family protein, angiopoietin‐3
Author(s) -
Kim Injune,
Kwak Hee Jin,
Ahn Ji Eun,
So June-No,
Liu Mingzhu,
Koh Keum Nim,
Koh Gou Young
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00008-3
Subject(s) - complementary dna , amino acid , homology (biology) , biology , peptide sequence , cloning (programming) , gene , microbiology and biotechnology , secretion , signal peptide , angiopoietin , biochemistry , computer science , programming language , vascular endothelial growth factor , cancer research , vegf receptors
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 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. 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.