Abstract
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 (approximately 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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adult
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Amino Acid Sequence
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Angiopoietin-1
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Angiopoietin-2
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Angiopoietin-Like Protein 1
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Angiopoietin-like Proteins
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Angiopoietins
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Cell Line
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Cloning, Molecular*
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Culture Media, Conditioned / pharmacology
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DNA / biosynthesis
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Endothelium / cytology
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Gene Expression
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Heart
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Humans
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Intercellular Signaling Peptides and Proteins*
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Membrane Glycoproteins / chemistry
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Membrane Glycoproteins / genetics
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Mitogens / physiology
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Molecular Sequence Data
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Protein Sorting Signals / genetics
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Proteins / chemistry
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Proteins / genetics*
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Proteins / metabolism
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RNA, Messenger / analysis
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Receptor Protein-Tyrosine Kinases / physiology
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Receptor, TIE-2
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Sequence Homology, Amino Acid
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Transfection
Substances
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ANGPT1 protein, human
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ANGPTL1 protein, human
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Angiopoietin-1
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Angiopoietin-2
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Angiopoietin-Like Protein 1
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Angiopoietin-like Proteins
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Angiopoietins
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Culture Media, Conditioned
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Intercellular Signaling Peptides and Proteins
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Membrane Glycoproteins
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Mitogens
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Protein Sorting Signals
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Proteins
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RNA, Messenger
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DNA
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Receptor Protein-Tyrosine Kinases
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Receptor, TIE-2