Hepatic expression, synthesis and secretion of a novel fibrinogen/angiopoietin-related protein that prevents endothelial-cell apoptosis

Using degenerate PCR we isolated a cDNA encoding a novel 406- and 410-amino acid protein from human and mouse embryonic cDNAs and have designated it 'hepatic fibrinogen/angiopoietin-related protein' (HFARP). The N-terminal and C-terminal portions of HFARP contain the characteristic coiled-...

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Bibliographic Details
Published in:Biochemical journal 2000-03, Vol.346 Pt 3 (3), p.603-610
Main Authors: Kim, I, Kim, H G, Kim, H, Kim, H H, Park, S K, Uhm, C S, Lee, Z H, Koh, G Y
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Angiopoietin-like 4 Protein
Angiopoietin-like Proteins
Angiopoietins
Animals
Apoptosis
Blood Proteins - chemistry
Blood Proteins - genetics
Blood Proteins - metabolism
Cells, Cultured
Cloning, Molecular
DNA Replication
DNA, Complementary
Endothelium, Vascular - cytology
Humans
Intercellular Signaling Peptides and Proteins
Liver - metabolism
Mice
Molecular Sequence Data
Protein Binding
Receptor Protein-Tyrosine Kinases - metabolism
Receptor, TIE-1
Receptor, TIE-2
Receptors, Cell Surface - metabolism
Receptors, TIE
RNA, Messenger - genetics
RNA, Messenger - metabolism
Sequence Homology, Amino Acid
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Summary:Using degenerate PCR we isolated a cDNA encoding a novel 406- and 410-amino acid protein from human and mouse embryonic cDNAs and have designated it 'hepatic fibrinogen/angiopoietin-related protein' (HFARP). The N-terminal and C-terminal portions of HFARP contain the characteristic coiled-coil domains and fibrinogen-like domains that are conserved in angiopoietins. In human and mouse tissues, HFARP mRNA is specifically expressed in the liver. HFARP mRNA and protein are mainly present in the hepatocytes. HFARP has a highly hydrophobic region at the N-terminus that is typical of a secretory signal sequence and one consensus glycosylation site. Recombinant HFARP expressed in COS-7 cells is secreted and glycosylated. HFARP protein is present not only in the hepatocytes, but also in the circulating blood. Recombinant HFARP acts as an apoptosis survival factor for vascular endothelial cells, but does not bind to Tie1 or Tie2 (endothelial-cell tyrosine kinase receptors). These results suggest that HFARP may exert a protective function on endothelial cells through an endocrine action.
ISSN:0264-6021
1470-8728
DOI:10.1042/0264-6021:3460603