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

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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.
Publisher
PORTLAND PRESS
Issue Date
2000-03
Language
English
Article Type
Article
Keywords

RECEPTOR TYROSINE KINASE; MOLECULAR-CLONING; TIE2 RECEPTOR; ANGIOGENESIS; FIBRINOGEN; ANGIOPOIETIN-1; SEQUENCE; DOMAINS; LIGAND

Citation

BIOCHEMICAL JOURNAL, v.346, pp.603 - 610

ISSN
0264-6021
DOI
10.1042/0264-6021:3460603
URI
http://hdl.handle.net/10203/77573
Appears in Collection
MSE-Journal Papers(저널논문)
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