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Biosynthesis and secretion of factor VII, protein C, protein S, and the
Protein C inhibitor from a human hepatoma cell line
DS Fair and RA Marlar
Using specific radioimmunoassays, 8 day cultures of Hep G2 cells were shown
to contain in their supernatants 16, 74, and 828 ng/mL and in their cell
lysates, 8, 55, and 48 ng/2 X 10(8) cells of factor VII, protein C, and
protein S, respectively. These proteins and the protein C inhibitor were
functionally active, and each of these activities was neutralized by their
respective polyclonal antibodies. Although vitamin K had a modest effect,
warfarin decreased the activity of secreted factor VII, protein C, and
protein S by 50% to 90%. Protein C and protein S antigens were reduced
three- to fourfold by warfarin. The protein C inhibitor antigen and
activity were unaffected by vitamin K or warfarin treatment. Intrinsic
labeling and immunoprecipitation indicated that factor VII, protein S, and
the protein C inhibitor were secreted as 52,000, 77,000, and 58,000
molecular weight (mol wt) proteins, respectively. Protein C was secreted as
a single-chain protein of about 65,000 mol wt, indicating that all of the
vitamin K- dependent proteins are translated and secreted as single-chain
molecules. Each of the four proteins studied represented their plasma
protein counterparts structurally, functionally, and immunochemically.
Thus, all of the known soluble components of the protein C pathway are
produced by liver parenchymal cells.
Volume 67,
Issue 1,
pp. 64-70,
01/01/1986
Copyright © 1986 by The American Society of Hematology
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