Key result
The C-terminal domain of thrombopoietin appears to regulate its specific activity, circulating half-life, and promote efficient biosynthesis and secretion compared to truncated forms.
Population
Recombinant Thrombopoietin (TPO) proteins produced in cell culture
Comparison
C-terminally truncated TPO proteins vs Full-length intact TPO (70 kDa glycoprotein)
Design
Preclinical
Authors
Loading...
Should not alter clinical practice; leaves open whether C-terminal modifications enhance thrombopoietin in humans.
The C-terminal domain of thrombopoietin is essential for regulating its specific activity, circulating half-life, and efficient biosynthesis and secretion.
Foster et al. (1996) studied this question. C-terminally truncated TPO proteins vs. Full-length intact TPO was evaluated on Specific activity, circulating half-life, and biosynthesis/secretion. The C-terminal domain of thrombopoietin appears to regulate its specific activity, circulating half-life, and promote efficient biosynthesis and secretion compared to truncated forms.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: