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Platelet-derived growth factor in vivo: levels, activity, and rate of
clearance
DF Bowen-Pope, TW Malpass, DM Foster and R Ross
Platelet-derived growth factor (PDGF) is a potent mitogen for many cultured
connective tissue cells. It is present in concentrated form within the
platelet alpha-granules and is believed to be released during platelet
degranulation at sites of vascular injury. We have used a sensitive
radioreceptor assay to measure PDGF levels in whole blood serum from normal
humans [17.5 +/- 3.1 (SD) ng/mL] and baboons (2.7 +/- 1.2 ng/mL). PDGF was
not detected in plasma from either species. In addition, plasma was found
to substantially reduce the ability of added purified PDGF to bind to the
cell surface PDGF receptor on cultured cells, suggesting that plasma may
contain a PDGF-binding protein that would serve to inactivate PDGF released
into plasma. Calculations of PDGF concentrations in serum have been
corrected for the effects of the binding protein. 125I-PDGF injected
intravenously into normal baboons was cleared rapidly from the plasma (t1/2
= two minutes). The rapid clearance of 125I-PDGF did not result from
iodination damage, as purified unlabeled PDGF was cleared with comparable
kinetics. The rapid clearance of purified and iodinated PDGF did not result
from changes in PDGF structure during purification or from removal of
PDGF-associated proteins during purification, as PDGF present in
freeze-thaw lysates of fresh platelets was cleared equally rapidly. We
conclude that release of PDGF at sites of vascular injury would greatly
increase the local concentration of PDGF and that PDGF not localized to the
site of injury would be rapidly cleared from the circulation.
Volume 64,
Issue 2,
pp. 458-469,
08/01/1984
Copyright © 1984 by The American Society of Hematology
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