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J. Biol. Chem., Vol. 261, Issue 21, 9579-9582, 07, 1986
TO Daniel, VC Gibbs, DF Milfay, MR Garovoy and LT Williams
We have determined whether expression of the c-sis gene product,
platelet-derived growth factor (PDGF), is regulated in cultured renal
microvascular endothelial cells by factors to which vascular endothelial
cells may be exposed at sites of perivascular cellular proliferation.
Thrombin exposure increased endothelial cell levels of c- sis message by
3-5-fold over a time course that peaked at 4 h after exposure. Similarly,
thrombin-exposed microvascular endothelial cells released increased amounts
of PDGF activity into their media. The thrombin effect was not mediated
through the proteolytic activity of thrombin, as proteolytically inactive
thrombin stimulated the c-sis expression as well as native thrombin. This
stimulation was mimicked by exposure of cells to biologically active
phorbol esters, suggesting that thrombin action may be mediated through
activation of kinase C (Ca2+/phospholipid-dependent enzyme). Thus, thrombin
regulates the expression and release of PDGF activity from endothelial
cells in culture and may act in vivo to stimulate mitogen release from
endothelial cells, thereby inducing proliferation of perivascular cells.
Thrombin stimulates c-sis gene expression in microvascular endothelial cells
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