Abstract
We investigated the modulation of platelet-derived growth factor (PDGF) receptor dephosphorylation in Swiss 3T3 cells using a novel assay permitting monitoring of receptor dephosphorylation in intact cells. PDGF treatment of the cells reduced the receptor dephospphorylation rate to 41%, the elevators of intracellular Ca 2+, A23187 and thapsigargin increasing it to 227 and 138%, respectively. The cAMP elevators forskolin and isobutylmethylxanthine also accelerated PDGF receptor dephosphorylation. The involvement of Ca 2+- and cAMP-dependent protein kinases in the regulation of PDGF receptor dephosphorylation is suggested.
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