Effect of platelet-derived growth factor on XXXX -hydrolyzing phospholipase D in osteoblast-like cells.

@entity864 @entity47150 @entity46365 @entity670 @entity19 @entity2434 @entity7131 @entity4621 @entity1877 @entity10913 @entity141 @entity669 @entity2945 @entity7256
We examined the effect of platelet-derived growth factor (PDGF) on the activation of @entity2434 -hydrolyzing phospholipase D in osteoblast-like @entity19 cells. PDGF-BB stimulated both the formation of @entity1877 (EC50 = 15 ng/ml) and @entity7256 (EC50 = 5 ng/ml). However, PDGF-BB had little effect on the formation of @entity2945 . The formation of @entity1877 stimulated by a combination of PDGF-BB and @entity864 , a @entity7131 ( @entity7131 )-activating @entity4621 , was additive. H-7, an inhibitor of protein kinases, inhibited @entity864 -induced @entity1877 formation, whereas @entity46365 , a control for H-7 as @entity7131 inhibitor, had little effect. Neither H-7 nor @entity46365 affected the PDGF-BB-induced formation of @entity1877 . @entity670 and @entity10913 , inhibitors of protein @entity669 kinases, dose dependently inhibited the PDGF-BB-induced formation of @entity1877 . PDGF-BB stimulated @entity141 influx from extracellular space. PDGF-BB-induced @entity1877 formation was significantly reduced by chelating extracellular @entity141 with EGTA. PDGF-BB stimulated DNA synthesis of MC3YT @entity19 cells, and H-7 inhibited the DNA synthesis. These results strongly suggest that PDGF activates @entity47150 - @entity1877 -hydrolyzing phospholipase D independently from @entity7131 activated by phosphoinositide hydrolysis in osteoblast-like cells, and that both @entity669 kinase activation and @entity141 influx are essential for this mechanism.
