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  • Title: Phosphatidylcholine-specific phospholipase C and RhoA are involved in the thyrotropin-induced activation of phospholipase D in FRTL-5 thyroid cells.
    Author: Kim JH, Kim SW, Jung PJ, Yon C, Kim SC, Han JS.
    Journal: Mol Cells; 2002 Oct 31; 14(2):272-80. PubMed ID: 12442901.
    Abstract:
    We investigated the possible involvement of phosphatidylcholine-specific phospholipase C (PC-PLC) in the thyroid-stimulating hormone (TSH)-induced protein kinase C (PKC)/phospholipase D (PLD) activation in FRTL-5 thyroid cells. Treatment of TSH resulted in both dose- and time-dependent increases in PLD activity. TSH induced translocations of PKCalpha and RhoA from the cytosol to the membrane within 30 min. TSH also stimulated diacylglycerol (DAG)/phosphorylcholine (PhoCho) production via PC-PLC. Pretreatment of the cells with D609, a potent inhibitor of PC-PLC, effectively inhibited the translocation of PKCalpha from the cytosol to the membrane and significantly decreased TSH-induced PLD activation. Moreover, C3 transferase, an inhibitor of RhoA, significantly inhibited PLD activity that was stimulated by TSH, which suggests that RhoA is also involved in TSH-induced PLD activation. As we expected, pretreatment of the cells with both C3 transferase and D609 completely inhibited the TSH-induced PLD activity. These findings suggest that DAG that is produced from cellular PC through PC-PLC plays an essential role in the TSH-induced PKC/PLD activation. Also, RhoA and PKCalpha are involved in the regulation of TSH-induced PLD activation in FRTL-5 thyroid cells.
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