Top

Research Article

Split Viewer

Mol. Cells 2002; 14(2): 272-280

Published online October 31, 2002

© The Korean Society for Molecular and Cellular Biology

Phosphatidylcholine-specific Phospholipase C and RhoA Are Involved in the Thyrotropin-induced Activation of Phospholipase D in FRTL-5 Thyroid Cells

Jong-Hoon Kim, Sang Woo Kim, Pa Jong Jung, Changsuek Yon, Sang-Chul Kim, Joong-Soo Han

Abstract

We investigated the possible involvement of phos-phatidylcholine-specific phospholipase C (PC-PLC) in the thyroid-stimulating hormone (TSH)-induced pro-tein 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 activ-ity. TSH induced translocations of PKCa and RhoA from the cytosol to the membrane within 30 min. TSH also stimulated diacylglycerol (DAG)/phosphorylcho-line (PhoCho) production via PC-PLC. Pretreatment of the cells with D609, a potent inhibitor of PC-PLC, effectively inhibited the translocation of PKCa from the cytosol to the membrane and significantly de-creased TSH-induced PLD activation. Moreover, C3 transferase, an inhibitor of RhoA, significantly inhib-ited 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 find-ings 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 PKCa are involved in the regulation of TSH-induced PLD activation in FRTL-5 thyroid cells.

Keywords Phosphatidylcholine-specific Phospholipase C, Phos

Article

Research Article

Mol. Cells 2002; 14(2): 272-280

Published online October 31, 2002

Copyright © The Korean Society for Molecular and Cellular Biology.

Phosphatidylcholine-specific Phospholipase C and RhoA Are Involved in the Thyrotropin-induced Activation of Phospholipase D in FRTL-5 Thyroid Cells

Jong-Hoon Kim, Sang Woo Kim, Pa Jong Jung, Changsuek Yon, Sang-Chul Kim, Joong-Soo Han

Abstract

We investigated the possible involvement of phos-phatidylcholine-specific phospholipase C (PC-PLC) in the thyroid-stimulating hormone (TSH)-induced pro-tein 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 activ-ity. TSH induced translocations of PKCa and RhoA from the cytosol to the membrane within 30 min. TSH also stimulated diacylglycerol (DAG)/phosphorylcho-line (PhoCho) production via PC-PLC. Pretreatment of the cells with D609, a potent inhibitor of PC-PLC, effectively inhibited the translocation of PKCa from the cytosol to the membrane and significantly de-creased TSH-induced PLD activation. Moreover, C3 transferase, an inhibitor of RhoA, significantly inhib-ited 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 find-ings 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 PKCa are involved in the regulation of TSH-induced PLD activation in FRTL-5 thyroid cells.

Keywords: Phosphatidylcholine-specific Phospholipase C, Phos

Mol. Cells
Sep 30, 2021 Vol.44 No.9, pp. 627~698
COVER PICTURE
Non-mitochondrial localization of the N-terminal-deleted mutant form of ACSL1 in Cos7 cells. Green, ACSL1 mutant; Red, mitotracker; Blue, DAPI (Nan et al., pp. 637-646).

Share this article on

  • line
  • mail

Related articles in Mol. Cells

Molecules and Cells

eISSN 0219-1032
qr-code Download