Toxicological Research

  • 제21권4호
  • /
  • Pages.291-295
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  • 2005
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  • 1976-8257(pISSN)
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  • 2234-2753(eISSN)
한국독성학회 (Korean Society of Toxicology & Korea Environmental Mutagen Society)
권호 표지

Silica Induced Phospholipase D (PLD) Activation in Rat2 Fibroblasts

  • Ahn Eun-Kyung (Department of Occupational and Environmental Medicine, St. Mary's Hospital, College of Medicine, The Catholic University) ;
  • Lim Oh-Kyung (Department of Occupational and Environmental Medicine, St. Mary's Hospital, College of Medicine, The Catholic University) ;
  • Nam Hae-Yun (Department of Occupational and Environmental Medicine, St. Mary's Hospital, College of Medicine, The Catholic University) ;
  • Kim Hyung Jung (Department of Internal Medicine, College of Medicine, Yonsei University) ;
  • Chung Namhyun (College of Life and Environmental Sciences Korea University) ;
  • Bae Gwi-Nam (Air Resources Research Center Korea Institute of Science and Technology) ;
  • Lim Young (Department of Occupational and Environmental Medicine, St. Mary's Hospital, College of Medicine, The Catholic University)
  • 발행 : 2005.12.01
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초록

To define the effect of silica on the stimulator of signaling pathway, we studied the phospholipase D (PLD) activity in the Rat2 fibroblasts. Silica stimulated the accumulation of labeled $[^3H]$ phosphatidylethanol$([^3H]\;PEt)$ in a time- and concentration-dependent manner. This Silicainduced PLD activity was partially attenuated by the pretreatment with U73122 (phospholipase C inhibitor), genistein (protein tyrosine kinase inhibitor), PD 98056 (MEK inhibitor) and mepacrine (phospholipase $A_2$ inhibitor). But, sphingosine (protein kinase C inhibitor) and DPI (NADPH reductase inhibitor) had not effect the PLD activity. Silica also increased the PLD activity about four fold, which imply that the PLD activity is more influenced by the mobilization of PLD than other signaling mediators. The PLD activity also partially inhibited calcium chelator EGTA or/and BAPTA/AM compared to silica. Finally, we concluded that a silica-stimulated phospholipase D activity is present in the Rat2 fibroblasts and is modulated by combination of various signaling mediators.

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