We have investigated whether arachidonic acid could regulate tissue transglutaminase (tTGase) via intracellular reactive oxygen species (ROS) in NIH3T3 cells. tTGase was identified in NIH3T3 cells by Western blot and confocal microscopy. Arachidonic acid elevated in situ tTGase activity in dose- and time-dependent manners with a maximal level at 1 h, and ROS scavengers, N-(2-mercaptopropionyl)glycine and catalase, blocked the tTGase activation by arachidonic acid. The activation of tTGase by arachidonic acid was largely inhibited by transfection of tTGase siRNA. The role of intracellular ROS in the activation of in situ tTGase was supported by the activation of in situ tTGase by exogenous H 2O 2. Arachidonic acid stimulated the formation of stress fibers in a dose- and time-dependent manner, and the ROS scavengers suppressed the arachidonic acid-induced formation of stress fibers. These results suggested that the activation of in situ tTGase and stress fiber formation by arachidonic acid was mediated by intracellular ROS in NIH3T3 cells.
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - 2004 Dec 17|
Bibliographical noteFunding Information:
This work was supported in part by grants from the Vascular System Research Center of KOSEF and the Korea Science and Engineering Foundation (1999-2-20700-004-5).
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology