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Updated: Sep 26, 2026

In Vivo Imaging of Reactive Oxygen Species in a Murine Wound Model
Published on: November 17, 2018
Activation of in situ tissue transglutaminase by intracellular reactive oxygen species
Zee-Won Lee1, Sang-Mo Kwon, Sung-Woo Kim
1Cell Research Team, Korea Basic Science Institute, Taejon 305-333, Republic of Korea.
Abstract:
We have investigated the novel function of intracellular reactive oxygen species (ROS) in the activation of in situ tissue transglutaminase (tTGase) by lysophosphatidic acid (LPA) and transforming growth factor-beta (TGF-beta) in Swiss 3T3 fibroblasts. LPA induced a transient increase of intracellular ROS with a maximal increase at 10 min, which was blocked by ROS scavengers, N-acetyl-L-cysteine and catalase. LPA activated tTGase with a maximal increase at 1h, which was inhibited by cystamine and ROS scavengers. Incubation with exogenous H(2)O(2) activated tTGase. TGF-beta also activated tTGase with a maximal activation at 2h and the tTGase activation was inhibited by the ROS scavengers. Scrape-loading of C3 transferase inhibited the ROS production and in situ tTGase activation by LPA and TGF-beta, and the inhibitory effect of C3 transferase was reversed by exogenous H(2)O(2). Microinjection of GTPgammaS inhibited transamidating activity of tTGase stimulated by LPA, TGF-beta, and maitotoxin. These results suggested that intracellular ROS was essential for the activation of in situ tTGase in response to LPA and TGF-beta.
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