Abstract
In order to investigate the role of a small GTP-binding protein RhoA in lysophosphatidic acid (LPA)-induced stress fiber formation, C3 ADP-ribosyltransferase was prepared by expressing in E. coli and then applied to Rat-2 fibroblasts. C3 transferase isolated from E. coli was as effective as the toxin from Clostridium botulinum in ADP-ribosylation of RhoA. Incubation of the cells with C3 transferase for 2 days induced ADP-ribosylation of RhoA by a dose-dependent manner, with a sub-maximal induction at 25 μg/ml. As expected, LPA-induced stress fiber formation was completely blocked by pre-incubation with C3 transferase for 2 days. However, exogenously added C3 transferase had no significant effect on the formation of phosphatidylethanol by LPA. These results suggested that phospholipase D was not activated by RhoA in the LPA-induced stress fiber formation.
| Original language | English |
|---|---|
| Pages (from-to) | 337-341 |
| Number of pages | 5 |
| Journal | Journal of Biochemistry and Molecular Biology |
| Volume | 30 |
| Issue number | 5 |
| Publication status | Published - 1997 Sept 30 |
| Externally published | Yes |
Keywords
- C3 transferase
- Lysophosphatidic acid
- Phospholipase D
- RhoA
- Stress fibers
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology