Inhibition of vanadate-induced astrocytic stress fiber formation by C3 ADP-ribosyltransferase.

Mechanisms of vanadate-induced actin reorganization were examined in cultured astrocytes. Treatment of protoplasmic astrocytes with 0.5 mM dibutyryl cAMP (DBcAMP) caused the disappearance of stress fibers (SFs) and focal adhesions (FAs) accompanied with cellular stellation. A subsequent addition of 1 mM orthovanadate (VO4(3-) reorganized SFs and FAs in DBcAMP-treated cells. The newly formed FAs had increased phosphotyrosine levels. VO4(3-) reorganized SFs and FAs in stellate astrocytes induced by 5 microM cytochalasin B, 50 microM ML-9 and 20 microM W-7. Cytoplasmic microinjection of 20 micrograms/ml C3 ADP-ribosyltransferase of C. botulinum, which inactivates rho proteins, caused disappearance of SFs. The effect of C3 enzyme on SFs was not reversed by a subsequent addition of VO4(3-). These results suggest that rho proteins are involved in vanadate-induced reorganization of cytoskeletal actin.