Regulation and drug insensitivity of f‐actin association with adhesion areas of transformed cells

Abstract

F-actin aggregates have been found near the substrate attachments in a variety of transformed cells (Carley et al., 1981). Interference reflection microscopy shows that these aggregates are present in central close adhesion areas in Rous sarcoma virus (RSV)-transformed rat kidney cells. If these transformed cells are incubated with N6, O2-dibutyryl 3':5'-cyclic monophosphoric acid (db-cAMP), adenosine 5'-monophosphoric acid (5'-AMP) or adenosine, the F-actin aggregates and their associated close adhesion areas disappear, and the cells flatten out. Treatment of untransformed cells with db-cAMP spreads their focal adhesion plaques and thickens microfilament bundles. Furthermore, F-actin aggregates are substantially more resistant to cytochalasin B and the Ca2+ ionophore A23187 than microfilament bundles in untransformed cells. These differences between F-actin complexes in untransformed and in RSV-transformed cells, with respect to morphology and sensitivities to db-cAMP and cytoskeleton-disrupting drugs, define properties of the change in F-actin regulation and association with the plasma membrane due to transformation.