title: 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.
mesh_terms: D000199:Actins / Q000502:physiology*; D000241:Adenosine / Q000494:pharmacology; D000818:Animals; D001358:Avian Sarcoma Viruses / Q000235:genetics*; D003994:Bucladesine / Q000494:pharmacology; D000001:Calcimycin / Q000494:pharmacology; D002448:Cell Adhesion / Q000187:drug effects; D002449:Cell Aggregation / Q000187:drug effects; D002460:Cell Line; D002471:Cell Transformation, Neoplastic; D007365:Intercellular Junctions / Q000187:drug effects; D007668:Kidney; D007700:Kinetics; D051381:Rats
chemical_list: D000199:Actins; D000001:Calcimycin; D003994:Bucladesine; D000241:Adenosine