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Regulation and drug insensitivity of f‐actin association with adhesion areas of transformed cells
Author(s) -
Carley William W.,
Lipsky Mary G.,
Webb Watt W.
Publication year - 1983
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041170218
Subject(s) - microfilament , cytochalasin b , cytochalasin d , rous sarcoma virus , actin , adhesion , microbiology and biotechnology , adenosine , biology , cytochalasin , cytoskeleton , biophysics , chemistry , cell , biochemistry , organic chemistry , gene
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 N 6 , O 2 ‐dibutyryl 3′:5′‐cyclic monophosphoric acid (db‐cAMP), adenosine (5′‐monophosphoric acid (5′‐cAMP) 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 local adhesion plaques and thickens microfilament bundles. Furthermore, f‐action aggregates are substantially more resistant to cytochalasin B and the Ca 2+ ionophore A23187 than microfilament bundles in untrasformed cells. These differences between F‐acttin 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.