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Actin depolymerization in the cyclic AMP‐stimulated toad bladder epithelial cell, determined by the DNAse method
Author(s) -
Hays Richard M.,
Lindberg Uno
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80340-9
Subject(s) - toad , actin , phalloidin , chemistry , deoxyribonuclease i , microbiology and biotechnology , cytochalasin d , microfilament , depolymerization , actin binding protein , cytoskeleton , biochemistry , actin cytoskeleton , biophysics , biology , cell , endocrinology , gene , base sequence , organic chemistry
Previous studies with the rhodamine phalloidin binding assay have shown that antidiuretic hormone and 8‐Br‐cAMP rapidly depolymerize F‐actin in toad bladder epithelial cells. We have extended these studies with DNAse inhibition assay and have found that in isolated epithelial cell suspensions, G‐actin increases from 37 to 56% of total actin following 8‐br‐cAMP stimulation. The G‐actin concentration in the epithelial cell greatly exceeds its critical concentration, indicating the requirement for a G‐actin sequestering protein or proteins in this system.