Actin depolymerization in the cyclic AMP-stimulated toad bladder epithelial cell, determined by the DNAse method.
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 the 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.
Hays
R M
RM
Albert Einstein College of Medicine, Bronx, New York 10461.
Lindberg
U
U
D015124:8-Bromo Cyclic Adenosine Monophosphate / Q000494:pharmacology*; D000199:Actins / Q000378:metabolism*; D000818:Animals; D002024:Bufo marinus; D002478:Cells, Cultured; D003851:Deoxyribonucleases; D004848:Epithelium / Q000187:drug effects / Q000378:metabolism; D001743:Urinary Bladder / Q000187:drug effects / Q000378:metabolism*
D000199:Actins; D015124:8-Bromo Cyclic Adenosine Monophosphate; D003851:Deoxyribonucleases