Vasopressin depolymerizes F-actin in toad bladder epithelial cells
| Autor: | Nicholas Franki, John S. Condeelis, Guohua Ding, Richard M. Hays |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Vasopressin
medicine.medical_specialty Amanitins Vesicle fusion Macromolecular Substances Physiology Water flow Urinary Bladder 8-Bromo Cyclic Adenosine Monophosphate Stimulation macromolecular substances Toad In Vitro Techniques Biology Epithelium chemistry.chemical_compound biology.animal Internal medicine medicine Animals Deamino Arginine Vasopressin Cytoskeleton Rana catesbeiana Forskolin Vesicle Cell Biology Actins Arginine Vasopressin Microscopy Electron Endocrinology chemistry Bufo marinus Female hormones hormone substitutes and hormone antagonists |
| Zdroj: | American Journal of Physiology-Cell Physiology. 260:C9-C16 |
| ISSN: | 1522-1563 0363-6143 |
| DOI: | 10.1152/ajpcell.1991.260.1.c9 |
| Popis: | Vasopressin (AVP) induces the rapid fusion of water channel-containing vesicles with the luminal membrane of its target cell. We have carried out a quantitative study of the F-actin content of toad bladder epithelial cells, using the rhodamine phalloidin binding assay. As early as 1 min after AVP stimulation, there is a significant 15% reduction of cellular F-actin, which remains reduced by 20-30% for the duration of action of AVP. Comparable reductions were seen following 8-bromoadenosine 3',5'-cyclic monophosphate, 1-desamino-8-D-arginine vasopressin, and forskolin. F-actin content rose to and then exceeded that of control bladders after AVP washout. Inhibition of prostaglandin synthesis enhanced both water flow and the decrease of F-actin. In the living cell, stabilization of F-actin with NBD-phallacidin selectively inhibited water flow. In view of the rapidity of the response, we conclude that AVP shifts the equilibrium between F-actin and G-actin monomers, and this depolymerization may be required for vesicle fusion. |
| Databáze: | OpenAIRE |
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