Vasopressin depolymerizes F-actin in toad bladder epithelial cells

G. Ding, N. Franki, J. Condeelis, R. M. Hays

Research output: Contribution to journalArticle

74 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)C9-C16
JournalAmerican Journal of Physiology - Cell Physiology
Volume260
Issue number1 29-1
DOIs
StatePublished - Jan 1 1991

Keywords

  • Actin depolymerization
  • Cytoskeleton
  • Rhodamine phalloidin

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

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