Multiple Roles of Actin Cytoskeleton in Catecholamine Release from Chromaffin Cell

  • Konosuke Kumakura
  • Mica Ohara-Imaizumi
  • Fiorenzo Battaini
  • Nobuyuki Sasakawa
  • Shingo Ohkubo
Part of the Advances in Behavioral Biology book series (ABBI, volume 53)

Abstract

In adrenal chromaffin cells, it is generally accepted that sub-plasmalemmal actin network acts as a barrier to secretory vesicles.1 On the other hand, we have demonstrated previously that myosin light chain kinase which regulates actin-myosin interaction are required for ATP-dependent priming or for step before the priming of exocytosis in adrenal chromaffin cells,2 and suggested that actin-myosin interaction is required for the vesicle recruitment in these cells. In order to clarify the implication of actin-myosin interaction and of actin cytoskeleton in the mechanism of CA release, we studied the effects of Mycalolide B (MLB), Cytochalasin D (CD), and Wortmannin (WT) on the vesicle movement and kinetics of exocytotic events. Mycalolide B depolymerizes F-actin to G-actin and therefore inhibits actin-myosin interaction.3 Cytochalasin D severs F-actin into short filaments, but does not inhibit actin-myosin interaction.3 Wortmannin inhibit the phosphorylation of myosin light chain thus inhibit actin-myosin interaction, but does not depolymeraize F-actin.4

Keywords

Actin Cytoskeleton Chromaffin Cell Myosin Light Chain Kinase Adrenal Chromaffin Cell Vesicle Movement 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 2002

Authors and Affiliations

  • Konosuke Kumakura
    • 1
  • Mica Ohara-Imaizumi
    • 1
  • Fiorenzo Battaini
    • 2
  • Nobuyuki Sasakawa
    • 1
  • Shingo Ohkubo
    • 1
  1. 1.Life Science InstituteSophia UniversityTokyoJapan
  2. 2.Uiversity of Rome Tor VergataRomeItaly

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