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
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References
J-M. Trifaró, M. L. Vitale, Cytoskeleton dynamics during neurotransmitter release, Trends Neurosci. 16, 466–472 (1993).
K. Kumakura, K. Sasai, T. Sakurai, M. Ohara-Imaaizumi, H. Misonou. S. Nakamura, and Y. Nonomura, Essential role of myosin light chain kinase in the mechanism for MgATP-dependent priming of exocytosis in adrenal chromaffin cells, J. Neurosci. 14,7695–7703 (1994).
S. Saito, S. Watanabe, H. Ozaki, N. Fusetani, and H. Karaki, Mycalolide B., a novel actin depolymerizing agenT., J. Biol. Chem. 269, 29710–29714 (1994).
S. Nakanishi, S. Kakita, I. Takahashi, K. Kawahara, E. Tsukada, T. Sano, K. Yamada, M. Yoshida, H. Kase, Y. Matsuda, Y. Hashimoto, and Y. Nonomura, Wortmanni, a microbial product inhibitor of myosin light chain kinase, J. Biol. Chem. 267, 2157–2163 (1992).
K. Kumakura, M. Ohara, and G. P. Satô, Real-time monitoring of the secretory function of cultured adrenal chromaffin cells, J. Neurochem. 46, 1851–1858 (1986).
H. Misonou, M. Ohara-Imaizumi, T. Murakami, M. Kawasaki, K. Dceda, T. Wakai, and K. Kumakura, Protein kinase C controls the priming step of regulated exocytosis in adrenal chromaffin cells., Cell Mil. Neurobiol. 18, 379–390 (1998).
D. Ron, C.-H. Chen, J. Caldwell, L. Jamieson, E. Orr, and D. Mochly-Rozen, Cloning of an intracellular receptor for protein kinase C: A homolog of the b subunit of G proteins, Proc. Natl. Acad. Sci. USA, 91, 839–843 (1994).
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Kumakura, K., Ohara-Imaizumi, M., Battaini, F., Sasakawa, N., Ohkubo, S. (2002). Multiple Roles of Actin Cytoskeleton in Catecholamine Release from Chromaffin Cell. In: Nagatsu, T., Nabeshima, T., McCarty, R., Goldstein, D.S. (eds) Catecholamine Research. Advances in Behavioral Biology, vol 53. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-3538-3_10
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DOI: https://doi.org/10.1007/978-1-4757-3538-3_10
Publisher Name: Springer, Boston, MA
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