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Journal of Neuroscience, Vol 14, 7695-7703, Copyright © 1994 by Society for Neuroscience
Essential role of myosin light chain kinase in the mechanism for MgATP- dependent priming of exocytosis in adrenal chromaffin cells
K Kumakura, K Sasaki, T Sakurai, M Ohara-Imaizumi, H Misonou, S Nakamura, Y Matsuda and Y Nonomura
Life Science Institute, Sophia University, Tokyo, Japan.
Ca(2+)-induced exocytosis in chromaffin cells now seems to consist of at
least two distinct steps:MgATP-dependent Ca(2+)-dependent priming of the
secretory apparatus, and Ca(2+)-dependent MgATP-independent step that
triggers exocytosis (Bittner and Holz, 1992). Recently we found that a
specific inhibitor of myosin light chain kinase (MLCK), wortmannin,
inhibits Ca(2+)-induced catecholamine release from digitonin-permeabilized
chromaffin cells, suggesting an implication of MLCK in the mechanisms of
Ca(2+)-induced exocytosis (Imaizumi et al., 1992b). To elucidate further
the implication of MLCK in the mechanism of exocytosis, we studied the
effects of wortmannin and a peptide inhibitor (SM-1) corresponding to the
pseudosubstrate domain of MLCK on MgATP-dependent and MgATP-independent
release in digitonin- permeabilized chromaffin cells. Ca(2+)-induced
exocytosis from the permeabilized cells in the presence of MgATP was
inhibited by both SM-1 and wortmannin. Inhibitory effect of wortmannin on
the rate of release induced by 10 microM Ca2+ in the presence of MgATP was
much prominent in the later phase (1-10 min), although the initial rate was
also decreased. SM-1 strongly inhibited ATP-dependent release without
affecting Ca(2+)-dependent ATP-independent release at all. In addition,
priming effect of MgATP that underlies Ca(2+)-dependent ATP-independent
release was remarkably reduced by both wortmannin and SM-1. These results
suggest that MLCK plays an essential role in ATP-dependent priming of
Ca(2+)-induced exocytosis in chromaffin cells.
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