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  Fusion pore expansion in horse eosinophils is modulated by Ca2+ and protein kinase C via distinct mechanisms.

Scepek, S., Corsson, J. R., & Lindau, M. (1998). Fusion pore expansion in horse eosinophils is modulated by Ca2+ and protein kinase C via distinct mechanisms. EMBO Journal, 17(15), 4340-4345. doi:10.1093%2Femboj%2F17.15.4340.

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Scepek, S., Author
Corsson, J. R., Author
Lindau, M.1, Author              
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1Research Group of Nanoscale Cell Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1832294              

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 Abstract: Using the patch-clamp technique, we studied the role of protein phosphorylation and dephosphorylation on the exocytotic fusion of secretory granules with the plasma membrane in horse eosinophils. Phorbol 12-myristate 13-acetate (PMA) had no effect on the amplitude and dynamics of degranulation, indicating that the formation of fusion pores is insensitive to activation of protein kinase C (PKC). Fusion pore expansion, however, was accelerated approximately 2-fold by PMA, and this effect was abolished by staurosporine. Elevating intracellular Ca2+ to 1.5 microM also resulted in a 2-fold acceleration of pore expansion; this effect was not prevented by staurosporine, indicating that intracellular Ca2+ and activation of PKC accelerate fusion pore expansion via distinct mechanisms. However, fusion pores can expand fully even when PKC is inhibited. In contrast, the phosphatase inhibitor alpha-naphthylphosphate inhibits exocytotic fusion and slows fusion pore expansion. These results demonstrate that, subsequent to its formation, fusion pore expansion is under control of proteins subject to functional changes based on their phosphorylation states.

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Language(s): eng - English
 Dates: 1998-08-03
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1093%2Femboj%2F17.15.4340
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Title: EMBO Journal
Source Genre: Journal
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Pages: - Volume / Issue: 17 (15) Sequence Number: - Start / End Page: 4340 - 4345 Identifier: -