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Title 

IL-6-Induced calmodulin-dependent protein phosphorylation in B9 hybridoma cells

Authors 

In Pyo ChoiWoo-Jin NaHyung Sik KangKwang Ho Pyun

Publisher 

American Association of Immunologists

Issue Date 

1994

Citation 

Journal of Immunology, vol. 152, no. 4, pp. 1532-1537

Keywords 

calmodulininterleukin 6n (6 aminohexyl) 5 chloro 1 naphthalenesulfonamideprotein kinaseprotein kinase inhibitorprotein p25animal cellcell proliferationhybrid cellhybridoma

Abstract 

The addition of IL-6 to the IL-6-dependent B9-55 hybridoma cells starved for IL-6 for 16 h induced an increased phosphorylation of a 25-kda protein (p25). Phosphorylation of p25 was IL-6 dependent and maximal at 5 min after IL-6 stimulation. Phosphorylation of p25 was inhibited by N-(6-aminohexyl)- 5-chloro-1-naphthalene sulfonamide (W-7), an inhibitor of calmodulin- dependent protein kinase, but not by tyrphostin nor ionomycin. When enolase was used as an exogenous substrate, similar results were obtained. Furthermore, calmodulin stimulated p25 phosphorylation in vitro. IL-6- starved B9 hybridoma cells synthesized DNA at 9 to 12 h after addition of IL- 6. Preincubation of cells with W-7 before IL-6 stimulation blocked DNA synthesis. Similar effects were observed when cells were preincubated with tyrphostin or ionomycin but to a lesser extent. The concentrations of W-7 required for blocking p25 phosphorylation and DNA synthesis correlated relatively well. These results suggest that an IL-6-inducible calmodulin- dependent protein kinase is involved in IL-6 signal transduction, including p25 phosphorylation and B9 hybridoma proliferation.

ISSN 

0022-1767

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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