BMB Reports
- 제34권6호
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- Pages.517-525
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- 2001
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- 1976-670X(eISSN)
Characterization of Protein Kinases Activated during Treatment of Cells with Okadaic Acid
- Bogoyevitch, Marie A. (Department of Biochemistry, University of Western Australia) ;
- Thien, Marilyn (Department of Biochemistry, University of Western Australia) ;
- Ng, Dominic C.H. (Department of Biochemistry, University of Western Australia)
- 투고 : 2001.07.17
- 심사 : 2001.08.21
- 발행 : 2001.11.30
초록
Six renaturable protein kinases that utilize the myelin basic protein (MBP) as a substrate were activated during prolonged exposure of cardiac myocytes to okadaic acid (OA). We characterized the substrate preference and activation of these kinases, with particular emphasis on 3 novel kinases-MBPK-55, MBPK-62 and MBPK-87. The transcription factors c-Jun, Elk, ATF2, and c-Fos that are used to assess mitogen-activated protein kinase activation were all poor substrates for these three kinases. MAPKAPK2 was also not phosphorylated. In contrast, Histone IIIS was phosphorylated by MBPK-55 and MBPK-62. These protein kinases were activated in cultured cardiac fibroblasts, H9c2 cardiac myoblasts, and Cos cells. High concentrations (0.5 to