Publication: Differential regulation of parallel mitogen-activated protein kinases in cardiac myocytes revealed by phosphatase inhibition
Issued Date
1998-10-09
Resource Type
ISSN
0006291X
Other identifier(s)
2-s2.0-0032500755
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Mahidol University
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SCOPUS
Bibliographic Citation
Biochemical and Biophysical Research Communications. Vol.251, No.1 (1998), 328-333
Suggested Citation
Monica B. Andersson, Albert J. Ketterman, Marie A. Bogoyevitch Differential regulation of parallel mitogen-activated protein kinases in cardiac myocytes revealed by phosphatase inhibition. Biochemical and Biophysical Research Communications. Vol.251, No.1 (1998), 328-333. doi:10.1006/bbrc.1998.9476 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/18288
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Title
Differential regulation of parallel mitogen-activated protein kinases in cardiac myocytes revealed by phosphatase inhibition
Abstract
Previous studies have suggested that the contribution of inducible phosphatases to ERK MAPK deactivation is both cell-type- and agonist-specific. The aim of this study was to define the role of inducible phosphatases in ERK MAPK regulation in cardiac myocytes. We examined the kinetics of activation/deactivation of ERK MAPKs following the exposure of cardiac myocytes to endothelin-1 or phorbol ester. Deactivation was prevented by inhibition of protein synthesis indicating a contribution of inducible phosphatases. In contrast, okadaic acid failed to prolong ERK MAPK activation, but activated three myelin basic protein kinases (MBPKs, 55, 62, and 87 kDa) and two c-Jun kinases (46 and 55 kDa). Although the identity of the MBPKs is unknown, the c-Jun kinases corresponded to JNK MAPKs. Simultaneous exposure of cardiac myocytes to okadaic acid and osmotic shock potentiated JNK MAPK activation. Thus, inducible phosphatases regulate ERK MAPK deactivation, whereas okadaic acid-sensitive phosphatases regulate JNK MAPKs and three novel MBPKs.