Insulin regulates MAP kinase phosphatase-1 induction in Hirc B cells via activation of both extracellular signal-regulated kinase (ERK) and c-Jun-N-terminal kinase (JNK) |
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Authors: | Byon John C.H. Dadke Shrikrishna S. Rulli Samuel Kusari Anasua B. Kusari Jyotirmoy |
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Affiliation: | (1) Department of Physiology, Tulane University School of Medicine, New Orelans, LA 70112, USA;(2) Molecular and Cellular Biology Program, Tulane University School of Medicine, New Orelans, LA 70112, USA;(3) Allergan Inc., 2525 Dupont Drive, P.O. Box 19534, Irvine, CA 92623, USA |
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Abstract: | Previously, we have reported that insulin induces the expression of the dual-specificity tyrosine phosphatase Mitogen-activated protein (MAP) kinase phosphatase-1 (MKP-1) and that this may represent a negative feedback mechanism to regulate insulin-stimulated MAP kinase activity. In this work, the mechanism of regulation of MKP-1 expression by insulin was examined, particularly the role of the MAP kinase superfamily. Inhibition of the ERK pathway attenuated insulin-stimulated MKP-1 mRNA expression. Expression of dominant negative molecules of the JNK pathway also abolished insulin-stimulated MKP-1 expression. However, inhibition of p38MAPK activity by SB202190 had no effect on insulin-stimulated MKP-1 induction. Simultaneous inhibition of the ERK and JNK pathways abolished the ability of insulin to stimulate MKP-1 expression, however, this combined inhibition was neither additive nor synergistic, suggesting these pathways converge to act on a common final effector. In conclusion, induction of MKP-1 mRNA expression in Hirc B cells by insulin requires activation of both the ERK and JNK pathways, but not p38MAPK. |
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Keywords: | insulin MKP-1 ERK JNK p38 kinase Hirc B cells |
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