Picture of DNA strand

Pioneering chemical biology & medicinal chemistry through Open Access research...

Strathprints makes available scholarly Open Access content by researchers in the Department of Pure & Applied Chemistry, based within the Faculty of Science.

Research here spans a wide range of topics from analytical chemistry to materials science, and from biological chemistry to theoretical chemistry. The specific work in chemical biology and medicinal chemistry, as an example, encompasses pioneering techniques in synthesis, bioinformatics, nucleic acid chemistry, amino acid chemistry, heterocyclic chemistry, biophysical chemistry and NMR spectroscopy.

Explore the Open Access research of the Department of Pure & Applied Chemistry. Or explore all of Strathclyde's Open Access research...

Inactivation of jNK ACtivity by mitogen-activated protein kinase phosphatase-2 in Eahy926 endothelial cells is dependent upon agonist-specific jNK translocation to the nucleus

Robinson, C. and Sloss, C.M. and Plevin, R.J. (2001) Inactivation of jNK ACtivity by mitogen-activated protein kinase phosphatase-2 in Eahy926 endothelial cells is dependent upon agonist-specific jNK translocation to the nucleus. Cellular Signalling, 13 (1). pp. 29-41. ISSN 1873-3913

Full text not available in this repository. Request a copy from the Strathclyde author

Abstract

We have investigated the termination of agonist-stimulated mitogen-activated protein (MAP) kinase activity in EAhy926 cells by MAP kinase phosphatase-2 (MKP-2). In cells expressing either wild-type (WT) or catalytically inactive (CI)-MKP-2, there was no significant differences in TNFα-stimulated JNK or p38 MAP kinase activity, however hydrogen peroxide (H2O2)-stimulated JNK activity was substantially reduced in WT-MKP-2 expressing clones and enhanced in cells expressing CI-MKP-2. Consistent with these findings, we observed substantial nuclear translocation of JNK occurred in response to H2O2 but not TNFα. Using a phosphospecific anti-JNK antibody, we found that TNFα-stimulated JNK activity was associated principally with the cytosol while in response to H2O2, JNK activity was found within the nucleus. These results show that the role of MKP-2 in terminating JNK activity is determined by the translocation of JNK to the nucleus, which is under agonist-specific regulation and not a universal cellular response to stimulation.