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Ouabain inhibits p38 activation in thymocytes
Author(s) -
RodriguesMascarenhas Sandra,
Bloise Flavia Fonseca,
Moscat Jorge,
Rumjanek Vivian M.
Publication year - 2008
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1016/j.cellbi.2008.07.012
Subject(s) - ouabain , nfat , phosphorylation , p38 mitogen activated protein kinases , microbiology and biotechnology , chemistry , signal transduction , mapk/erk pathway , biology , transcription factor , biochemistry , sodium , organic chemistry , gene
The MAPK p38 is phosphorylated by multiple stimuli and regulates a number of transcription factors. It is reported that activation of p38 leading to the regulation of NFAT may result from an alternative MKK‐independent mechanism. This alternative pathway involves the protein Dlgh1 as an essential scaffold that assembles a module for the activation of p38. Ouabain, a specific inhibitor of the Na + /K + ‐ATPase, is capable of inducing the activation of various signal transduction cascades. In the present work, P‐p38 levels of ConA‐activated thymocytes treated with ouabain (1, 10 and 100 nM) were measured as also the effect of ouabain on NFATc1 expression. p38 phosphorylation and NFATc1 levels were analyzed by flow cytometry. The results indicated that ouabain inhibited both ConA‐dependent increase in P‐p38 and NFATc1 levels, which suggests an effect of ouabain on the p38 alternative pathway.