Premium
Role of PP2A in the regulation of p38 MAPK activation in bovine aortic endothelial cells exposed to cyclic strain
Author(s) -
Lee Taeseung,
Kim Sang Joon,
Sumpio Bauer E.
Publication year - 2003
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.10211
Subject(s) - okadaic acid , protein phosphatase 2 , phosphorylation , mapk/erk pathway , phosphatase , p38 mitogen activated protein kinases , protein kinase a , mitogen activated protein kinase , protein subunit , chemistry , microbiology and biotechnology , strain (injury) , biochemistry , biology , anatomy , gene
We have previously reported that cyclic strain results in rapid phosphorylation of p38 mitogen activated protein kinase (MAPKs). The aim of this study was to examine the role of protein phosphatase type 2A (PP2A) in regulating p38 MAPK activation in bovine aortic endothelial cells exposed to cyclic strain. In this study, we demonstrate that the catalytic subunit of PP2A is tyrosine phosphorylated by cyclic strain, resulting in inhibition of phosphatase activity. Okadaic acid, an inhibitor of PP2A at lower concentrations increased phosphorylation of p‐38. Phospho‐p38 MAPK physically associated with the catalytic subunit, PP2Ac. Phospho‐p38 MAPK was dephosphorylated by purified PP2Ac in cell lysates, but if pretreated with okadaic acid, phospho‐p38 MAPK was maintained. Taken together, our result suggests that PP2A plays a regulatory role in p38 MAPK activation in endothelial cells exposed to cyclic strain. J. Cell. Physiol. 194: 349–355, 2003. © 2003 Wiley‐Liss, Inc.