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Pervanadate elicits proliferation and mediates activation of mitogen‐activated protein (MAP) kinase in the nucleus 1
Author(s) -
Krady Marie-Marthe,
Freyermuth Solange,
Rogue Patrick,
Malviya Anant N
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00821-1
Subject(s) - protein tyrosine phosphatase , mitogen activated protein kinase , mitogen activated protein kinase kinase , microbiology and biotechnology , protein kinase a , tyrosine phosphorylation , ask1 , chemistry , tyrosine , platelet derived growth factor receptor , c raf , map kinase kinase kinase , map2k7 , phosphorylation , tyrosine kinase , cyclin dependent kinase 2 , biology , biochemistry , signal transduction , growth factor , receptor
There is growing evidence for the role of protein tyrosine phosphatases in controlling such fundamental cellular processes as growth and differentiation. Pervanadate is a potent inhibitor of protein tyrosine phosphatase which has been observed here to induce proliferation in C3H10T1/2 mouse fibroblasts. Pervanadate also translocated/activated p42/44 mitogen‐activated protein (MAP) kinase to the cell nucleus. An almost similar pattern of nuclear p42/44 MAP kinase stimulation is seen with TPA. On the other hand, TPA treatment results in a rapid activation of cytosolic MAP kinase which declines with time. Thus pervanadate appears as a very useful tool for studying tyrosine phosphorylation.