Pervanadate elicits proliferation and mediates activation of mitogen-activated protein (MAP) kinase in the nucleus

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 fibrobla...

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Veröffentlicht in:FEBS letters 1997-08, Vol.412 (3), p.420-424
Hauptverfasser: Krady, Marie-Marthe, Freyermuth, Solange, Rogue, Patrick, Malviya, Anant N
Format: Artikel
Sprache:eng
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Zusammenfassung: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)00821-1