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 |
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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. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/S0014-5793(97)00821-1 |