Activation of MAPK by potassium bisperoxo(1,10- phenanthroline)oxovanadate (V)

Neurochemistry International

Volumn 34, Issue 4, 1999, Pages 337-344

  Cerovac, Zeljka ^a   Ban, Jasna ^a   Morinville, Anne ^b   Yaccato, Karin ^b   Shaver, Alan ^b   Maysinger, Dusica ^b  

^a UNIVERSITY OF ZAGREB   (Croatia)

^b MCGILL UNIVERSITY   (Canada)

Author keywords

51V NMR; ERK; JNK; PC12 cells; Peroxovanadium complexes

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; STRESS ACTIVATED PROTEIN KINASE;

ANIMAL CELL; ARTICLE; CELL DEATH; CELL PROLIFERATION; CELL SURVIVAL; DECOMPOSITION; ENZYME ACTIVATION; ENZYME PHOSPHORYLATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL;

ANIMALS; CA(2+)-CALMODULIN DEPENDENT PROTEIN KINASE; CELL DIVISION; CELL SURVIVAL; DOSE-RESPONSE RELATIONSHIP, DRUG; DRUG STABILITY; ENZYME ACTIVATION; JNK MITOGEN-ACTIVATED PROTEIN KINASES; MITOGEN-ACTIVATED PROTEIN KINASES; ORGANOMETALLIC COMPOUNDS; P38 MITOGEN-ACTIVATED PROTEIN KINASES; PC12 CELLS; PHENANTHROLINES; PHOSPHORYLATION; RATS;

ANIMALIA;

EID: 0032986090     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0197-0186(99)00018-2     Document Type: Article

References (27)

1. Abe J., Kusuhara M., Ulevitch R.J., Berk B.C., Lee J.D. Big mitogen-activated protein kinase 1 (BMK1) is a redox-sensitive kinase. J. Biol. Chem. 271:1996;16,586-16,590.
2. Alessi D.R., Cuenda A., Cohen P., Dudley D.T., Saltiel A.R. PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo. J. Biol. Chem. 270:1995;27,489-27,494.
3. Band C.J., Posner B.I. Phosphatidylinositol 3′-kinase and p70s6k are required for insulin but not bisperoxovanadium 1,10-phenanthroline (bpV(phen))inhibition of insulin-like growth factor binding protein gene expression. Evidence for MEK-independent activation of mitogen-activated protein kinase by bpV(phen). J. Biol. Chem. 272:1997;138-145.
4. Chang S.T., Yung B.Y.M. Potentiation of sodium butyrate-induced apoptosis by vanadate in human promyelocytic leukemia cell line HL-60. Biochem. Biophys. Res. Comm. 221:1996;594-601.
5. Chen Y.R., Wang X., Templeton D., Davis R.J., Tan T.H. The role of c-Jun N-terminal kinase (JNK) in apoptosis induced by ultraviolet C and gamma radiation. Duration of JNK activation may determine cell death and proliferation. J. Biol. Chem. 271:1996;31,929-31,936.
6. Dudley D.T., Pang L., Decker S.J., Bridges A.J., Saltiel A.R. A synthetic inhibitor of the mitogen-activated protein kinase cascade. Proc. Natl. Acad. Sci. USA. 92:1995;7686-7689.
7. Faure R., Vincent M., Dufour M., Shaver A., Posner B.I. Arrest at the G2/M transition of the cell cycle by protein-tyrosine phosphatase inhibition: studies on a neuronal and a glial cell line. J. Cell. Biochem. 58:1995;389-401.
8. Fukunaga K., Miyamoto E. Role of MAP Kinase in neurons. Mol. Neurobiol. 16:1998;79-95.
9. Greene L., Tischler A. Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor. Proc. Natl. Acad. Sci. USA. 73:1976;2424-2426.
10. Huyer G., Liu S., Kelly J., Moffat J., Payette P., Kennedy B., Tsaprailis G., Gresser M.J., Ramachandran C. Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. J. Biol. Chem. 272:1997;843-851.
11. Imbert V., Peyron J.F., Fahari Far D., Mari B., Auberger P., Rossi B. Induction of tyrosine phosphorylation and T-cell activation by vanadate peroxide, an inhibitor of protein tyrosine phosphatases. Biochem. J. 297:1994;163-173.
12. Ip Y.T., Davis R.J. Signal transduction by the c-jun N-terminal kinase (JNK) - from inflammation to development. Curr. Opin. Cell Biol. 10:1998;205-219.
13. Krady M.M., Freyermuth S., Rogue P., Malviya A.N. Pervanadate elicits proliferation and mediates activation of mitogen-activated protein (MAP) kinase in the nucleus. FEBS Lett. 412:1997;420-424.
14. Krejsa C.M., Nadler S.G., Esselstyn J.M., Kavanagh T.J., Ledbetter J.A., Schieven G.L. Role of oxidative stress in the action of vanadium phosphotyrosine phosphatase inhibitors. Redox independent activation of NF-kappaB. J. Biol. Chem. 272:1997;11,541-11,549.
15. Kwong D.W.J., Chan O.Y., Wong R.N.S., Musser S.M., Vaca L., Chan S.I. DNA-photocleavage activities of Vanadium(V)-Peroxo Complexes. Inorg. Chem. 36:1997;1276-1277.
16. Morinville A., Maysinger D., Shaver A. From Vanadis to Atropos: Vanadium compounds as pharmacological tools in cell death signalling. Trends Pharmacol. Sci. 19:1998;452-460.
17. Oetken C., von Willebrand M., Marie-Cardine A., Pessa-Morikawa T., Stahls A., Fisher S., Mustelin T. Induction of hyperphosphorylation and activation of the p56lck protein tyrosine kinase by phenylarsine oxide, a phosphotyrosine phosphatase inhibitor. Mol. Immunol. 31:1994;1295-1302.
18. Pandey S.K., Chiasson J.L., Srivastava A.K. Vanadium salts stimulate mitogen-activated protein (MAP) kinases and ribosomal S6 kinases. Mol. Cell. Biochem. 153:1995;69-78.
19. Pang L., Sawada T., Decker S.J., Saltiel A.R. Inhibition of MAP kinase kinase blocks the differentiation of PC-12 cells induced by nerve growth factor. J. Biol. Chem. 270:1995;13,585-13,588.
20. Posner B.I., Faure R., Burgess J.W., Bevan A.P., Lachance D., Zhang-Sun G., Fantus I.G., Ng J.B., Hall D.A., Soo Lum B., Shaver A. Peroxovanadium compounds: a new class of potent phosphotyrosine phosphatase inhibitors which are insulin mimetics. J. Biol. Chem. 269:1994;4596-4604.
21. Raingeaud J., Gupta S., Rogers J.S., Dickens M., Han J., Ulevitch R.J., Davis R.J. Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J. Biol. Chem. 270:1995;7420-7426.
22. Raingeaud J., Whitmarsh A.J., Barret T., Derijard B., Davis R.J. MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway. Mol. Cell. Biol. 16:1996;1247-1255.
23. Sekar N., Li J., Shechter Y. Vanadium salts as insulin substitutes: mechanisms of action, a scientific and therapeutic tool in diabetes mellitus research. Critical Rev. Biochem. Mol. Biol. 31:1996;339-359.
24. Smith A., Ramos-Morales F., Ashworth A., Collins M. A role for JNK/SAPK in proliferation, but not apoptosis, of IL-3-dependent cells. Curr. Biol. 7:1997;893-896.
25. Virdee K., Bannister A.J., Hunt S.P., Tolkovsky A.M. Comparison between the timing of JNK activation, c-Jun phosphorylation, and onset of death commitment in sympathetic neurones. J. Neurochem. 69:1997;550-561.
26. Xia Z., Dickens M., Raingeaud J., Davis R.J., Greenberg M.E. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science. 270:1995;1326-1331.
27. Zhao Z., Tan Z., Diltz C.D., You M., Fischer E.H. Activation of mitogen-activated protein (MAP) kinase pathway by pervanadate, a potent inhibitor of tyrosine phosphatases. J. Biol. Chem. 271:1997;22,251-22,255.