Vanadium compounds as pro-inflammatory agents: Effects on cyclooxygenases

International Journal of Molecular Sciences

Volumn 16, Issue 6, 2015, Pages 12648-12668

  Korbecki, Jan ^a   Baranowska Bosiacka, Irena ^a   Gutowska, Izabela ^a   Chlubek, Dariusz ^a  

^a POMERANIAN MEDICAL UNIVERSITY   (Poland)

Author keywords

Cell signalling; Cyclooxygenase; Tyrosine phosphatise; Vanadium

Indexed keywords

CALCIUM ION; CYCLOOXYGENASE 2; CYSTEINE; CYTOSOLIC PHOSPHOLIPASE A2; DIACYLGLYCEROL; EPIDERMAL GROWTH FACTOR RECEPTOR; HYDROGEN PEROXIDE; I KAPPA B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INOSITOL TRISPHOSPHATE; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE KINASE 4; MITOGEN ACTIVATED PROTEIN KINASE PHOSPHATASE; PHOSPHOLIPASE C GAMMA; PROSTAGLANDIN SYNTHASE; PROTEASOME; PROTEIN TYROSINE KINASE; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR SP1; VANADIC ACID; VANADIUM DERIVATIVE; VANADYL DERIVATIVE; AUTACOID;

ACUTE KIDNEY FAILURE; APOPTOSIS; CELL RESPIRATION; DRUG DIFFUSION; DRUG METABOLISM; DRUG TARGETING; DRUG TRANSFORMATION; ENZYME ACTIVATION; ENZYME ACTIVITY; GENE; GENE EXPRESSION; HUMAN; HYPOGLYCEMIA; INFLAMMATION; INTRACELLULAR SIGNALING; LIVER INJURY; OXIDATIVE STRESS; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; REVIEW; SIGNAL TRANSDUCTION; ANIMAL; DOSE RESPONSE; DRUG EFFECTS; METABOLISM;

ANIMALS; DOSE-RESPONSE RELATIONSHIP, DRUG; HUMANS; INFLAMMATION MEDIATORS; PROSTAGLANDIN-ENDOPEROXIDE SYNTHASES; SIGNAL TRANSDUCTION; VANADIUM COMPOUNDS;

EID: 84931292285     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms160612648     Document Type: Review

References (118)

1. Thompson, K.H.; Orvig, C. Vanadium in diabetes: 100 years from Phase 0 to Phase I. J. Inorg. Biochem. 2006, 100, 1925–1935.
2. Thompson, K.H.; Lichter, J.; LeBel, C.; Scaife, M.C.; McNeill, J.H.; Orvig, C. Vanadium treatment of type 2 diabetes: A view to the future. J. Inorg. Biochem. 2009, 103, 554–558.
3. Kurt, O.; Ozden, T.Y.; Ozsoy, N.; Tunali, S.; Can, A.; Akev, N.; Yanardag, R. Influence of vanadium supplementation on oxidative stress factors in the muscle of STZ-diabetic rats. Biometals 2011, 24, 943–949.
4. Missaoui, S.; Ben Rhouma, K.; Yacoubi, M.T.; Sakly, M.; Tebourbi, O. Vanadyl sulfate treatment stimulates proliferation and regeneration of beta cells in pancreatic islets. J. Diabetes Res. 2014, 2014, 540242.
5. Pirmoradi, L.; Mohammadi, M.T.; Safaei, A.; Mesbah, F.; Dehghani, G.A. Does the relief of glucose toxicity act as a mediator in proliferative actions of vanadium on pancreatic islet beta cells in streptozocin diabetic rats? Iran. Biomed. J. 2014, 18, 173–180.
6. Sun, L.; Shi, D.J.; Gao, X.C.; Mi, S.Y.; Yu, Y.; Han, Q. The protective effect of vanadium against diabetic cataracts in diabetic rat model. Biol. Trace Elem. Res. 2014, 158, 219–223.
7. Soveid, M.; Dehghani, G.A.; Omrani, G.R. Long-term efficacy and safety of vanadium in the treatment of type 1 diabetes. Arch. Iran. Med. 2013, 16, 408–411.
8. Evangelou, A.M. Vanadium in cancer treatment. Crit. Rev. Oncol. Hematol. 2002, 42, 249–265.
9. Bishayee, A.; Waghray, A.; Patel, M.A.; Chatterjee, M. Vanadium in the detection, prevention and treatment of cancer: the in vivo evidence. Cancer Lett. 2010, 294, 1–12.
10. Liu, T.T.; Liu, Y.J.; Wang, Q.; Yang, X.G.; Wang, K. Reactive-oxygen-species-mediated Cdc25C degradation results in differential antiproliferative activities of vanadate, tungstate, and molybdate in the PC-3 human prostate cancer cell line. J. Biol. Inorg. Chem. 2012, 17, 311–320.
11. Suwalsky, M.; Fierro, P.; Villena, F.; Gallardo, M.J.; Jemiola-Rzeminska, M.; Strzalka, K.; Gul-Hinc, S.; Ronowska, A.; Zysk, M.; Szutowicz, A. Effects of sodium metavanadate on in vitro neuroblastoma and red blood cells. Arch. Biochem. Biophys. 2013, 535, 248–256.
12. Wu, Y.; Ma, Y.; Xu, Z.; Wang, D.; Zhao, B.; Pan, H.; Wang, J.; Xu, D.; Zhao, X.; Pan, S.; et al. Sodium orthovanadate inhibits growth of human hepatocellular carcinoma cells in vitro and in an orthotopic model in vivo. Cancer Lett. 2014, 351, 108–116.
13. Kucera, J.; Byrne, A.R.; Mravcová, A.; Lener, J. Vanadium levels in hair and blood of normal and exposed persons. Sci. Total Environ. 1992, 115, 191–205.
14. Nadal, M.; Schuhmacher, M.; Domingo, J.L. Metal pollution of soils and vegetation in an area with petrochemical industry. Sci. Total Environ. 2004, 321, 59–69.
15. Pourang, N.; Nikouyan, A.; Dennis, J.H. Trace element concentrations in fish, surficial sediments and water from northern part of the Persian Gulf. Environ. Monit. Assess. 2005, 109, 293–316.
16. Moreno, T.; Querol, X.; Alastuey, A.; de la Rosa, J. SánchezdelaCampa, A.M.; Minguillón, M.; Pandolfi, M.; González-Castanedo, Y.; Monfort, E.; Gibbons, W. Variations in vanadium, nickel and lanthanoid element concentrations in urban air. Sci. Total Environ. 2010, 408, 4569–4579.
17. Guzmán-Morales, J.; Morton-Bermea, O.; Hernández-Álvarez, E.; Rodríguez-Salazar, M.T.; García-Arreola, M.E.; Tapia-Cruz, V. Assessment of atmospheric metal pollution in the urban area of Mexico City, using Ficus benjamina as biomonitor. Bull. Environ. Contam. Toxicol. 2011, 86, 495–500.
18. Speight, J. Chemical composition. In The Chemistry and Technology of Petroleum, 3rd ed.; CRC Press: New York, NY, USA; Basel, Switzerland, 1999; pp. 215–243.
19. Bednar, A.J.; Chappell, M.A.; Seiter, J.M.; Stanley, J.K.; Averett, D.E.; Jones, W.T.; Pettway, B.A.; Kennedy, A.J.; Hendrix, S.H.; Steevens, J.A. Geochemical investigations of metals release from submerged coal fly ash using extended elutriate tests. Chemosphere 2010, 81, 1393–1400.
20. Lin, T.S.; Chang, C.L.; Shen, F.M. Whole blood vanadium in Taiwanese college students. Bull. Environ. Contam. Toxicol. 2004, 73, 781–786.
21. Azay, J.; Brès, J.; Krosniak, M.; Teissedre, P.L.; Cabanis, J.C.; Serrano, J.J.; Cros, G. Vanadium pharmacokinetics and oral bioavailability upon single-dose administration of vanadyl sulfate to rats. Fundam. Clin. Pharmacol. 2001, 15, 313–324.
22. Klein, A.; Holko, P.; Ligeza, J.; Kordowiak, A.M. Sodium orthovanadate affects growth of some human epithelial cancer cells (A549, HTB44, DU145). Folia Biol. 2008, 56, 115–121.
23. McNicol, A.; Robertson, C.; Gerrard, J.M. Vanadate activates platelets by enhancing arachidonic acid release. Blood 1993, 81, 2329–2338.
24. Tsujishita, Y.; Asaoka, Y.; Nishizuka, Y. Regulation of phospholipase A2 in human leukemia cell lines: Its implication for intracellular signaling. Proc. Natl. Acad. Sci. USA 1994, 91, 6274–6278.
25. Lin, W.W.; Hsu, Y.W. Cycloheximide-induced cPLA(2) activation is via the MKP-1 down-regulation and ERK activation. Cell Signal. 2000, 12, 457–461.
26. Korbecki, J.; Baranowska-Bosiacka, I.; Gutowska, I.; Piotrowska, K.; Chlubek, D. Cyclooxygenase-1 as the main source of proinflammatory factors after sodium orthovanadate treatment. Biol. Trace Elem. Res. 2015, 163, 103–111.
27. Greenhough, A.; Smartt, H.J.; Moore, A.E.; Roberts, H.R.; Williams, A.C.; Paraskeva, C.; Kaidi, A. The COX-2/PGE2 pathway: Key roles in the hallmarks of cancer and adaptation to the tumour microenvironment. Carcinogenesis 2009, 30, 377–386.
28. Chien, P.S.; Mak, O.T.; Huang, H.J. Induction of COX-2 protein expression by vanadate in A549 human lung carcinoma cell line through EGF receptor and p38 MAPK-mediated pathway. Biochem. Biophys. Res. Commun. 2006, 339, 562–568.
29. Boulassel, B.; Sadeg, N.; Roussel, O.; Perrin, M.; Belhadj-Tahar, H. Fatal poisoning by vanadium. Forensic Sci. Int. 2011, 206, e79–e81.
30. Crans, D.C.; Smee, J.J.; Gaidamauskas, E.; Yang, L. The chemistry and biochemistry of vanadium and the biological activities exerted by vanadium compounds. Chem. Rev. 2004, 104, 849–902.
31. Yang, X.; Wang, K.; Lu, J.; Crans, D.C. Membrane transport of vanadium compounds and the interaction with the erythrocyte membrane. Coord. Chem. Rev. 2003, 237, 103–111.
32. Bruech, M.; Quintanilla, M.E.; Legrum, W.; Koch, J.; Netter, K.J.; Fuhrmann, G.F. Effects of vanadate on intracellular reduction equivalents in mouse liver and the fate of vanadium in plasma, erythrocytes and liver. Toxicology 1984, 31, 283–295.
33. Ding, M.; Gannett, P.M.; Rojanasakul, Y.; Liu, K.; Shi, X. One-electron reduction of vanadate by ascorbate and related free radical generation at physiological pH. J. Inorg. Biochem. 1994, 55, 101–112.
34. Shi, X.L.; Dalal, N.S. Flavoenzymes reduce vanadium (V) and molecular oxygen and generate hydroxyl radical. Arch. Biochem. Biophys. 1991, 289, 355–361.
35. Shi, X.; Dalal, N.S. Hydroxyl radical generation in the NADH/microsomal reduction of vanadate. Free Radic. Res. Commun. 1992, 17, 369–376.
36. Shi, X.; Dalal, N.S. Vanadate-mediated hydroxyl radical generation from superoxide radical in the presence of NADH: Haber–Weiss vs. Fenton mechanism. Arch. Biochem. Biophys. 1993, 307, 336–341.
37. Capella, L.S.; Gefé, M.R.; Silva, E.F.; Affonso-Mitidieri, O.; Lopes, A.G.; Rumjanek, V.M.; Capella, M.A. Mechanisms of vanadate-induced cellular toxicity: Role of cellular glutathione and NADPH. Arch. Biochem. Biophys. 2002, 406, 65–72.
38. Crans, D.C.; Zhang, B.; Gaidamauskas, E.; Keramidas, A.D.; Willsky, G.R.; Roberts, C.R. Is vanadate reduced by thiols under biological conditions? Changing the redox potential of V(V)/V(IV) by complexation in aqueous solution. Inorg. Chem. 2010, 49, 4245–4256.
39. 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. 1997, 272, 843–851.
40. Meng, F.G.; Zhang, Z.Y. Redox regulation of protein tyrosine phosphatase activity by hydroxyl radical. Biochim. Biophys. Acta 2013, 1834, 464–469.
41. Fantus, I.G.; Deragon, G.; Lai, R.; Tang, S. Modulation of insulin action by vanadate: Evidence of a role for phosphotyrosine phosphatase activity to alter cellular signaling. Mol. Cell. Biochem. 1995, 153, 103–112.
42. Pugazhenthi, S.; Tanha, F.; Dahl, B.; Khandelwal, R.L. Decrease in protein tyrosine phosphatase activities in vanadate-treated obese Zucker (fa/fa) rat liver. Mol. Cell. Biochem. 1995, 153, 125–129.
43. Pugazhenthi, S.; Tanha, F.; Dahl, B.; Khandelwal, R.L. Inhibition of a Src homology 2 domain containing protein tyrosine phosphatase by vanadate in the primary culture of hepatocytes. Arch. Biochem. Biophys. 1996, 335, 273–282.
44. Ostman, A.; Frijhoff, J.; Sandin, A.; Böhmer, F.D. Regulation of protein tyrosine phosphatases by reversible oxidation. J. Biochem. 2011, 150, 345–356.
45. 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. 1996, 271, 22251–22255.
46. Lee, K.; Esselman, W.J. Inhibition of PTPs by H2O2 regulates the activation of distinct MAPK pathways. Free Radic. Biol. Med. 2002, 33, 1121–1132.
47. Sturla, L.M.; Amorino, G.; Alexander, M.S.; Mikkelsen, R.B.; Valerie, K.; Schmidt-Ullrichr, R.K. Requirement of Tyr-992 and Tyr-1173 in phosphorylation of the epidermal growth factor receptor by ionizing radiation and modulation by SHP2. J. Biol. Chem. 2005, 280, 14597–145604.
48. Mbonye, U.R.; Song, I. Posttranscriptional and posttranslational determinants of cyclooxygenase expression. BMB Rep. 2009, 42, 552–560.
49. Ueda, N.; Yamashita, R.; Yamamoto, S.; Ishimura, K. Induction of cyclooxygenase-1 in a human megakaryoblastic cell line (CMK) differentiated by phorbol ester. Biochim. Biophys. Acta 1997, 1344, 103–110.
50. Okahara, K.; Sun, B.; Kambayashi, J. Upregulation of prostacyclin synthesis-related gene expression by shear stress in vascular endothelial cells. Arterioscler. Thromb. Vasc. Biol. 1998, 18, 1922–1926.
51. Gibson, L.L.; Hahner, L.; Osborne-Lawrence, S.; German, Z.; Wu, K.K.; Chambliss, K.L.; Shaul, P.W. Molecular basis of estrogen-induced cyclooxygenase type 1 upregulation in endothelial cells. Circ. Res. 2005, 96, 518–525.
52. Tanabe, T.; Tohnai, N. Cyclooxygenase isozymes and their gene structures and expression. Prostaglandins Other Lipid Mediat. 2002, 68–69, 95–114.
53. Hwang, D.; Jang, B.C.; Yu, G.; Boudreau, M. Expression of mitogen-inducible cyclooxygenase induced by lipopolysaccharide: Mediation through both mitogen-activated protein kinase and NF-kappaB signaling pathways in macrophages. Biochem. Pharmacol. 1997, 54, 87–96.
54. Faour, W.H.; He, Y.; He, Q.W.; de Ladurantaye, M.; Quintero, M.; Mancini, A.; di Battista, J.A. Prostaglandin E(2) regulates the level and stability of cyclooxygenase-2 mRNA through activation of p38 mitogen-activated protein kinase in interleukin-1 beta-treated human synovial fibroblasts. J. Biol. Chem. 2001, 276, 31720–31731.
55. Parfenova, H.; Balabanova, L.; Leffler, C.W. Posttranslational regulation of cyclooxygenase by tyrosine phosphorylation in cerebral endothelial cells. Am. J. Physiol. 1998, 274, C72–C81.
56. Alexanian, A.; Miller, B.; Chesnik, M.; Mirza, S.; Sorokin, A. Post-translational regulation of COX2 activity by FYN in prostate cancer cells. Oncotarget 2014, 5, 4232–4243.
57. Hirai, K.; Takayama, H.; Tomo, K.; Okuma, M. Protein-tyrosine-kinase-dependent expression of cyclo-oxygenase-1 and -2 mRNAs in human endothelial cells. Biochem. J. 1997, 322, 373–377.
58. Hirai, K.; Ezumi, Y.; Nishida, E.; Uchiyama, T.; Takayama, H. Comparative study of vanadate- and phorbol ester-induced cyclo-oxygenase-2 expression in human endothelial cells. Thromb. Haemost. 1999, 82, 1545–1552.
59. DeLong, C.J.; Smith, W.L. An intronic enhancer regulates cyclooxygenase-1 gene expression. Biochem. Biophys. Res. Commun. 2005, 338, 53–61.
60. Ding, M.; Li, J.J.; Leonard, S.S.; Ye, J.P.; Shi, X.; Colburn, N.H.; Castranova, V.; Vallyathan, V. Vanadate-induced activation of activator protein-1: role of reactive oxygen species. Carcinogenesis 1999, 20, 663–668.
61. Chuang, J.Y.; Wang, Y.T.; Yeh, S.H.; Liu, Y.W.; Chang, W.C.; Hung, J.J. Phosphorylation by c-Jun NH2-terminal kinase 1 regulates the stability of transcription factor Sp1 during mitosis. Mol. Biol. Cell 2008, 19, 1139–1151.
62. Chu, S. Transcriptional regulation by post-transcriptional modification-role of phosphorylation in Sp1 transcriptional activity. Gene 2012, 508, 1–8.
63. Chen, F.; Demers, L.M.; Vallyathan, V.; Ding, M.; Lu, Y.; Castranova, V.; Shi, X. Vanadate induction of NF-kappaB involves IkappaB kinase beta and SAPK/ERK kinase 1 in macrophages. J. Biol. Chem. 1999, 274, 20307–20312.
64. Li, Q.; Engelhardt, J.F. Interleukin-1beta induction of NFkappaB is partially regulated by H2O2-mediated activation of NFkappaB-inducing kinase. J. Biol. Chem. 2006, 281, 1495–1505.
65. Jung, K.J.; Lee, E.K.; Yu, B.P.; Chung, H.Y. Significance of protein tyrosine kinase/protein tyrosine phosphatase balance in the regulation of NF-kappaB signaling in the inflammatory process and aging. Free Radic. Biol. Med. 2009, 47, 983–991.
66. Milarski, K.L.; Zhu, G.; Pearl, C.G.; McNamara, D.J.; Dobrusin, E.M.; MacLean, D.; Thieme-Sefler, A.; Zhang, Z.Y.; Sawyer, T.; Decker, S.J.; et al. Sequence specificity in recognition of the epidermal growth factor receptor by protein tyrosine phosphatase 1B. J. Biol. Chem. 1993, 268, 23634–23639.
67. Agazie, Y.M.; Hayman, M.J. Molecular mechanism for a role of SHP2 in epidermal growth factor receptor signaling. Mol. Cell. Biol. 2003, 23, 7875–7886.
68. Keilhack, H.; Tenev, T.; Nyakatura, E.; Godovac-Zimmermann, J.; Nielsen, L.; Seedorf, K.; Böhmer, F.D. Phosphotyrosine 1173 mediates binding of the protein-tyrosine phosphatase SHP-1 to the epidermal growth factor receptor and attenuation of receptor signaling. J. Biol. Chem. 1998, 273, 24839–24846.
69. Jorissen, R.N.; Walker, F.; Pouliot, N.; Garrett, T.P.; Ward, C.W.; Burgess, A.W. Epidermal growth factor receptor: Mechanisms of activation and signaling. Exp. Cell Res. 2003, 284, 31–53.
70. Wu, W.; Graves, L.M.; Jaspers, I.; Devlin, R.B.; Reed, W.; Samet, J.M. Activation of the EGF receptor signaling pathway in human airway epithelial cells exposed to metals. Am. J. Physiol. 1999, 277, L924–L931.
71. Wu, W.; Jaspers, I.; Zhang, W.; Graves, L.M.; Samet, J.M. Role of Ras in metal-induced EGF receptor signaling and NF-kappaB activation in human airway epithelial cells. Lung Cell. Mol. Physiol. 2002, 282, L1040–L1048.
72. Tao, Q.; Spring, S.C.; Terman, B.I. Comparison of the signaling mechanisms by which VEGF, H2O2, and phosphatase inhibitors activate endothelial cell ERK1/2 MAP-kinase. Microvasc. Res. 2005, 69, 36–44.
73. Roskoski, R. Src kinase regulation by phosphorylation and dephosphorylation. Biochem. Biophys. Res. Commun. 2005, 331, 1–14.
74. Ingley, E. Src family kinases: Regulation of their activities, levels and identification of new pathways. Biochim. Biophys. Acta 2008, 1784, 56–65.
75. Roskoski, R. Src protein-tyrosine kinase structure and regulation. Biochem. Biophys. Res. Commun. 2004, 324, 1155–1164.
76. Chiarugi, P. Src redox regulation: There is more than meets the eye. Mol. Cells 2008, 26, 329–337.
77. Giannoni, E.; Taddei, M.L.; Chiarugi, P. Src redox regulation: again in the front line. Free Radic. Biol. Med. 2010, 49, 516–527.
78. Lluis, J.M.; Buricchi, F.; Chiarugi, P.; Morales, A.; Fernandez-Checa, J.C. Dual role of mitochondrial reactive oxygen species in hypoxia signaling: Activation of nuclear factor-κB via c-SRC and oxidant-dependent cell death. Cancer Res. 2007, 67, 7368–7377.
79. Boulven, I.; Robin, P.; Desmyter, C.; Harbon, S.; Leiber, D. Differential involvement of Src family kinases in pervanadate-mediated responses in rat myometrial cells. Cell Signal. 2002, 14, 341–349.
80. Fan, C.; Li, Q.; Ross, D.; Engelhardt, J.F. Tyrosine phosphorylation of I kappa B alpha activates NF kappa B through a redox-regulated and c-Src-dependent mechanism following hypoxia/reoxygenation. J. Biol. Chem. 2003, 278, 2072–2080.
81. Kmiecik, T.E.; Johnson, P.J.; Shalloway, D. Regulation by the autophosphorylation site in overexpressed pp60c-src. Mol. Cell. Biol. 1988, 8, 4541–4546.
82. Irtegun, S.; Wood, R.J.; Ormsby, A.R.; Mulhern, T.D.; Hatters, D.M. Tyrosine 416 is phosphorylated in the closed, repressed conformation of c-Src. PLoS ONE 2013, 8, e71035.
83. Farooq, A.; Zhou, M.M. Structure and regulation of MAPK phosphatases. Cell Signal. 2004, 16, 769–779.
84. Kondoh, K.; Nishida, E. Regulation of MAP kinases by MAP kinase phosphatases. Biochim. Biophys. Acta 2007, 1773, 1227–1237.
85. Turpeinen, T.; Nieminen, R.; Moilanen, E.; Korhonen, R. Mitogen-activated protein kinase phosphatase-1 negatively regulates the expression of interleukin-6, interleukin-8, and cyclooxygenase-2 in A549 human lung epithelial cells. J. Pharmacol. Exp. Ther. 2010, 333, 310–318.
86. Misra-Press, A.; Rim, C.S.; Yao, H.; Roberson, M.S.; Stork, P.J. A novel mitogen-activated protein kinase phosphatase. Structure, expression, and regulation. J. Biol. Chem. 1995, 270, 14587–14596.
87. Muda, M.; Boschert, U.; Smith, A.; Antonsson, B.; Gillieron, C.; Chabert, C.; Camps, M.; Martinou, I.; Ashworth, A.; Arkinstall, S. Molecular cloning and functional characterization of a novel mitogen-activated protein kinase phosphatase, MKP-4. J. Biol. Chem. 1997, 272, 5141–5151.
88. Han, D.; Ybanez, M.D.; Ahmadi, S.; Yeh, K.; Kaplowitz, N. Redox regulation of tumor necrosis factor signaling. Antioxid. Redox Signal. 2009, 11, 2245–2263.
89. O’Dea, E.; Hoffmann, A. The regulatory logic of the NF-kappaB signaling system. Cold Spring Harb. Perspect. Biol. 2010, 2, a000216.
90. Barbeau, B.; Bernier, R.; Dumais, N.; Briand, G.; Olivier, M.; Faure, R.; Posner, B.I.; Tremblay, M. Activation of HIV-1 long terminal repeat transcription and virus replication via NF-kappaB-dependent and -independent pathways by potent phosphotyrosine phosphatase inhibitors, the peroxovanadium compounds. J. Biol. Chem. 1997, 272, 12968–12977.
91. Lee, F.S.; Peters, R.T.; Dang, L.C.; Maniatis, T. MEKK1 activates both IkappaB kinase alpha and IkappaB kinase beta. Proc. Natl. Acad. Sci. USA 1998, 95, 9319–9324.
92. Herscovitch, M.; Comb, W.; Ennis, T.; Coleman, K.; Yong, S.; Armstead, B.; Kalaitzidis, D.; Chandani, S.; Gilmore, T.D. Intermolecular disulfide bond formation in the NEMO dimer requires Cys54 and Cys347. Biochem. Biophys. Res. Commun. 2008, 367, 103–108.
93. Morgan, M.J.; Liu, Z.G. Crosstalk of reactive oxygen species and NF-κB signaling. Cell Res. 2011, 21, 103–115.
94. Siomek, A. NF-κB signaling pathway and free radical impact. Acta Biochim. Pol. 2012, 59, 323–331.
95. Imbert, V.; Rupec, R.A.; Livolsi, A.; Pahl, H.L.; Traenckner, E.B.; Mueller-Dieckmann, C.; Farahifar, D.; Rossi, B.; Auberger, P.; Baeuerle, P.A.; et al. Tyrosine phosphorylation of I kappa B-alpha activates NF-kappa B without proteolytic degradation of I kappa B-alpha. Cell 1996, 86, 787–798.
96. Singh, S.; Darnay, B.G.; Aggarwal, B.B. Site-specific tyrosine phosphorylation of IkappaBalpha negatively regulates its inducible phosphorylation and degradation. J. Biol. Chem. 1996, 271, 31049–31054.
97. Béraud, C.; Henzel, W.J.; Baeuerle, P.A. Involvement of regulatory and catalytic subunits of phosphoinositide 3-kinase in NF-kappaB activation. Proc. Natl. Acad. Sci. USA 1999, 96, 429–434.
98. Mukhopadhyay, A.; Manna, S.K.; Aggarwal, B.B. Pervanadate-induced nuclear factor-kappaB activation requires tyrosine phosphorylation and degradation of IkappaBalpha. Comparison with tumor necrosis factor-alpha. J. Biol. Chem. 2000, 275, 8549–8555.
99. Singh, S.; Aggarwal, B.B. Protein-tyrosine phosphatase inhibitors block tumor necrosis factor-dependent activation of the nuclear transcription factor NF-kappa B. J. Biol. Chem. 1995, 270, 10631–10639.
100. Kang, Y.J.; Mbonye, U.R.; DeLong, C.J.; Wada, M.; Smith, W.L. Regulation of intracellular cyclooxygenase levels by gene transcription and protein degradation. Prog. Lipid Res. 2007, 46, 108–125.
101. Tanaka, K.; Waxman, L.; Goldberg, A.L. Vanadate inhibits the ATP-dependent degradation of proteins in reticulocytes without affecting ubiquitin conjugation. J. Biol. Chem. 1984, 259, 2803–2809.
102. Kanayama, H.O.; Tamura, T.; Ugai, S.; Kagawa, S.; Tanahashi, N.; Yoshimura, T.; Tanaka, K.; Ichihara, A. Demonstration that a human 26S proteolytic complex consists of a proteasome and multiple associated protein components and hydrolyzes ATP and ubiquitin-ligated proteins by closely linked mechanisms. Eur. J. Biochem. 1992, 206, 567–578.
103. Misra, A.; Srivastava, S.; Ankireddy, S.R.; Islam, N.S.; Chandra, T.; Kumar, A.; Barthwal, M.K.; Dikshit, M. Phospholipase C-γ2 via p38 and ERK1/2 MAP kinase mediates diperoxovanadate-asparagine induced human platelet aggregation and sCD40L release. Redox Rep. 2013, 18, 174–185.
104. Murakami, M.; Kudo, I. Phospholipase A2. J. Biochem. 2002, 131, 285–292.
105. Goldman, R.; Ferber, E.; Zor, U. Involvement of reactive oxygen species in phospholipase A2 activation: Inhibition of protein tyrosine phosphatases and activation of protein kinases. Adv. Exp. Med. Biol. 1997, 400A, 25–30.
106. Helgadóttir, A.; Halldórsson, H.; Magnúsdóttir, K.; Kjeld, M.; Thorgeirsson, G. A role for tyrosine phosphorylation in generation of inositol phosphates and prostacyclin production in endothelial cells. Arterioscler. Thromb. Vasc. Biol. 1997, 17, 287–294.
107. Varecka, L.; Peterajová, E.; Sevcík, J. Vanadate changes Ca2+ influx pathway properties in human red blood cells. Gen. Physiol. Biophys. 1997, 16, 359–372.
108. Törnquist, K.; Dugué, B.; Ekokoski, E. Protein tyrosine phosphorylation and calcium signaling in thyroid FRTL-5 cells. J. Cell. Physiol. 1998, 175, 211–219.
109. Randazzo, P.A.; Olshan, J.S.; Bijivi, A.A.; Jarett, L. The effect of orthovanadate on phosphoinositide metabolism in NIH 3T3 fibroblasts. Arch. Biochem. Biophys. 1992, 292, 258–265.
110. Bianchini, L.; Todderud, G.; Grinstein, S. Cytosolic [Ca2+] homeostasis and tyrosine phosphorylation of phospholipase C gamma 2 in HL60 granulocytes. J. Biol. Chem. 1993, 268, 3357–3363.
111. Ohmori, T.; Yatomi, Y.; Wu, Y.; Osada, M.; Satoh, K.; Ozaki, Y. Wheat germ agglutinin-induced platelet activation via platelet endothelial cell adhesion molecule-1: Involvement of rapid phospholipase C gamma 2 activation by Src family kinases. Biochemistry 2001, 40, 12992–13001.
112. Choi, J.H.; Ryu, S.H.; Suh, P.G. On/off-regulation of phospholipase C-gamma 1-mediated signal transduction. Adv. Enzym. Regul. 2007, 47, 104–116.
113. Machide, M.; Kamitori, K.; Kohsaka, S. Hepatocyte growth factor-induced differential activation of phospholipase cgamma 1 and phosphatidylinositol 3-kinase is regulated by tyrosine phosphatase SHP-1 in astrocytes. J. Biol. Chem. 2000, 275, 31392–31398.
114. Kawakami, N.; Shimohama, S.; Hayakawa, T.; Sumida, Y.; Fujimoto, S. Tyrosine phosphorylation and translocation of phospholipase C-gamma 2 in polymorphonuclear leukocytes treated with pervanadate. Biochim. Biophys. Acta 1996, 1314, 167–174.
115. Irani, K.; Pham, Y.; Coleman, L.D.; Roos, C.; Cooke, G.E.; Miodovnik, A.; Karim, N.; Wilhide, C.C.; Bray, P.F.; Goldschmidt-Clermont, P.J. Priming of platelet alphaIIbbeta3 by oxidants is associated with tyrosine phosphorylation of beta3. Arterioscler. Thromb. Vasc. Biol. 1998, 18, 1698–706.
116. Shanmugam, N.; Gaw Gonzalo, I.T.; Natarajan, R. Molecular mechanisms of high glucose-induced cyclooxygenase-2 expression in monocytes. Diabetes 2004, 53, 795–802.
117. Kordowiak, A.M.; Klein, A.; Goc, A.; Dabroś, W. Comparison of the effect of VOSO4, Na3VO4 and NaVO3 on proliferation, viability and morphology of H35-19 rat hepatoma cell line. Pol. J. Pathol. 2007, 58, 51–57.
118. Cuesta, S.; Francés, D.; García, G.B. ROS formation and antioxidant status in brain areas of rats exposed to sodium metavanadate. Neurotoxicol. Teratol. 2011, 33, 297–302.