The effects of dehydrocostus lactone on osteoblastic MC3T3-E1 cells in redox changes and PI3K/Akt/CREB

References

• Andreyev, A.Y., Kushnareva, Y.E., Starkov, A.A. Mitochondrial metabolism of reactive oxygen species. Biochemistry Mosc 2005, 70, 200–214.
   PubMed Web of Science ®Google Scholar
• Maguire, J.J., Kagan, V.E., Packer, L. Electron transport between cytochrome c and alpha tocopherol. Biochem Biophys Res Commun 1992, 188, 190–197.
   PubMed Web of Science ®Google Scholar
• Baudry, N., Laemmel, E., Vicaut, E. In vivo reactive oxygen species production induced by ischemia in muscle arterioles of mice: involvement of xanthine oxidase and mitochondria. Am J Physiol Heart Circ Physiol 2008, 294, H821–H828.
   PubMed Web of Science ®Google Scholar
• Franke, T.F., Kaplan, D.R., Cantley, L.C. PI3K: downstream AKTion blocks apoptosis. Cell 1997, 88, 435–437.
   PubMed Web of Science ®Google Scholar
• Du, K., Montminy, M. CREB is a regulatory target for the protein kinase Akt/PKB. J Biol Chem 1998, 273, 32377–32379.
   PubMed Web of Science ®Google Scholar
• Cammarota, M., Paratcha, G., Bevilaqua, L.R., Levi de Stein, M., Lopez, M., Pellegrino de Iraldi, A., Izquierdo, I., Medina, J.H. Cyclic AMP-responsive element binding protein in brain mitochondria. J Neurochem 1999, 72, 2272–2277.
   PubMed Web of Science ®Google Scholar
• Ryu, H., Lee, J., Impey, S., Ratan, R.R., Ferrante, R.J. Antioxidants modulate mitochondrial PKA and increase CREB binding to D-loop DNA of the mitochondrial genome in neurons. Proc Natl Acad Sci USA 2005, 102, 13915–13920.
   PubMed Web of Science ®Google Scholar
• Damre, A.A., Damre, A.S., Saraf, M.N. Evaluation of sesquiterpene lactone fraction of Saussurea lappa on transudative, exudative and proliferative phases of inflammation. Phytother Res 2003, 17, 722–725.
   PubMed Web of Science ®Google Scholar
• Rüngeler, P., Castro, V., Mora, G., Gören, N., Vichnewski, W., Pahl, H.L., Merfort, I., Schmidt, T.J. Inhibition of transcription factor NF-κB by sesquiterpene lactones: a proposed molecular mechanism of action. Bioorg Med Chem 1999, 7, 2343–2352.
   PubMed Web of Science ®Google Scholar
• Lee, H.J., Kim, N.Y., Jang, M.K., Son, H.J., Kim, K.M., Sohn, D.H., Lee, S.H., Ryu, J.H. A sesquiterpene, dehydrocostus lactone, inhibits the expression of inducible nitric oxide synthase and TNF-alpha in LPS-activated macrophages. Planta Med 1999, 65, 104–108.
   PubMed Web of Science ®Google Scholar
• Choi, E.M., Kim, G.H., Lee, Y.S. Protective effects of dehydrocostus lactone against hydrogen peroxide-induced dysfunction and oxidative stress in osteoblastic MC3T3-E1 cells. Toxicol In Vitro 2009, 23, 862–867.
   PubMed Web of Science ®Google Scholar
• Quarles, L.D., Yohay, D.A., Lever, L.W., Caton, R., Wenstrup, R.J. Distinct proliferative and differentiated stages of murine MC3T3-E1 cells in culture: an in vitro model of osteoblast development. J Bone Miner Res 1992, 7, 68C3–692.
   Google Scholar
• Downward, J. PI 3-kinase, Akt and cell survival. Semin Cell Dev Biol 2004, 15, 177–182.
   Google Scholar
• Sarbassov, D.D., Ali, S.M., Kim, D.H., Guertin, D.A., Latek, R.R., Erdjument-Bromage, H., Tempst, P., Sabatini, D.M. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr Biol 2004, 14, 1296–1302.
   PubMed Web of Science ®Google Scholar
• Yao, R., Cooper, G.M. Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor. Science 1995, 267, 2003–2006.
   PubMed Web of Science ®Google Scholar
• del Peso, L., González-García, M., Page, C., Herrera, R., Nuñez, G. Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 1997, 278, 687–689.
   PubMed Web of Science ®Google Scholar
• Ozes, O.N., Mayo, L.D., Gustin, J.A., Pfeffer, S.R., Pfeffer, L.M., Donner, D.B. NF-κB activation by tumour necrosis factor requires the Akt serine-threonine kinase. Nature 1999, 401, 82–85.
   PubMed Web of Science ®Google Scholar
• Lauder, A., Castellanos, A., Weston, K. c-Myb transcription is activated by protein kinase B (PKB) following interleukin 2 stimulation of Tcells and is required for PKB-mediated protection from apoptosis. Mol Cell Biol 2001, 21, 5797–5805.
   PubMed Web of Science ®Google Scholar
• Mayr, B., Montminy, M. Transcriptional regulation by the phosphorylation-dependent factor CREB. Nat Rev Mol Cell Biol 2001, 2, 599–609.
   PubMed Web of Science ®Google Scholar
• Brami-Cherrier, K., Valjent, E., Garcia, M., Pagès, C., Hipskind, R.A., Caboche, J. Dopamine induces a PI3-kinase-independent activation of Akt in striatal neurons: a new route to cAMP response element-binding protein phosphorylation. J Neurosci 2002, 22, 8911–8921.
   PubMed Web of Science ®Google Scholar
• Fiol, C.J., Williams, J.S., Chou, C.H., Wang, Q.M., Roach, P.J., Andrisani, O.M. A secondary phosphorylation of CREB341 at Ser129 is required for the cAMP-mediated control of gene expression. A role for glycogen synthase kinase-3 in the control of gene expression. J Biol Chem 1994, 269, 32187–32193.
   PubMedGoogle Scholar
• Grimes, C.A., Jope, R.S. CREB DNA binding activity is inhibited by glycogen synthase kinase-3 β and facilitated by lithium. J Neurochem 2001, 78, 1219–1232.
   PubMed Web of Science ®Google Scholar
• Berndt, C., Lillig, C.H., Holmgren, A. Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system. Am J Physiol Heart Circ Physiol 2007, 292, H1227–H1236.
   PubMed Web of Science ®Google Scholar
• Yamawaki, H., Haendeler, J., Berk, B.C. Thioredoxin: a key regulator of cardiovascular homeostasis. Circ Res 2003, 93, 1029–1033.
   PubMed Web of Science ®Google Scholar
• Myers, J.M., Myers, C.R. The effects of hexavalent chromium on thioredoxin reductase and peroxiredoxins in human bronchial epithelial cells. Free Radic Biol Med 2009, 47, 1477–1485.
   PubMed Web of Science ®Google Scholar
• Belenky, P., Bogan, K.L., Brenner, C. NAD+ metabolism in health and disease. Trends Biochem Sci 2007, 32, 12–19.
   PubMed Web of Science ®Google Scholar
• Pollak, N., Dölle, C., Ziegler, M. The power to reduce: pyridine nucleotides–small molecules with a multitude of functions. Biochem J 2007, 402, 205–218.
   PubMed Web of Science ®Google Scholar