Spry2-mediated inhibition of the Ras/ERK pathway through interaction with Src kinase following cerebral ischemia

References

• Sugino T, Nozaki K, Takagi Y, Hattori I, Hashimoto N, Moriguchi T, et al. Activation of mitogen-activated protein kinases after transient forebrain ischemia in gerbil hippocampus. Journal of Neuroscience 2000; 20: 4506–4514
   PubMed Web of Science ®Google Scholar
• Bae JH, Jang BC, Suh SI, Ha E, Baik HH, Kim SS, Lee MY, Shin DH. Manganese induces inducible nitric oxide synthase (iNOS) expression via activation of both MAP kinase and PI3K/Akt pathways in BV2 microglial cells. Neuroscience Letters 2006; 398: 151–154
   PubMed Web of Science ®Google Scholar
• Park EM, Joh TH, Volpe BT, Chu CK, Song G, Cho S. A neuroprotective role of extracellular signal-regulated kinase in N-acetyl-O-methyldopamine-treated hippocampal neurons after exposure to in vitroand in vivoischemia. Neuroscience 2004; 123: 147–154
   PubMedGoogle Scholar
• Guo J, Wu HW, Hu G, Han X, De W, Sun YJ. Sustained activation of Src-family tyrosine kinases by ischemia: A potential mechanism mediating extracellular signal-regulated kinase cascades in hippocampal dentate gyrus. Neuroscience 2006; 143: 827–836
   PubMed Web of Science ®Google Scholar
• Casci T, Vinos J, Freeman M. Sprouty, an intracellular inhibitor of Ras signaling. Cell 1999; 96: 655–665
   PubMed Web of Science ®Google Scholar
• Chandler LJ, Sutton G, Dorairaj NR. N-methyl D-aspartate receptor-mediated bidirectional control of extracellular signal-regulated kinase activity in cortical neuronal cultures. Journal of Biological Chemistry 2001; 276: 2627–2636
   PubMed Web of Science ®Google Scholar
• Zhang S, Lin Y, Itaranta P, Yagi A, Vainio S. Expression of Sprouty genes 1, 2 and 4 during mouse organogenesis. Mechanical Developments 2001; 109: 367–370
   Google Scholar
• Li Z, Hosoi Y, Cai K, Tanno Y, Matsumoto Y, Enomoto A, Morita A, Nakagawa K, Miyagawa K. Src tyrosine kinase inhibitor PP2 suppresses ERK1/2 activation and epidermal growth factor receptor transactivation by X-irradiation. Biochemistry and Biophysics Research Communications 2006; 341: 363–368
   PubMed Web of Science ®Google Scholar
• Mason JM, Morrison DJ, Bassit B, Dimri M, Band H, Licht JD, et al. Tyrosine phosphorylation of Sprouty proteins regulates their ability to inhibit growth factor signaling, a dual feedback loop. Molecular Biology of the Cell 2004; 15: 2176–2188
   PubMedGoogle Scholar
• Hanafusa H, Torii S, Yasunaga T, Nishida E. Sprouty1 and Sprouty2 provide a control mechanism for the Ras/MAPK signalling pathway. Natural Cell Biology 2002; 4: 850–858
   PubMed Web of Science ®Google Scholar
• Ryan PE, Davies GC, Nau MM, Lipkowitz S. Regulating the regulator: negative regulation of Cbl ubiquitin ligases. Trends in Biochemical Science 2006; 31: 79–88
   PubMedGoogle Scholar
• Hong JK, Dafna B. Modulation of signalling by sprouty: a developing story. Nature Reviews in Molecular Cell Biology 2004; 5: 441–450
   PubMedGoogle Scholar
• Pulsinelli WA, Brierley JB. A new model of bilateral hemispheric ischemia in the unanesthetized rat. Stroke 1979; 10: 267–272
   PubMed Web of Science ®Google Scholar
• Bradford MM. A rapid and sensitive for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 1976; 72: 248–254
   PubMed Web of Science ®Google Scholar
• Guo J, Meng F, Zhang G, Zhang Q. Free radicals are involved in continuous activation of nonreceptor tyrosine protein kinase c-Src after ischemia-reperfusion in rat hippocampus. Neuroscience Letters 2003; 345: 101–104
   PubMedGoogle Scholar
• Ivanov A, Pellegrino C, Rama S, Dumalska I, Salyha Y, Ben-Ari Y, Medina I. Opposing role of synaptic and extrasynaptic NMDA receptors in regulation of the extracellular signal-regulated kinases (ERK) activity in cultured rat hippocampal neurons. Journal of Physiology 2006; 572: 789–798
   PubMed Web of Science ®Google Scholar
• Rusanescu G, Qi H, Thomas SM, Brugge JS, Halegoua S. Calcium influx induces neurite growth through a Src-Ras signaling cassette. Neuron 1995; 15: 1415–1425
   PubMed Web of Science ®Google Scholar
• Aikawa R, Komuro I, Yamazaki T, Zou Y, Kudoh S, Tanaka M, et al. Oxidative stress activates extracellular signal-regulated kinases through Src and Ras in cultured cardiac myocytes of neonatal rats. Journal of Clinical Investigations 1997; 100: 1813–1821
   PubMed Web of Science ®Google Scholar
• Salter MW, Kalia LV. Src kinases: a hub for NMDA receptor regulation. Nature Reviews in Neuroscience 2004; 5: 317–328
   PubMed Web of Science ®Google Scholar
• Li X, Brunton VG, Burgar HR, Wheldon LM, Heath JK. FRS2-dependent SRC activation is required for fibroblast growth factor receptor-induced phosphorylation of Sprouty and suppression of ERK activity. Journal of Cell Science 2004; 117: 6007–6017
   PubMedGoogle Scholar
• Huo JZ, Dykstra CM, Gurd JW. Increase in tyrosine phosphorylation of the NMDA receptor following the induction of status epilepticus. Neuroscience Letters 2006; 401: 266–270
   PubMedGoogle Scholar
• Anteby EY, Natanson-Yaron S, Greenfield C, Goldman-Wohl D, Haimov-Kochman R, Holzer H, Yagel S. Human placental Hofbauer cells express sprouty proteins: a possible modulating mechanism of villous branching. Placenta 2005; 26: 476–483
   PubMedGoogle Scholar
• Gross I, Bassit B, Benezra M, Licht JD. Mammalian Sprouty proteins inhibit cell growth and differentiation by preventing Ras activation. Journal of Biological Chemistry 2001; 276: 46460–46468
   PubMed Web of Science ®Google Scholar
• Yusoff P, Lao DH, Ong SH, Wong ES, Lim J, Lo TL, et al. Sprouty2 inhibits the Ras/MAP kinase pathway by inhibiting the activation of Raf. Journal of Biological Chemistry 2002; 277: 3195–3201
   PubMed Web of Science ®Google Scholar