Modulation of ERK1/2 activity is crucial for sphingosine-induced death of glioma C6 cells

• Authors: Patryk Krzemiński
• Languages of publication: EN

Abstracts

EN

In this study the contribution of the ERK1/2 pathway to sphingosine-induced death and morphological changes of the actin cytoskeleton in glioma C6 cells was investigated. Surprisingly, the level of ERK1/2 phosphorylation does not change after incubation of cells with sphingosine. Despite this, sphingosine induces rounding and detachment of cells without formation of apoptotic bodies. To shed light on this process, a specific inhibitor of ERK1/2 phosphorylation, U0126, was used. Cells incubated simultaneously with sphingosine and U0126 not only detached, but also exhibited formation of apoptotic-like blebs. These data suggest that during sphingosine-induced glioma C6 cell death apoptotic blebbing is dependent on ERK1/2 signalling and occurs only when ERK1/2 activity is decreased or abolished.

Keywords

EN

glioma C6; ERK1/2; cytoskeleton; programmed cell death

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2005
• Volume: 52
• Issue: 4
• Pages: 927-930

Dates

published

2005

received

2005-07-07

revised

2005-10-19

accepted

2005-10-20

(unknown)

2005-11-21

Contributors

author

Patryk Krzemiński

• Laboratory of Signal Transduction, Department of Cellular and Molecular Neurobiology, Nencki Institute of Experimental Biology, Warszawa, Poland

References

• Amran D (2005) Biochim Biophys Acta 1743: 269-279.
• Bhaskara VK, Panigrahi M, Challa S, Babu PP (2005) Neuropathology 25: 48-53.
• Boldt S, Weidle UH, Kolch W (2002) Carcinogenesis 23: 1831-1838.
• Burstein E, Duckett CS (2003) Curr Opin Cell Biol 15: 732-737.
• Chang SE, Kim KJ, Ro KH, Lim YJ, Choi JH, Moon KC, Sung KJ (2004) J Dermatol 31: 1-5.
• Cuvillier O (2002) Biochim Biophys Acta 1585: 153-162.
• Daido S, Kanzawa T, Yamamoto A, Takeuchi H, Kondo Y, Kondo S (2004) Cancer Res 64: 4286-4293.
• Dawson G, Goswami R, Kilkus J, Wiesner D, Dawson S (1998) Acta Biochim Polon 45: 287-297.
• Domnina LV, Ivanova OY, Pletjushkina OY, Fetisova EK, Chernyak B, Skulachev VP, Vasiliev JM (2004) Cell Biol Int 28: 471-475.
• Engelbrecht AM, Gebhardt S, Louw L (2005) Cancer Lett (available on line May 31).
• Fang JY, Richardson BC (2005) Lancet Oncol 6: 322-327.
• Favata MF, Horiuchi KY, Manos EJ, Daulerio AJ, Stradley DA, Feeser WS, Van Dyk DE, Pitts WJ, Earl RA, Hobbs F, Copeland RA, Magolda RL, Scherle PA, Trzaskos JM (1998) J Biol Chem 273: 18623-18632.
• Freeman SM (2004) Drug News Perspect 17: 237-242.
• Green DR (1998) Cell 94: 695-698.
• Harada J, Foley M, Moskowitz MA, Waeber C (2004) J Neurochem 88: 1026-1039.
• Kerr JFR, Wyllie AH, Currie AR (1972) Br J Cancer 26: 239-257.
• Lockman K, Hinson JS, Medlin MD, Morris D, Taylor JM, Mack CP (2004) J Biol Chem 279: 42422-42430.
• Mengubas K, Riordan FA, Bravery CA, Lewin J, Owens DL, Mehta AB, Hoffbrand AV, Wickremasinghe RG (1999) Oncogene 18: 2499-2506.
• Miller F, Kaplan DR (2001) Cell Mol Life Sci 58: 1045-1053.
• Pascual M, Valles SL, Renau-Piqueras J, Guerri C (2003) J Neurochem 87: 1535-1545.
• Pebay A, Toutant M, Premont J, Calvo CF, Venance L, Cordier J, Glowinski J, Tence M (2001) Eur J Neurosci 13: 2067-2076.
• Spiegel S, Cuvillier O, Edsall LC, Kohama T, Menzeleev R, Olah Z, Olivera A, Pirianov G, Thomas DM, Tu Z, Van Brocklyn JR, Wang F (1998) Ann N Y Acad Sci 845: 11-18.
• Stoica BA, Movsesyan VA, Lea PM, Faden AI (2003) Mol Cell Neurosci 22: 365-382.
• Sweeney EA, Sakakura C, Shirahama T, Masamune A, Ohta H, Hakomori S, Igarashi Y (1996) Int J Cancer 66: 358-366.
• Van Brocklyn JR, Tu Z, Edsall LC, Schmidt RR, Spiegel S (1999) J Biol Chem 274: 4626-4632.
• Wajant H, Pfizenmaier K, Scheurich P (2003) Cytokine Growth Factor Rev 14: 53-66.