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2006 | 53 | 4 | 825-831

Article title

Effect of Rho-associated kinase inhibition on actin cytoskeleton structure and calcium response in glioma C6 cells

Content

Title variants

Languages of publication

EN

Abstracts

EN
The role of actin cytoskeleton functional state in glioma C6 cell morphology and calcium signaling was investigated through modification of myosin II activity by blocking Rho-associated kinase with the specific inhibitor Y-27632. Treatment of glioma C6 cells with ROCK inhibitor resulted in actin cytoskeleton reorganization and also in the changed shape and distribution of mitochondria. Changes in the distribution of ER, the main calcium store in glioma C6 cells, were not visible. The inhibition of myosin II activity influences the first phase of calcium signaling evoked by agonist, and both phases of thapsigargin-evoked calcium response. We suggest that the observed increase in Ca2+ release from intracellular stores induced by IP3 formation as well as inhibition of SERCA ATPase is at least in part related to severely affected mitochondria. Enhancement of capacitative calcium entry evoked by thapsigargin is probably associated with the reorganization of the acto-myosin II system. ATP-induced calcium response presents no changes in the second phase. We observed that ATP stimulation of Y-27632 pretreated cells leads to immediate morphological rearrangement of glioma C6 cells. It is a consequence of actin cytoskeleton reorganization: formation of stress fibers and relocation of phosphorylated myosin II to actin filaments. It seems that the agonist-evoked strong calcium signal may be sufficient for myosin II activation and the stress fiber organization. This is the first work showing the dependence between the functional state of the acto-myosin II system and calcium signaling stressing the reversible character of this relationship.

Year

Volume

53

Issue

4

Pages

825-831

Physical description

Dates

published
2006
received
2006-10-01
revised
2006-11-08
accepted
2006-11-16
(unknown)
2006-11-19

Contributors

  • Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology Polish Academy of Sciences, Warszawa, Poland
  • Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology Polish Academy of Sciences, Warszawa, Poland
  • Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology Polish Academy of Sciences, Warszawa, Poland
  • Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology Polish Academy of Sciences, Warszawa, Poland
  • Department of Muscle Biochemistry, Nencki Institute of Experimental Biology Polish Academy of Sciences, Warszawa, Poland
  • Department of Molecular and Cellular Neurobiology, Nencki Institute of Experimental Biology Polish Academy of Sciences, Warszawa, Poland

References

  • Aber S, Barbayannis FA, Hanser H, Schneider C, Stanyon CA, Bernard O, Caroni P (1998) Nature 393: 805-809.
  • Berridge MJ (1995) Biochem J 312: 1-11.
  • Bishop AL, Hall A (2000) Biochem J 348: 241-255.
  • Burridge K, Chrzanowska-Wodnicka M (1996) Annu Rev Cell Biol 12: 463-518.
  • Clapham DE (1995) Cell 80: 259-268.
  • Czajkowski R, Lei L, Sabała P, Barańska J (2002) FEBS Lett 513: 179-183.
  • Fukata Y, Amano M, Kaibuchi K (2001) Trends Pharmacol Sci 22: 32-39.
  • Grynkiewicz G, Poenie M, Tsien RY (1985) J Biol Chem 260: 3440-3450.
  • Katoh K, Kano Y, Amano M, Onishi H, Kaibuchi K, Fujiwara K (2001) J Cell Biol 153: 569-583.
  • Kimura K, Ito M, Amano M, Chihara K, Fukata Y, Nakafuku M, Yamamori B, Feng J, Nakano T, Okawa K, Iwamatsu A, Kaibuchi K (1996) Science 273: 245-248.
  • Leung T, Chen XQ, Manser E, Lim L (1996) Mol Cell Biol 16: 5313-5327.
  • Matsui T et al. (1996) EMBO J 15: 2208-2216.
  • Nobes CD, Hawkins P, Stephens L, Hall A (1995) J Cell Sci 108: 225-233.
  • Omatsu-Kanbe M, Shibata M, Yamamoto T, Isono T, Matsuura H (2004) Biochem J 381: 389-396.
  • Pomorski P, Targos B, Barańska J (2005) Biochem Biophys Res Commun 328: 1126-1132.
  • Putney JW Jr (1986) Cell Calcium 7: 1-12.
  • Putney JW Jr, Bird G (1993) Endocr Rev 14: 610-631.
  • Ren XD, Kiosses WB, Sieg DJ, Otey CA, Schlaepfer DD, Schwartz MA (2000) J Cell Sci 113: 3673-3678.
  • Ridley AJ, Hall A (1992) Cell 70: 389-399.
  • Ridley AJ, Paterson HF, Johnston CL, Diekmann D, Hall A (1992) Cell 70: 401-410.
  • Riento K, Ridley AJ (2003) Nat Rev Mol Cell Biol 4: 446-456.
  • Rizzuto R, Pozzan T (2006) Physiol Rev 86: 369-408.
  • Rottner K, Hall A, Small JV (1999) Curr Biol 9: 640-648.
  • Sabała P, Czajkowski R, Przybyłek K, Kalita K, Kaczmarek L, Barańska J (2001) Br J Pharmacol 132: 393-402.
  • Sabała P, Targos B, Caravelli A, Czajkowski R, Lim D, Gragnanicllo G, Santella L, Barańska J (2002) Biochem Biophys Res Commun 296: 484-491.
  • Supłat D, Targos B, Sabała P, Barańska J, Pomorski P (2004) Biochem Biophys Res Commun 323: 870-875.
  • Targos B, Barańska J, Pomorski P (2005) Acta Biochim Polon 52: 379-409.
  • Tsuji et al. (2002) J Cell Biol 157: 819-830.
  • Van Aelst L, D'Souza-Schorey C (1997) Genes Dev 11: 2295-2322.

Document Type

Publication order reference

Identifiers

YADDA identifier

bwmeta1.element.bwnjournal-article-abpv53p825kz
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