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2011 | 58 | 1 | 125-130
Article title

Is MLC phosphorylation essential for the recovery from ROCK inhibition in glioma C6 cells?

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Abstracts
EN
Inhibition of Rho-associated protein kinase (ROCK) activity in glioma C6 cells induces changes in actin cytoskeleton organization and cell morphology similar to those observed in other types of cells with inhibited RhoA/ROCK signaling pathway. We show that phosphorylation of myosin light chains (MLC) induced by P2Y2 receptor stimulation in cells with blocked ROCK correlates in time with actin cytoskeleton reorganization, F-actin redistribution and stress fibers assembly followed by recovery of normal cell morphology. Presented results indicate that myosin light-chain kinase (MLCK) is responsible for the observed phosphorylation of MLC. We also found that the changes induced by P2Y2 stimulation in actin cytoskeleton dynamics and morphology of cells with inhibited ROCK, but not in the level of phosphorylated MLC, depend on the presence of calcium in the cell environment.
Publisher

Year
Volume
58
Issue
1
Pages
125-130
Physical description
Dates
published
2011
received
2010-11-16
revised
2010-12-09
accepted
2010-12-10
(unknown)
2011-03-07
Contributors
  • Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warszawa, Poland
  • Medical University of Lodz, Łódź, Poland
  • Centro de Investigación del Cáncer, CSIC-University of Salamanca, Salamanca, Spain
author
  • Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warszawa, Poland
author
  • Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warszawa, Poland
  • Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warszawa, Poland
  • Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warszawa, Poland
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv58i1p125kz
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