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Zachowania wyborcze w wyborach parlamentarnych i prezydenckich w Polsce w latach 2005-2007 - wzory przestrzennych zroznicowan

100%

Krzeminski P.

Przegląd Geograficzny. Polska Akademia Nauk

2009

tom 81

nr 2

259-281

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

100%

Krzeminski P.

2005

tom 52

nr 4

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.

Calcium response induced by stimulation of P2Y nucleotide receptors n long-term serum-deprived glioma C6 cells

51%

Suplat D. , Krzeminski P. , Pomorski P. , Baranska J.

2006

tom 53

nr Supplement 1

Cofilin-like protein influences the motility of Amoeba proteus

44%

Klopocka W. , Wierzbicka K. , Pomorski P. , Krzeminski P. , Wasik A.

Acta Protozoologica

2006

tom 45

nr 4

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

38%

Korczynski J. , Sobierajska K. , Krzeminski P. , Wasik A. , Wypych D. , Pomorski P. , Klopocka W.

tom 58

nr 1

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.