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1

The effects of the interaction of myosin essential light chain isoforms with actin in skeletal muscles

100%
Nieznanska H., Nieznanski K., Stepkowski D.
Acta Biochimica Polonica
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2002
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tom 49
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nr 3
In order to compare the ability of different isoforms of myosin essential light chain to interact with actin, the effect of the latter protein on the proteolytic susceptibility of myosin light chains (MLC-1S and MLC-1V — slow specific and same as ventricular isoform) from slow skeletal muscle was examined. Actin protects both slow muscle es­sential light chain isoforms from papain digestion, similarly as observed for fast skel­etal muscle myosin (Nieznańska et al., 1998, Biochim. Biophys. Acta 1383: 71). The ef­fect of actin decreases as ionic strength rises above physiological values for both fast and slow skeletal myosin, confirming the ionic character of the actin-essential light chain interaction. To better understand the role of this interaction, we examined the effect of synthetic peptides spanning the 10-amino-acid N-terminal sequences of myo­sin light chain 1 from fast skeletal muscle (MLC-1F) (MLCFpep: KKDVKKPAAA), MLC-1S (MLCSpep: KKDVPVKKPA) and MLC-1V (MLCVpep: KPEPKKDDAK) on the myofibrillar ATPase of fast and slow skeletal muscle. In the presence of MLCFpep, we observed an about 19% increase, and in the presence of MLCSpep about 36% increase, in the myofibrillar ATPase activity of fast muscle. On the other hand, in myofibrillar preparations from slow skeletal muscle, MLCSpep as well as MLCVpep caused a lowering of the ATPase activity by about 36%. The above results suggest that MLCSpep induces opposite effects on ATPase activity, depending on the type of myofibrils, but not through its specific N-terminal sequence — which differs from other MLC N-terminal peptides. Our observations lead to the conclusion that the action of different isoforms of long essential light chain is similar in slow and fast skeletal muscle. However the interaction of essential light chains with actin leads to different physiological effects probably depending on the isoforms of other myofibrillar proteins.
2

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

84%
Korczynski J., Sobierajska K., Krzeminski P., Wasik A., Wypych D., Pomorski P., Klopocka W.
Acta Biochimica Polonica
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2011
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tom 58
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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.
3

Reconstitution of ventricular myosin with atrial light chains 1 improves its functional properties

84%
Khalina Y. N., Bartsch H., Petzhold D., Haase H., Podlubnaya Z. A., Shpagina M. D., Morano I.
Acta Biochimica Polonica
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2005
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tom 52
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nr 2
Atrial light chain 1 (ALC-1) is expressed in embryonic and hypertrophied human ventricles but not in normal adult human ventricles. We investigated the effects of recombinant human atrial light chains (hALC-1) on the structure and enzymatic activity of synthetic filaments of ventricular myosin. The endogenous ventricular myosin light chain 1 (VLC-1) was partially replaced by recombinant hALC-1 yielding hALC-1 levels of 12%, 24% and 42%. This reconstitution of ventricular myosin with hALC-1 did not change the length of synthetic myosin filaments but led to more rounded myosin heads in comparison with those of control filaments. Actin-activated ATPase activity of myosin, a parameter of functional activity of molecular motor, amounted to 79.5 nmol Pi/mg per min in control myosin filaments. Reconstitution with hALC-1 caused a profound increase of the actin-activated myosin ATPase activity in a dose dependent manner, for example, synthetic myosin filaments formed with 12%, 24% and 42% hALC-1 reconstituted myosin revealed the actin-activated ATPase activity increased by 18%, 26% and 36%, respectively, as compared to control. These results strongly suggest that in vivo expression of ALC-1 enhances ventricular myosin function, thereby contributing to cardiac compensation.
4

Differentiation of pork and beef from meat mixtures and processed products on the basis of skeletal muscle myosin light chain isoforms

67%
Montowska M., Pospiech E.
Polish Journal of Food and Nutrition Sciences
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2011
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tom 61
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nr Suppl.1
5
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Alteration in expressions of RhoA and Rho-kinases during pregnancy in rats: their roles in uterine contractions and onset of labour

67%
Domokos D., Ducza E., Falkay G., Gaspar R.
Journal of Physiology and Pharmacology
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2017
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tom 68
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nr 3
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