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Myosin-activating protein kinases are possible regulators of nonmuscle myosin in developing human heart

  • Biophysics and biochemistry
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Bulletin of Experimental Biology and Medicine Aims and scope

We studied the localization of myosin-activating protein kinases in cardiomyocytes obtained from fetal human heart at 8–9 weeks gestation. It was found that at this developmental stage, smooth muscle/nonmuscle myosin light chain kinase (MLCK, 108 kDa) and its high-molecular weight isoform (MLCK, 210 kDa), skeletal MLCK and death-associated protein kinase (DAPK) are co-localized with nonmuscle myosin IIB in the premyofibrils. The data obtained suggest that cardiac nonmuscle myosin at 8–9 weeks gestation may serve as the substrate of the studied myosin-activating protein kinases that are likely to cooperatively regulate the formation of myofibrils. We revealed high-molecular weight isoform of smooth muscle/nonmuscle kinase MLCK-210 in developing human heart and determined the ratios of MLCK-108 and MLCK-210 at different gestational stages. In this case, the approximate time period of changes in these isoforms ratio was revealed (between 8–9 and 13 weeks), that can be associated with functional changes in the developing myocardium.

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Correspondence to O. V. Stepanova.

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Translated from Byulleten’ Eksperimental’noi Biologii i Meditsiny, Vol. 152, No. 8, pp. 158–161, August, 2011.

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Stepanova, O.V., Chadin, A.V., Masyutin, A.G. et al. Myosin-activating protein kinases are possible regulators of nonmuscle myosin in developing human heart. Bull Exp Biol Med 152, 198–201 (2011). https://doi.org/10.1007/s10517-011-1487-5

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  • DOI: https://doi.org/10.1007/s10517-011-1487-5

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