1,25-Dihydroxy vitamin D3 Affects the Synthesis, Phosphorylation and in vitro Calmodulin Binding of Myoblast Cytoskeletal Proteins

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Abstract

Incubation of chick embryo myoblasts with 1.25-dihydroxyvitamin [1,25(OH):DJ D310–10M, 24 h), markedly stimulated the incorporation of [3H]leucine into total cytoskeletal proteins and this effect was abolished when the sterol treatment was performed in the presence of cycloheximide or actinomycin D. l,25(OH)2D3selectively stimulated the de novo synthesis of several proteins with apparent molecular massesisoelectric points) of 220 kDa6.1 and 9.7), 150 kDa7.5), 110 kDa7.2), 68 kDa9.5, 7.5 and 4.5), 50 kDa8.5), 44 kDa6.3), 27 kDa7.8) and 15 kDa5.5). Labelling of proteins with [l125]calmodulin after their separation on SDS-polyacrylamide gels showed that 1,25(OH)2D3-dependent protein of 110 kDa is the major calmodulin-binding component of myoblasts cytoskeleton. In addition, the sterol increased the phosphorylation of several cytoskeletal proteins including that of 110 and 15 kDa whose synthesis potentiates. © 1990, Verlag der Zeitschrift für Naturforschung. All rights reserved.

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Brunner, A., & de Boland, A. R. (1990). 1,25-Dihydroxy vitamin D3 Affects the Synthesis, Phosphorylation and in vitro Calmodulin Binding of Myoblast Cytoskeletal Proteins. Zeitschrift Fur Naturforschung - Section C Journal of Biosciences, 45(11–12), 1156–1160. https://doi.org/10.1515/znc-1990-11-1212

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