Ouabain is a reversible inhibitor of myogenic fusion

Pauw, Peter G.; Hermann, Greg J.

doi:10.1007/bf02631408

Cited by 5 publications

(4 citation statements)

References 15 publications

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“…This process absolutely requires influx of Ca'+ [3] and accompanies various cellular events, such as redistribution of membrane nroteins and reorganization of cytoskeletons [4,5]. A number of reports have suggested that protein breakdown plays an important role in mediating myoblast fusion .…”

Section: Introductionmentioning

confidence: 99%

“…A prominent event in myogenesis is the membrane fusion of mononucleated myoblasts to multinucleated myotubes [1,2]. This process absolutely requires influx of Ca'+ [3] and accompanies various cellular events, such as redistribution of membrane nroteins and reorganization of cytoskeletons [4,5]. A number of reports have suggested that protein breakdown plays an important role in mediating myoblast fusion [6-91. It has been shown that Ca'+-activated thiol-protease requiring mtllimolar Ca" (m-calpain: henceforth referred to as calpain) is relocalized from cytosol to membrane during the fusion [7,8].…”

Section: Introductionmentioning

confidence: 99%

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Cell‐penetrating inhibitors of calpain block both membrane fusion and filamin cleavage in chick embryonic myoblasts

et al. 1993

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Benzyloxycarbonyl(Z)-Leu-nLeu-H(calpeptin) and Z-Leu-Met-H, cell-penetrating mhtbitors of calpain. were found to block myoblast fusion without any effect on cell proliferation and alignment along then bipolar axts. They also inhibited the accumulation of creatine kinase during myogenesis. These effects were dose-dependent, and could be reversed upon removal of the drug from the culture medium. Furthermore, treatment of the inhibitors prevented the hydrolysis of filamm, which is sensitive to cleavage by calpam m vitro and interferes with actin-myosin filament formation by cross-linking F-actin molecules. On the other hand. leupeptm, which can also mhtbtt calpain m vitro but can not penetrate into cells, showed little or no effect on both myoblast fusion and filamin cleavage. These results suggest that calpam may play an important role m cytoskeletal reorganization that is requisite for myoblast fuston. The role of calpam on the expression of muscle-spectfic proteins remams unknown Calpain: Ftlamin. Calpeptin. Myoblast fusion

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Cell‐penetrating inhibitors of calpain block both membrane fusion and filamin cleavage in chick embryonic myoblasts

et al. 1993

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“…5d ). Similarly, in rodent L6 or C2 myoblasts, ouabain (> 300 μM) hampers myogenesis [ 23 ]. The striking difference in the concentration to achieve this effect between species is possibly due to existence of the ouabain-resistant α1 isoform in rodents [ 34 ].…”

Section: Resultsmentioning

confidence: 99%

“…Although the effect of cardiotonic steroids in chick skeletal myogenesis is unknown, previous studies demonstrated that addition of high concentrations (300–400 μM) of ouabain to L6 or C2 myoblast cell line produced nearly complete inhibition of myoblast fusion, and removal of ouabain allowed complete fusion to occur [ 23 ]. Nevertheless, an overall reduction rate of protein synthesis was considered to be a consequence of ouabain-induced dissipation of Na + and K + gradients and low rates of cell fusion, i.e., a nonspecific role of Na + /K + -ATPase in the phenomenon [ 20 ].…”

Section: Introductionmentioning

confidence: 99%

The Role of Na+/K+-ATPase during Chick Skeletal Myogenesis

et al. 2015

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The formation of a vertebrate skeletal muscle fiber involves a series of sequential and interdependent events that occurs during embryogenesis. One of these events is myoblast fusion which has been widely studied, yet not completely understood. It was previously shown that during myoblast fusion there is an increase in the expression of Na+/K+-ATPase. This fact prompted us to search for a role of the enzyme during chick in vitro skeletal myogenesis. Chick myogenic cells were treated with the Na+/K+-ATPase inhibitor ouabain in four different concentrations (0.01-10 μM) and analyzed. Our results show that 0.01, 0.1 and 1 μM ouabain did not induce changes in cell viability, whereas 10 μM induced a 45% decrease. We also observed a reduction in the number and thickness of multinucleated myotubes and a decrease in the number of myoblasts after 10 μM ouabain treatment. We tested the involvement of MEK-ERK and p38 signaling pathways in the ouabain-induced effects during myogenesis, since both pathways have been associated with Na+/K+-ATPase. The MEK-ERK inhibitor U0126 alone did not alter cell viability and did not change ouabain effect. The p38 inhibitor SB202190 alone or together with 10 μM ouabain did not alter cell viability. Our results show that the 10 μM ouabain effects in myofiber formation do not involve the MEK-ERK or the p38 signaling pathways, and therefore are probably related to the pump activity function of the Na+/K+-ATPase.

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Involvement of gap junctional communication in myogenesis

Constantin

Cronier

2000

International Review of Cytology

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Ouabain is a reversible inhibitor of myogenic fusion

Cited by 5 publications

References 15 publications

Cell‐penetrating inhibitors of calpain block both membrane fusion and filamin cleavage in chick embryonic myoblasts

Cell‐penetrating inhibitors of calpain block both membrane fusion and filamin cleavage in chick embryonic myoblasts

The Role of Na+/K+-ATPase during Chick Skeletal Myogenesis

Involvement of gap junctional communication in myogenesis

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